Modified immune cells with increased resistance to allorejection

Abstract

The present disclosure features allogeneic modified cells (e.g., T- or NK-cells) having increased persistence, increased resistance to immune rejection, and / or decreased risk of eliciting a host-versus-graft reaction, or a combination thereof. Methods for producing and using the same are also provided.

Description

[0001]ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 MODIFIED IMMUNE CELLS WITH INCREASED RESISTANCE TO ALLOREJECTION CROSS REFERENCE TO RELATED APPLICATIONS The present application claims priority to U.S. Provisional Applications No. 63 / 726,729 filed December 2, 2024, 63 / 682,578, filed August 13, 2024, and 63 / 618,520, filed January 8, 2024, the entire contents of which are hereby incorporated by reference in their entirety. SEQUENCE LISTING This application contains a Sequence Listing which has been submitted electronically in XML format and is hereby incorporated by reference in its entirety. The Sequence Listing XML file, created on December 30, 2024, is named 180802-056504PCT_SL.xml, and is 1,183,483 bytes in size. BACKGROUND Autologous and allogeneic immunotherapies are treatment approaches in which cells are administered to a subject. Autologous and allogeneic immunotherapies can be used to treat any of a variety of diseases including autoimmune diseases, graft-versus host disease (GVHD), and the like. For example, some diseases can be treated by administering to a subject in need thereof autologous or allogeneic immune effector cells capable of targeting and killing or inhibiting activity of disease-associated cells (e.g., neoplasia cells or autoantibody-producing cells) in a subject. Allogeneic cells (e.g., cells that are not recognized by a host’s immune system as other) may also be useful for organ and tissue replacement and repair. In some instances, autologous or allogeneic immunotherapies can be used to treat a disease (e.g., a cancer or autoimmune disease) by administering to a subject an immune effector cell modified to express a chimeric antigen receptor. To generate an immune cell that expresses a chimeric antigen receptor (CAR), the immune cell is first collected from the subject (autologous) or a donor separate from the subject receiving treatment (allogeneic) and genetically modified to express the chimeric antigen receptor. The resulting cell expresses the chimeric antigen receptor on its cell surface (e.g., CAR-T cell), and upon administration to the subject, the chimeric antigen receptor binds to a marker expressed by the neoplastic ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 cell. This interaction with the marker activates the CAR-T cell, which then kills the neoplastic cell. Autologous CAR-T cells have transformed the treatment paradigm for patients with hematological malignancies. Yet, the production of these CAR-T cells is lengthy, expensive and there is an inherent risk of manufacturing failure due to poor T cell fitness that may result from advanced disease and prior lines of therapy. Thus, CAR-T cells derived from healthy allogeneic donors is an attractive solution that could reduce patient wait-time to treatment and cost by standardizing a scalable manufacturing process. However, HLA mismatch between an allogeneic donor and recipient patient challenges the clinical feasibility of allogeneic CAR-T cells. For example, disruption of the endogenous T cell receptor in allogeneic T cells prevents life-threatening graft-vs-host disease, but retention of non-self HLA polypeptides renders these cells vulnerable to immunologic rejection by the recipient, which may serve to limit their in vivo persistence. The elimination of surface HLA class-I and HLA class-II expression by inactivating beta-2-microglobulin (β2M) and HLA class-II transcriptional activator (CIITA), respectively, renders allogeneic CAR-T cells invisible to HLA-mismatched T cells. However, the absence of HLA class-I triggers missing-self recognition and lysis by natural killer (NK) cells (10). Thus, there is a significant need for techniques to reduce susceptibility of allogeneic immune effector cells and other modified immune cells to lysis by immune effector cells of an allogeneic subject (e.g., alloreactive T cells or natural killer cells). SUMMARY The present disclosure features allogeneic modified cells (e.g., T- or NK-cells) having increased persistence, increased resistance to immune rejection, or decreased risk of eliciting a host-versus-graft reaction, or a combination thereof. Methods and compositions for producing and using the same are also provided. In embodiments, the methods for preparing the modified cells leverage base editing. Among other things, the present disclosure shows that allogeneic cells can be modified to be resistant to immune rejection. The present disclosure also features allogeneic modified immune cells (e.g., T- or NK-cells) having increased persistence, increased resistance to immune rejection, and / or decreased risk of eliciting a host-versus-graft reaction, and methods of producing and using such cells, for example, in the treatment of neoplasia or autoimmune diseases without the disadvantages of ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 autologous cell therapies such as long manufacturing times, or the need for an adequate supply of sufficiently healthy autologous donor cells. In one aspect, the disclosure features a fusion polypeptide containing a cognate peptide (cPep), a human leukocyte antigen E (HLA-E) polypeptide, or a fragment thereof, and a beta-2-microglobulin (B2M) polypeptide, or a fragment thereof. The cPep contains an amino acid sequence selected from one or more of: VMAPRTLFL (SEQ ID NO: 605); NMPARTVLF (SEQ ID NO: 444);VMAPRTLLL (SEQ ID NO: 434);VMAPRTLVL (SEQ ID NO: 435); VMAPRTLIL (SEQ ID NO: 436);VMAPRALLL (SEQ ID NO: 437);VTAPRTVLL (SEQ ID NO: 438); VMAPRTVLL (SEQ ID NO: 439); VTAPRTLLL (SEQ ID NO: 440); SAPLKTRFL (SEQ ID NO: 441);TGPWRSLWI (SEQ ID NO: 442); and TAPARTMFL (SEQ ID NO: 443). In another aspect, the disclosure features a fusion polypeptide containing an amino acid sequence with at least 85% sequence identity to a sequence selected from one or more of: BTx_CM525 MSRSVALAVLALLSLSGLEANMPARTVLFGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 490); BTx_CM499 MSRSVALAVLALLSLSGLEAVMAPRTLLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 469); BTx_CM500 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 MSRSVALAVLALLSLSGLEAVMAPRTLVLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 470); BTx_CM501 MSRSVALAVLALLSLSGLEAVMAPRTLILGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 471); BTx_CM502 MSRSVALAVLALLSLSGLEAVMAPRALLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 472); BTx_CM503 MSRSVALAVLALLSLSGLEAVTAPRTVLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 473); BTx_CM504 MSRSVALAVLALLSLSGLEAVMAPRTVLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 474); BTx_CM505 MSRSVALAVLALLSLSGLEAVTAPRTLLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 475); BTx_CM507 MSRSVALAVLALLSLSGLEASAPLKTRFLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 476); BTx_CM508 MSRSVALAVLALLSLSGLEATGPWRSLWIGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 477); BTx_CM509 MSRSVALAVLALLSLSGLEATAPARTMFLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 478); BTx_CM510 MSRSVALAVLALLSLSGLEANMPARTVLFGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 479); BTx_CM514 MSRSVALAVLALLSLSGLEAVMAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 480); BTx_CM515 MSRSVALAVLALLSLSGLEAVMAPRTLVLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 481); BTx_CM516 MSRSVALAVLALLSLSGLEAVMAPRTLILGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 482); BTx_CM517 MSRSVALAVLALLSLSGLEAVMAPRALLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 483); BTx_CM518 MSRSVALAVLALLSLSGLEAVTAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 484); BTx_CM519 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 MSRSVALAVLALLSLSGLEAVMAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 485); BTx_CM520 MSRSVALAVLALLSLSGLEAVTAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 486); BTx_CM522 MSRSVALAVLALLSLSGLEASAPLKTRFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 487); BTx_CM523 MSRSVALAVLALLSLSGLEATGPWRSLWIGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 488); BTx_CM524 MSRSVALAVLALLSLSGLEATAPARTMFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 489); MSRSVALAVLALLSLSGLEAVMAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 606); MSRSVALAVLALLSLSGLEAVMAPRTLVLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 607); MSRSVALAVLALLSLSGLEAVMAPRTLILGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 608); MSRSVALAVLALLSLSGLEAVMAPRALLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 609); MSRSVALAVLALLSLSGLEAVTAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 610); MSRSVALAVLALLSLSGLEAVMAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 611); MSRSVALAVLALLSLSGLEAVTAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 612); ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 MSRSVALAVLALLSLSGLEASAPLKTRFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 613); MSRSVALAVLALLSLSGLEATGPWRSLWIGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 614); MSRSVALAVLALLSLSGLEATAPARTMFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 615); MSRSVALAVLALLSLSGLEANMPARTVLFGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 616); and MSRSVALAVLALLSLSGLEAVMAPRTLFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 617). In another aspect, the disclosure features a polynucleotide encoding the fusion polypeptide of any aspect or embodiment of the disclosure. In another aspect, the disclosure features a polynucleotide encoding the fusion polypeptide of any aspect or embodiment of the disclosure, and containing a nucleotide sequence having at least 85% sequence identity to a sequence selected from one or more of: BTx_CM525 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAA TATGCCCGCTCGGACAGTATTGTTTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 512); BTx_CM499 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCCCCCAGGACTTTGCTTCTCGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 491); BTx_CM500 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT AATGGCCCCTCGAACCCTGGTACTCGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 492); BTx_CM501 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCTCCGCGAACTCTGATCCTCGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 493); BTx_CM502 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCGCCTCGAGCCCTGCTCCTTGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 494); ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 BTx_CM503 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT TACCGCTCCTAGAACAGTCCTGCTGGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 495); BTx_CM504 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCACCGAGGACCGTACTCCTCGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 496); BTx_CM505 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT TACCGCGCCCCGGACTCTCCTTTTGGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 497); BTx_CM507 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCTC CGCCCCTCTGAAGACCCGATTTTTGGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 498); BTx_CM508 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAC CGGGCCTTGGCGGTCCCTCTGGATTGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 499); BTx_CM509 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAC TGCTCCGGCCAGGACCATGTTCCTTGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 500); BTx_CM510 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAA TATGCCCGCTCGGACAGTATTGTTTGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 501); BTx_CM514 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCCCCCAGGACTTTGCTTCTCGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 502); BTx_CM515 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT AATGGCCCCTCGAACCCTGGTACTCGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 503); BTx_CM516 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCTCCGCGAACTCTGATCCTCGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 504); BTx_CM517 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCGCCTCGAGCCCTGCTCCTTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 505); BTx_CM518 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT TACCGCTCCTAGAACAGTCCTGCTGGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 506); BTx_CM519 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCACCGAGGACCGTACTCCTCGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 507); BTx_CM520 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT TACCGCGCCCCGGACTCTCCTTTTGGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 508); BTx_CM522 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCTC CGCCCCTCTGAAGACCCGATTTTTGGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 509); BTx_CM523 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAC CGGGCCTTGGCGGTCCCTCTGGATTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGCTGATAGT AA (SEQ ID NO: 510); BTx_CM524 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAC TGCTCCGGCCAGGACCATGTTCCTTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 511). In another aspect, the disclosure features a vector containing the polynucleotide of any aspect or embodiment of the disclosure. In another aspect, the disclosure features an allogeneic modified immune cell containing the fusion polypeptide, the polynucleotide, or the vector of any aspect or embodiment of the disclosure. In another aspect, the disclosure features a pharmaceutical composition containing the fusion polypeptide, the polynucleotide, the vector -35, or the cell of any aspect or embodiment of the disclosure, and a pharmaceutically acceptable excipient. In another aspect, the disclosure features a method for preparing a modified immune cell. The method involves a) modifying an immune cell to knock-out expression of an endogenous beta-2-microglobulin (B2M) polypeptide in the cell. The method further involves b) contacting the cell with a polynucleotide encoding the fusion polypeptide of any aspect or embodiment of the disclosure. In another aspect, the disclosure features a cell produced by the method of any aspect or embodiment of the disclosure. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 In another aspect, the disclosure features a method for treating a subject having a neoplasia or an autoimmune disease. The method involves administering to the subject the polynucleotide, vector, pharmaceutical composition, and / or cell of any aspect or embodiment of the disclosure. Without intending to be bound by theory, in any aspect or embodiment of the disclosure, an a fusion polypeptide of any aspect or embodiment of the disclosure inhibits NK cells via engaging and / or binding an NKG2A / CD94 heterodimer. In any aspect or embodiment of the disclosure, the method further involves assessing NKG2A expression in natural killer cells (NK cells) from the subject prior to administration of an agent to the subject (e.g., a polynucleotide, vector, pharmaceutical composition, and / or cell of any aspect or embodiment of the disclosure). In any aspect or embodiment of the disclosure, the polynucleotide, vector, pharmaceutical composition, and / or cell or any aspect or embodiment of the disclosure is administered to the subject only if at least about 50%, 60%, 70%, 80%, 90%, or 95% of NK cells from the subject are or are determined to be NKG2A+. In any aspect or embodiment of the disclosure, the polynucleotide, vector, pharmaceutical composition, and / or cell is administered to the subject if at least 70% of the NK cells from the subject are or are determined to be NKG2A+. In any aspect or embodiment of the disclosure, the method further involves determining the ratio of NKG2A expression to KIR expression in NK cells from the subject prior to of an agent to the subject (e.g., a polynucleotide, vector, pharmaceutical composition, and / or cell of any aspect or embodiment of the disclosure). In any aspect or embodiment of the disclosure, the polynucleotide, vector, pharmaceutical composition, and / or cell of any aspect or embodiment of the disclosure is administered to the subject only if the ratio of NKG2A expression to KIR expression in NK cells from the subject is determined to be at least 1:2, 1:1, 1.5:1.2:1, 2.5:1, 3:1, 4:1, 5:1, 7.5:1, 9:1, 10:1, 25:1, or greater. In any aspect or embodiment of the disclosure, NK cell in a subject are first to recover after a lymphodepleting chemotherapy, and early repopulating NK cells are predominately immature and approximately 90% are NKG2A+. In any aspect or embodiment of the disclosure, the subject has been administered a lymphodepleting agent (e.g., cyclophosphamide, fludarabine, anti-thymocyte globulin, or a combination thereof) (e.g., as part of a lymphodepleting chemotherapy) prior to being administered the polynucleotide, vector, pharmaceutical composition, and / or cell. In any aspect or embodiment of the disclosure, administering the polynucleotide, vector, pharmaceutical composition, and / or cell of any aspect or embodiment of the disclosure to the subject is initiated after administration of a lymphodepleting agent to the subject (e.g., as part of a lymphodepleting therapy) and ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 prior to leukocyte recovery following said administration of the lymphodepleting agent. In any aspect or embodiment of the disclosure, the polynucleotide, vector, pharmaceutical composition, and / or cell of any aspect or embodiment of the disclosure is administered to the subject following leukocyte recovery (e.g., within 1-4 days of or immediately after) subsequent to administration of a lymphodepleting agent to the subject (e.g., as part of a lymphodepleting chemotherapy). In any aspect or embodiment of the disclosure, the polynucleotide, vector, pharmaceutical composition, and / or cell of any aspect or embodiment of the disclosure is administered to the subject shortly after or immediately following (e.g., within 1-4 days) administration of a lymphodepleting agent to the subject (e.g., as part of a lymphodepleting chemotherapy). In any aspect or embodiment of the disclosure, the subject is administered an agent of any aspect or embodiment of the disclosure (e.g., a polynucleotide, vector, pharmaceutical composition, and / or cell of any aspect or embodiment of the disclosure) less than 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 8 days, 9 days, 10 days, 11 day, 12 days, 13 days, 14 days, 15 days, 20 days, 25 days, 30 days, 40 days, or 50 days following administration of a lymphodepleting agent to the subject (e.g., a lymphodepleting agent administered as part of a lymphodepleting chemotherapy). In another aspect, the disclosure provides a kit for use in the method of aspect of the disclosure, or embodiments thereof. The kit contains the fusion polypeptide, polynucleotide, vector, pharmaceutical composition, and / or cell of any aspect or embodiment of the disclosure. In any aspect or embodiment of the disclosure, the fusion polypeptide contains from N-terminus to C-terminus: a) the cPep, the B2M polypeptide or fragment thereof, and the HLA-E polypeptide or fragment thereof; b) the cPep, the HLA-E polypeptide or fragment thereof, and the B2M polypeptide or functional fragment thereof; c) the B2M polypeptide or fragment thereof, the cPep, and the HLA-E polypeptide or fragment thereof; or d) the HLA-E polypeptide or fragment thereof, the cPep, the B2M polypeptide or fragment thereof. In any aspect or embodiment of the disclosure, the fusion polypeptide further contains an N-terminal signal peptide. In any aspect or embodiment of the disclosure, the signal peptide is a B2M signal peptide. In any aspect or embodiment of the disclosure, the signal peptide contains the amino acid sequenceMSRSVALAVLALLSLSGLEA (SEQ ID NO: 428). In any aspect or embodiment of the disclosure, the fusion polypeptide contains one or more linkers. In any aspect or embodiment of the disclosure, the one or more linkers contains the amino acid sequence (GGGGS)n(SEQ ID NO: 247), or the amino acid sequence (GGGGS)n ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 (SEQ ID NO: 247) modified to include a cytidine amino acid. In any aspect or embodiment of the disclosure, n is between 1 and 5. In any aspect or embodiment of the disclosure, the linker contains an amino acid sequence selected from one or more of:GGGGSGGGGSGGGGS (SEQ ID NO: 460); GCGGSGGGGSGGGGS (SEQ ID NO: 461); and GGGGSGGGGSGGGGSGGGGSG (SEQ ID NO: 464). In any aspect or embodiment of the disclosure, the fusion polypeptide contains a linker connecting the cPep to the B2M polypeptide, or the fragment thereof. In any aspect or embodiment of the disclosure, the linker connecting the cPep to the B2M polypeptide, or the fragment thereof, contains a cytidine amino acid, and where the HLA-E polypeptide, or the fragment thereof, contains a cytidine amino acid capable of forming a disulfide bridge with the cytidine amino acid in the linker connecting the cPep to the B2M polypeptide. In any aspect or embodiment of the disclosure, the formation of the disulfide bridge mediates stable binding of the cPep by a binding groove of the HLA-E polypeptide, or the fragment thereof. In any aspect or embodiment of the disclosure, the linker connecting the cPep to the B2M polypeptide contains the amino acid sequence GCGGSGGGGSGGGGS (SEQ ID NO: 461) and the HLA-E polypeptide contains the amino acid sequence SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGCYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 457), or a functional fragment thereof. In any aspect or embodiment of the disclosure, the fusion polypeptide contains a linker connecting the B2M polypeptide, or the fragment thereof, to the HLA-E polypeptide, or the fragment thereof. In any aspect or embodiment of the disclosure, the linker connecting the B2M polypeptide, or the fragment thereof, to the HLA-E polypeptide, or the fragment thereof, contains the amino acid sequenceGGGGSGGGGSGGGGSGGGGSG (SEQ ID NO: 464), or a fragment thereof. In any aspect or embodiment of the disclosure, the HLA-E polypeptide, or fragment thereof, contains an amino acid sequence having at least 85% sequence identity to one of the following sequences, or a fragment thereof: SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 456); SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGCYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 457); and SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGCYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 618). In any aspect or embodiment of the disclosure, the B2M polypeptide, or fragment thereof, contains an amino acid sequence having at least 85% sequence identity to the following sequence, or a fragment thereof: IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSF YLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM (SEQ ID NO: 427). In any aspect or embodiment of the disclosure, the HLA-E polypeptide lacks a transmembrane domain. In any aspect or embodiment of the disclosure, the fusion polypeptide further contains a transmembrane domain N-terminal to the HLA-E polypeptide, or the fragment thereof. In any aspect or embodiment of the disclosure, the fusion polypeptide further contains a transmembrane domain C-terminal to the HLA-E polypeptide, or the fragment thereof. In any aspect or embodiment of the disclosure, the transmembrane domain contains a cluster of differentiation 4 (CD4) transmembrane (CD4TM) domain, an HLA-E*01:03 transmembrane domain, or a CD8a transmembrane domain. In any aspect or embodiment of the disclosure, the CD4TM domain contains the following sequence with up to 4 total amino acid alterations:MALIVLGGVAGLLLFIGLGIFF (SEQ ID NO: 433). In any aspect or embodiment of the disclosure, the CD4TM is fused at the C-terminus to a peptide containing the following amino acid sequence:CVRC (SEQ ID NO: 466). In any aspect or embodiment of the disclosure, the amino acid sequence has at least 95% sequence identity to the sequence. In any aspect or embodiment of the disclosure, the amino acid sequence contains or contains only the sequence. In any aspect or embodiment of ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 the disclosure, the amino acid sequence has at least 95% sequence identity to one or more of the following sequences: BTx_CM525 MSRSVALAVLALLSLSGLEANMPARTVLFGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 490); MSRSVALAVLALLSLSGLEAVMAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 606); MSRSVALAVLALLSLSGLEAVMAPRTLVLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 607); MSRSVALAVLALLSLSGLEAVMAPRTLILGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 608); MSRSVALAVLALLSLSGLEAVMAPRALLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 609); MSRSVALAVLALLSLSGLEAVTAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 610); MSRSVALAVLALLSLSGLEAVMAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 611); MSRSVALAVLALLSLSGLEAVTAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 612); and ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 MSRSVALAVLALLSLSGLEAVMAPRTLFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 617). In any aspect or embodiment of the disclosure, the nucleotide sequence has at least 95% sequence identity to the sequence. In any aspect or embodiment of the disclosure, the nucleotide sequence contains or contains only the sequence. In any aspect or embodiment of the disclosure, the nucleotide sequence has at least 95% sequence identity to the following sequence: BTx_CM525 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAA TATGCCCGCTCGGACAGTATTGTTTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 512). In any aspect or embodiment of the disclosure, the vector is a viral vector or a transposon. In any aspect or embodiment of the disclosure, the viral vector is a lentiviral vector. In any aspect or embodiment of the disclosure, the cell contains nucleobase alterations resulting in reduced expression of a functional B2M polypeptide and / or a functional cluster of differentiation 58 (CD58) polypeptide relative to an unmodified immune cell. In any aspect or embodiment of the disclosure, the cell has reduced expression levels of both the B2M and CD58 polypeptides relative to the unmodified immune cell and / or contains undetectable levels of functional B2M or CD58 polypeptides. In any aspect or embodiment of the disclosure, the allogeneic modified immune cell is a T cell or a macrophage cell. In any aspect or embodiment of the disclosure, the allogeneic modified immune cell expresses a chimeric antigen receptor (CAR). In any aspect or embodiment of the disclosure, the modified immune cell shows reduced lysis by a natural killer cell relative to an allogeneic immune cell that does not express the fusion polypeptide and / or that express a CD58 polypeptide. In any aspect or embodiment of the disclosure, lysis by the natural killer cell is reduced by at least 15%, 25%, 50%, or 75%. In any aspect or embodiment of the disclosure, the method further involves modifying the immune cell to knock-out expression of an endogenous cluster of differentiation 58 (CD58) polypeptide. In any aspect or embodiment of the disclosure, modifying the cell to knock-out expression of the B2M polypeptide and / or CD58 polypeptide is carried out using base editing. In any aspect or embodiment of the disclosure, the base editing involves contacting the cell with a base editor and: i) a guide polynucleotide targeting the base editor to effect an alteration of a nucleobase of an endogenous B2M gene in the cell, thereby knocking out expression of the endogenous B2M polypeptide in the cell; and / or ii) a guide polynucleotide targeting the base editor to effect an alteration of a nucleobase of an endogenous CD58 gene in the cell, thereby knocking out expression of the endogenous CD58 polypeptide in the cell. In any aspect or embodiment of the disclosure, the guide polynucleotide of i) contains a spacer having the nucleotide sequence ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CUUACCCCACUUAACUAUCU (SEQ ID NO: 467), and the guide polynucleotide of ii) contains a spacer having the nucleotide sequence ACUCACCAAAGCAGUGCAGC (SEQ ID NO: 468). In any aspect or embodiment of the disclosure, the guide polynucleotides of i) and ii) each contain a scaffold having the nucleotide sequence GUUUUAGAGCUAGAAAUAGCAAGUUAAAAUAAGGCUAGUCCGUUAUCAACUUGAAAAAGUGG CACCGAGUCGGUGCUUUU (SEQ ID NO: 317). In any aspect or embodiment of the disclosure, the base editor contains a nucleic acid programmable DNA binding protein (napDNAbp) domain and an adenosine deaminase domain. The adenosine deaminase domain contains an amino acid sequence with a least 90% sequence identity to the following amino acid sequence and further contains the amino acid alterations I76Y, V82S, Y123H, Y147R, and Q145R: MSEVEFSHEYWMRHALTLAKRARDEREVPVGAVLVLNNRVIGEGWNRAIGLHDPTAHAEIMA LRQGGLVMQNYRLIDATLYVTFEPCVMCAGAMIHSRIGRVVFGVRNAKTGAAGSLMDVLHYP GMNHRVEITEGILADECAALLCYFFRMPRQVFNAQKKAQSSTD (SEQ ID NO: 1). In any aspect or embodiment of the disclosure, the base editor contains a single adenosine deaminase domain. In any aspect or embodiment of the disclosure, the napDNAbp is a Cas9 nickase. In any aspect or embodiment of the disclosure, the method further involves expressing a chimeric antigen receptor in the cell. In any aspect or embodiment of the disclosure, the chimeric antigen receptor targets an antigen expressed on the surface of a neoplastic cell. In any aspect or embodiment of the disclosure, the cell is a T cell or a macrophage cell. In any aspect or embodiment of the disclosure, the T cell is a CD4+ or CD8+ T cell. In any aspect or embodiment of the disclosure, the modified immune cell shows reduced lysis by a natural killer cell relative to an allogeneic immune cell that does not express the fusion polypeptide and / or that express a CD58 polypeptide. In any aspect or embodiment of the disclosure, lysis by the natural killer cell is reduced by at least 15%, 25%, 50%, or 75%. In any aspect or embodiment of the disclosure, the HLA-E polypeptide, or fragment thereof, contains one or more amino acid alterations that reduce binding of a CD8 coreceptor to the fusion polypeptide. In any aspect or embodiment of the disclosure, the one or more amino acid alterations are selected from one or more of D227K, T228A, and A245V referenced to the following amino acid sequence, where the N-terminal S is position 2: SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 TRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 456). In any aspect or embodiment of the disclosure, the HLA-E polypeptide further contains a Y83C amino acid alteration referenced to SEQ ID NO: 456, where the N-terminal S is position 1. In any aspect or embodiment of the disclosure, the fusion polypeptide has reduced immunogenicity relative to a fusion polypeptide comprising an HLA-E polypeptide lacking one or more of the amino acid alterations. In any aspect or embodiment of the disclosure, the fusion polypeptide further contains a polypeptide containing an amino acid sequence with at least 85% identity to one of the following amino acid sequences, where the polypeptide is C-terminal to the HLA-E polypeptide: VGIIAGLVLLGSVVSGAVVAAVIWRKKSSGGKGGSYSKAEWSDSAQGSESHSL (SEQ ID NO: 619); IYIWAPLAGTCGVLLLSLVITLYC (SEQ ID NO: 620); and MALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 621). In any aspect or embodiment of the disclosure, the vector contains a promoter. Definitions Unless defined otherwise, all technical and scientific terms used herein have the meaning commonly understood by a person skilled in the art to which this disclosure belongs. The following references provide one of skill with a general definition of many of the terms used in this disclosure: Singleton et al., Dictionary of Microbiology and Molecular Biology (2nd ed.1994); The Cambridge Dictionary of Science and Technology (Walker ed., 1988); The Glossary of Genetics, 5th Ed., R. Rieger et al. (eds.), Springer Verlag (1991); and Hale & Marham, The Harper Collins Dictionary of Biology (1991). As used herein, the following terms have the meanings ascribed to them below, unless specified otherwise. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 By “adenine” or “ 9H-Purin-6-amine” is meant a purine nucleobase with the molecular formula C H N , having the 5 5 5 structure , and corresponding to CAS No.73-24-5. By “adenosine” or “ 4-Amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5- (hydroxymethyl)oxolan-2-yl]pyrimidin-2(1H)-one” is meant an adenine molecule attached to a ribose sugar via a glycosidic bond, having the structure , and corresponding to CAS No.65-46-3. Its molecular formula is C10H13N5O4. By “adenosine deaminase” or “adenine deaminase” is meant a polypeptide or fragment thereof capable of catalyzing the hydrolytic deamination of adenine or adenosine. In some embodiments, the deaminase or deaminase domain is an adenosine deaminase catalyzing the hydrolytic deamination of adenosine to inosine or deoxy adenosine to deoxyinosine. In some embodiments, the adenosine deaminase catalyzes the hydrolytic deamination of adenine or adenosine in deoxyribonucleic acid (DNA). The adenosine deaminases (e.g., engineered adenosine deaminases, evolved adenosine deaminases) provided herein may be from any organism (e.g., eukaryotic, prokaryotic), including but not limited to algae, bacteria, fungi, plants, invertebrates (e.g., insects), and vertebrates (e.g., amphibians, mammals). In some embodiments, the adenosine deaminase is an adenosine deaminase variant with one or more alterations and is capable of deaminating both adenine and cytosine in a target polynucleotide (e.g., DNA, RNA) and may be referred to as a “dual deaminase”. Non-limiting examples of dual deaminases include those described in PCT / US22 / 22050. In some embodiments, the target polynucleotide is single or double stranded. In some embodiments, the adenosine deaminase variant is capable of deaminating both adenine and cytosine in DNA. In some embodiments, the adenosine deaminase variant is capable of deaminating both adenine and cytosine in single-stranded DNA. In some embodiments, the ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 adenosine deaminase variant is capable of deaminating both adenine and cytosine in RNA. In embodiments, the adenosine deaminase variant is selected from those described in PCT / US2020 / 018192, PCT / US2020 / 049975, PCT / US2017 / 045381, PCT / US2021 / 016827, PCT / US2022 / 073781, PCT / US24 / 34189, or PCT / US2020 / 028568, the full contents of which are each incorporated herein by reference in their entireties for all purposes. Further non- limiting examples of adenosine deaminases include those disclosed or referenced in Rufflow, et al., “Design of highly functional genome editors by modeling of the universe of CRISPR- Cas Sequences,” bioRxiv, posted April 22, 2024, doi: 10.1101 / 2024.04.22.590591, the disclosure of which is incorporated herein by reference in its entirety for all purposes, which were designed using artificial intelligence. Further exemplary adenosine deaminase amino acid sequenes include: TadA-8e (SEQ ID NO: 517), Tad1 (SEQ ID NO: 518), Tad2 (SEQ ID NO: 519), Tad3 (SEQ ID NO: 520), Tad4 (SEQ ID NO: 521), Tad6 (SEQ ID NO: 522), Tad6-SR (SEQ ID NO: 523), TadA9 (SEQ ID NO: 524), TadA20 (SEQ ID NO: 525), Staphylococcus aureus TadA (SEQ ID NO: 526), Bacillus subtilis TadA (SEQ ID NO: 527), Salmonella typhimurium TadA (SEQ ID NO: 528), Shewanella putrefaciens (SEQ ID NO: 529), Haemophilus influenzae F3031 TadA (SEQ ID NO: 530), Caulobacter crescentus TadA (SEQ ID NO: 531), Geobacter sulfurreducens TadA (SEQ ID NO: 532), Streptococcus pyogenes TadA (SEQ ID NO: 533), Aquifex aeolicus TadA (SEQ ID NO: 534), and E. coli TadA deaminase (ecTadA) (SEQ ID NO: 535). By “adenosine deaminase activity” is meant catalyzing the deamination of adenine or adenosine to guanine in a polynucleotide. By “Adenosine Base Editor (ABE)” is meant a base editor comprising an adenosine deaminase. By “Adenosine Base Editor (ABE) polynucleotide” is meant a polynucleotide encoding an ABE. By “Adenosine Base Editor 8 (ABE8) polypeptide” or “ABE8” is meant a base editor as defined herein comprising an adenosine deaminase or adenosine deaminase variant comprising one or more of the alterations listed in Table 5B, one of the combinations of alterations listed in Table 5B, or an alteration at one or more of the amino acid positions listed in Table 5B, where such alterations are relative to the following reference sequence: MSEVEFSHEYWMRHALTLAKRARDEREVPVGAVLVLNNRVIGEGWNRAIGLHDPTAHAEIMA LRQGGLVMQNYRLIDATLYVTFEPCVMCAGAMIHSRIGRVVFGVRNAKTGAAGSLMDVLHYP GMNHRVEITEGILADECAALLCYFFRMPRQVFNAQKKAQSSTD (SEQ ID NO: 1), or a corresponding position in another adenosine deaminase. In embodiments, ABE8 comprises ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 alterations at amino acids 82 and / or 166 of SEQ ID NO: 1. In some embodiments, ABE8 comprises further alterations, as described herein, relative to the reference sequence. By “Adenosine Base Editor 8 (ABE8) polynucleotide” is meant a polynucleotide encoding an ABE8 polypeptide. “Administering” is referred to herein as providing one or more compositions described herein to a patient or a subject. By way of example and without limitation, composition administration (e.g., injection) can be performed by intravenous (i.v.) injection, sub-cutaneous (s.c.) injection, intradermal (i.d.) injection, intraperitoneal (i.p.) injection, or intramuscular (i.m.) injection. One or more such routes can be employed. Parenteral administration can be, for example, by bolus injection or by gradual perfusion over time. In some embodiments, parenteral administration includes infusing or injecting intravascularly, intravenously, intramuscularly, intraarterially, intrathecally, intratumorally, intradermally, intraperitoneally, transtracheally, subcutaneously, subcuticularly, intraarticularly, subcapsularly, subarachnoidly and intrasternally. Alternatively, or concurrently, administration can be by the oral route. By “agent” is meant any cellular therapeutic, small molecule chemical compound, antibody, nucleic acid molecule, or polypeptide, or functional fragments thereof. In an embodiment, the agent is an immune effector cell (e.g., T cell, NK cell) expressing an HLA-E single-chain trimer of the disclosure. In an embodiment, the agent is an immune effector cell (e.g., T cell, NK cell) with endogenous B2M and / or CD58 knockout and expressing an HLA- E single-chain trimer of the disclosure. “Allogeneic,” as used herein, refers to cells that are genetically dissimilar and immunologically incompatible. By “alteration” is meant a change in the level, structure, or activity of an analyte, gene or polypeptide as detected by standard art known methods such as those described herein. As used herein, an alteration includes a change (e.g., increase or reduction) in expression levels. In embodiments, the increase or reduction in expression levels is by 10%, 25%, 40%, 50% or greater. In some embodiments, an alteration includes an insertion, deletion, or substitution of a nucleobase or amino acid (by, e.g., genetic engineering). By “ameliorate” is meant reduce, suppress, attenuate, diminish, arrest, or stabilize the development or progression of a disease. By “analog” is meant a molecule that is not identical but has analogous functional or structural features. For example, a polypeptide analog retains the biological activity of a corresponding naturally-occurring polypeptide, while having certain biochemical ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 modifications that enhance the analog’s function relative to a naturally occurring polypeptide. Such biochemical modifications could increase the analog’s protease resistance, membrane permeability, or half-life, without altering, for example, ligand binding. An analog may include an unnatural amino acid. “Autologous,” as used herein, refers to cells from the same subject. By “base editor (BE),” or “nucleobase editor polypeptide (NBE)” is meant an agent that binds a polynucleotide and has nucleobase modifying activity. In various embodiments, the base editor comprises a nucleobase modifying polypeptide (e.g., a deaminase) and a polynucleotide programmable nucleotide binding domain (e.g., Cas9 or Cpf1). Representative nucleic acid and protein sequences of base editors include those sequences having about or at least about 85% sequence identity to any base editor sequence provided in the sequence listing, such as those corresponding to SEQ ID NOs: 2-11. By “BE4 cytidine deaminase (BE4) polypeptide,” is meant a base editor comprising a nucleic acid programmable DNA binding protein (napDNAbp) domain, a cytidine deaminase domain, and two uracil glycosylase inhibitor domains (UGIs). In embodiments, the napDNAbp is a Cas9n (D10A) polypeptide. Non-limiting examples of cytidine deaminase domains include rAPOBEC, ppAPOBEC, RrA3F, AmAPOBEC1, and SsAPOBEC3B. By “BE4 cytidine deaminase (BE4) polynucleotide,” is meant a polynucleotide encoding a BE4 polypeptide. By “base editing activity” is meant acting to chemically alter a base within a polynucleotide. In one embodiment, a first base is converted to a second base. In one embodiment, the base editing activity is cytidine deaminase activity, e.g., converting target C•G to T•A. In another embodiment, the base editing activity is adenosine or adenine deaminase activity, e.g., converting A•T to G•C. By “base editing efficiency” is meant the total percent of one or more target bases in a sample that have been modified using a base editor. In some cases, the base editing efficiency is calculated as the total percent of target polynucleotides in a sample containing a modified target base. In some instances, the base editing efficiency is calculated as the total percent of target polynucleotides in a sample containing a modification to one or more (e.g., 2, 3, 4, 5, 6, 7, 8, 9 or 10) of 2, 3, 4, 5, 6, 7, 8, 9, or 10 target bases. Methods for measuring base editing efficiency for a base editor are known in the art (see, e.g., Gaudelli, et al. Nature 551:464-471 (2017), the disclosure of which is incorporated herein in its entirety for all purposes). In some cases a base editing efficiency is a median base editing efficiency calculated across 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 60, 70, 80, 90, 100 or more target sites. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 By “base editing window” for a base editor is meant bases within a target polynucleotide sequence that can be modified using the base editor. In some embodiments, the position of the nucleobases in the target polynucleotide sequence are numbered relative to a protospacer adjacent motif (PAM) for which a nucleic acid programmable DNA binding protein (napDNAbp) domain of the base editor has specificity, where base 1 corresponds to the base immediately adjacent to the PAM. In some embodiments, the position of the nucleobases in the target polynucleotide sequence are numbered relative to the 5′ or 3′ end of a spacer of a guide polynucleotide used to guide a nucleic acid programmable DNA binding protein (napDNAbp) domain of the base editor to a target site, where base 1 corresponds to the 5′ or 3′ terminal base of the spacer. The term “base editor system” refers to an intermolecular complex for editing a nucleobase of a target nucleotide sequence. In various embodiments, the base editor (BE) system comprises (1) a polynucleotide programmable nucleotide binding domain, a deaminase domain (e.g., cytidine deaminase or adenosine deaminase) for deaminating nucleobases in the target nucleotide sequence; and (2) one or more guide polynucleotides (e.g., guide RNA) in conjunction with the polynucleotide programmable nucleotide binding domain. In various embodiments, the base editor (BE) system comprises a nucleobase editor domain selected from an adenosine deaminase or a cytidine deaminase, and a domain having nucleic acid sequence specific binding activity. In some embodiments, the base editor system comprises (1) a base editor (BE) comprising a polynucleotide programmable DNA binding domain and a deaminase domain for deaminating one or more nucleobases in a target nucleotide sequence; and (2) one or more guide RNAs in conjunction with the polynucleotide programmable DNA binding domain. In some embodiments, the polynucleotide programmable nucleotide binding domain is a polynucleotide programmable DNA binding domain. In some embodiments, the base editor is a cytidine base editor (CBE). In some embodiments, the base editor is an adenine or adenosine base editor (ABE). In some embodiments, the base editor is an adenine or adenosine base editor (ABE) or a cytidine or cytosine base editor (CBE). In some embodiments, the base editor system (e.g., a base editor system comprising a cytidine deaminase) comprises a uracil glycosylase inhibitor or other agent or peptide (e.g., a uracil stabilizing protein such as provided in WO2022015969, the disclosure of which is incorporated herein by reference in its entirety for all purposes) that inhibits the inosine base excision repair system. By “beta-2-microglobulin (β2M; B2M) polypeptide” is meant a protein having at least about 85% amino acid sequence identity to one or more of the exemplary B2M polypeptide ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 sequences provided below, or a functional fragment thereof having immunomodulatory activity. In embodiments, the B2M polypeptide contains a modification at one or more of positions selected from K58, W60, and W95 (e.g., a K58E, W60G, and / or W95G alteration) or a corresponding position(s), where the positions are numbered relative to the “B2M Reference Sequence” provided below. Exemplary human B2M polypeptide sequences are provided below and include the sequence corresponding to UniProt Accession No. P61769 and the “B2M Reference Sequence”. Further exemplary B2M polypeptide sequences include those disclosed in International Patent Application No. PCT / US23 / 72911, the disclosure of which is incorporated herein by reference in its entirety for all purposes. >sp|P61769|B2MG_HUMAN Beta-2-microglobulin OS=Homo sapiens OX=9606 GN=B2M PE=1 SV=1 MSRSVALAVLALLSLSGLEAIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKN GERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM (SEQ ID NO: 426). >B2M Reference Sequence IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSF YLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM (SEQ ID NO: 427). By “beta-2-microglobulin (β2M; B2M) polynucleotide” is meant a nucleic acid molecule encoding an β2M polypeptide, as well as the introns, exons, 3′ untranslated regions, 5′ untranslated regions, and regulatory sequences associated with its expression, or fragments thereof. The beta-2-microglobulin gene encodes a serum protein associated with the major histocompatibility complex. β2M is involved in non-self recognition by host CD8+ T cells. An exemplary β2M polynucleotide sequence is provided atGenBank Accession No. DQ217933.1. By “beta-2-microglobulin signal peptide (β2M SP; B2M SP)” is meant a polypeptide with at least about 85% amino acid sequence identity to the amino acid sequence MSRSVALAVLALLSLSGLEA (SEQ ID NO: 428), or a fragment thereof capable of functioning as a signal peptide. By “beta-2-microglobulin signal peptide (β2M SP; B2M SP) polynucleotide” is meant a nucleic acid molecule encoding a B2M SP. An exemplary B2M SP polynucleotide sequence is provided below. >B2M SP polynucleotide sequence ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCC (SEQ ID NO: 429). The term “Cas9” or “Cas9 domain” refers to an RNA guided nuclease comprising a Cas9 protein, or a fragment thereof (e.g., a protein comprising an active, inactive, or partially active DNA cleavage domain of Cas9, and / or the gRNA binding domain of Cas9). A Cas9 nuclease is also referred to sometimes as a casnl nuclease or a CRISPR (clustered regularly interspaced short palindromic repeat) associated nuclease. By “chimeric antigen receptor” or “CAR” is meant a synthetic or engineered receptor comprising an extracellular antigen binding domain operationally joined to one or more intracellular signaling domains where the CAR confers specificity for an antigen bound by the extracellular antigen binding domain onto an immune effector cell. In some cases, the intracellular signaling domain is a T cell signaling domain. In embodiments, the immune effector cell is a T cell, an NK cell, or a macrophage. In embodiments, the CAR is a SUPRA CAR, an anti-tag CAR, a TCR-CAR, or a TCR-like CAR (see, e.g., Guedan, et al. “Engineering and Design of Chimeric Antigen Receptors,” Methods and Clinical Development, 12:145-156 (2019); Poorebrahim, et al., “TCR-like CARs and TCR-CARs targeting neoepitopes: an emerging potential,” Cancer Gene Therapy, 28:581-589 (2021); and Minutolo, et al. “The Emergence of Universal Immune Receptor T Cell Therapy for Cancer,” Front Oncol., 9:176 (2019), the disclosures of which are incorporated herein by reference in their entireties for all purposes). By “chimeric antigen receptor (CAR) T cell” or “CAR-T cell” is meant a T cell expressing a CAR that has antigen specificity determined by the antibody-derived targeting domain of the CAR. As used herein, “CAR-T cells” include T cells, regulatory T cells (TREG), macrophages, or NK cells. As used herein, the term “CAR-T cells” includes cells engineered to express a CAR or a T cell receptor (TCR, sometimes referred to as TCR-CARs or TCR- like CARs). Methods of making CARs (e.g., for treatment of cancer) are publicly available (see, e.g., Park et al., Trends Biotechnol., 29:550-557, 2011; Grupp et al., N Engl J Med., 368:1509-1518, 2013; Han et al., J. Hematol Oncol.6:47, 2013; Haso et al., (2013) Blood, 121, 1165-1174; Mohseni, et al., (2020) Front. Immunol., 11, art.1608, doi: 10.3389 / fimmu.2020.01608; Eggenhuizen, et al. Int. J. Mol. Sci. (2020), 21:7015, doi: 10.3390 / ijms21197015; Poorebrahim, et al., Cancer Gene Ther 28, 581–589 (2021), doi.org / 10.1038 / s41417-021-00307-7, PCT Pubs. WO2012 / 079000, WO2013 / 059593; and U.S. Pub.2012 / 0213783, the disclosure of each of which is incorporated herein by reference herein in its entirety). ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 By “cluster of differentiation 8-alpha (CD8a) transmembrane and truncated cytoplasmic domain polypeptide” is meant a polypeptide with at least about 85% amino acid sequence identity to the amino acid sequenceIYIWAPLAGTCGVLLLSLVITLYC (SEQ ID NO: 620), or a fragment thereof capable of anchoring a polypeptide linked thereto to a cell membrane. By “cluster of differentiation 8-alpha (CD8a) transmembrane and truncated cytoplasmic domain polynucleotide” is meant a nucleic acid molecule encoding a CD8a transmembrane and truncated cytoplasmic domain polypeptide. By “Cluster of Differentiation 58 (CD58) polypeptide” is meant a protein having at least about 85% amino acid sequence identity to NCBI Reference Sequence Accession No. NP_001770.1, which is provided below, or a fragment thereof that functions in the immune system. CD58 and the immunobiology thereof is described in Zhang, et al. "CD58 Immunobiology at a Glance," Frontiers in Immunology, vol.12, article 705260 (2021), the disclosure of which is incorporated herein by reference in its entirety for all purposes. >CD58 MVAGSDAGRALGVLSVVCLLHCFGFISCFSQQIYGVVYGNVTFHVPSNVPLKEVLWKKQKDKVAELEN SEFRAFSSFKNRVYLDTVSGSLTIYNLTSSDEDEYEMESPNITDTMKFFLYVLESLPSPTLTCALTNG SIEVQCMIPEHYNSHRGLIMYSWDCPMEQCKRNSTSIYFKMENDLPQKIQCTLSNPLFNTTSSIILTT CIPSSGHSRHRYALIPIPLAVITTCIVLYMNGILKCDRKPDRTNSN (SEQ ID NO: 430). By “Cluster of Differentiation 58 (CD58) polynucleotide” is meant a nucleic acid molecule encoding an CD58 polypeptide, as well as the introns, exons, 3′ untranslated regions, 5′ untranslated regions, and regulatory sequences associated with its expression, or fragments thereof. An exemplary CD58 polynucleotide is provided at NCBI Accession No. NM_001779.3, which is reproduced below. ATGGTTGCTGGGAGCGACGCGGGGCGGGCCCTGGGGGTCCTCAGCGTGGTCTGCCTGCTGCACTGCTT TGGTTTCATCAGCTGTTTTTCCCAACAAATATATGGTGTTGTGTATGGGAATGTAACTTTCCATGTAC CAAGCAATGTGCCTTTAAAAGAGGTCCTATGGAAAAAACAAAAGGATAAAGTTGCAGAACTGGAAAAT TCTGAATTCAGAGCTTTCTCATCTTTTAAAAATAGGGTTTATTTAGACACTGTGTCAGGTAGCCTCAC TATCTACAACTTAACATCATCAGATGAAGATGAGTATGAAATGGAATCGCCAAATATTACTGATACCA TGAAGTTCTTTCTTTATGTGCTTGAGTCTCTTCCATCTCCCACACTAACTTGTGCATTGACTAATGGA AGCATTGAAGTCCAATGCATGATACCAGAGCATTACAACAGCCATCGAGGACTTATAATGTACTCATG GGATTGTCCTATGGAGCAATGTAAACGTAACTCAACCAGTATATATTTTAAGATGGAAAATGATCTTC CACAAAAAATACAGTGTACTCTTAGCAATCCATTATTTAATACAACATCATCAATCATTTTGACAACC TGTATCCCAAGCAGCGGTCATTCAAGACACAGATATGCACTTATACCCATACCATTAGCAGTAATTAC ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 AACATGTATTGTGCTGTATATGAATGGTATTCTGAAATGTGACAGAAAACCAGACAGAACCAACTCCA ATTGA (SEQ ID NO: 431). The CD58 gene corresponds to Ensembl: ENSG00000116815. The term “conservative amino acid substitution” or “conservative mutation” refers to the replacement of one amino acid by another amino acid with a common property. A functional way to define common properties between individual amino acids is to analyze the normalized frequencies of amino acid changes between corresponding proteins of homologous organisms (Schulz, G. E. and Schirmer, R. H., Principles of Protein Structure, Springer-Verlag, New York (1979)). According to such analyses, groups of amino acids can be defined where amino acids within a group exchange preferentially with each other, and therefore resemble each other most in their impact on the overall protein structure (Schulz, G. E. and Schirmer, R. H., supra). Non-limiting examples of conservative mutations include amino acid substitutions of amino acids, for example, lysine for arginine and vice versa such that a positive charge can be maintained; glutamic acid for aspartic acid and vice versa such that a negative charge can be maintained; serine for threonine such that a free –OH can be maintained; and glutamine for asparagine such that a free –NH2can be maintained. Amino acids generally can be grouped into classes according to the following common side- chain properties: (1) hydrophobic: Norleucine, Met, Ala, Val, Leu, He; (2) neutral hydrophilic: Cys, Ser, Thr, Asn, Gin; (3) acidic: Asp, Glu; (4) basic: His, Lys, Arg; (5) residues that influence chain orientation: Gly, Pro; (6) aromatic: Trp, Tyr, Phe. In some embodiments, conservative substitutions can involve the exchange of a member of one of these classes for another member of the same class. In some embodiments, non-conservative amino acid substitutions can involve exchanges between a member of one of these classes and another class. By “cluster of differentiation 4 (CD4) polypeptide” is meant a protein having at least about 85% amino acid sequence identity to GenBank accession No. AAB51309.1, or a functional fragment thereof. An exemplary CD4 polypeptide is provided below, where a transmembrane domain is shown as bold text and a truncated intracellular domain is shown as plain text. >Exemplary CD4 polypeptide MALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 432). ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 By “cluster of differentiation 4 (CD4) polynucleotide” is meant a nucleic acid molecule encoding a CD4 polypeptide, as well as the introns, exons, 3′ untranslated regions, 5′ untranslated regions, and regulatory sequences associated with its expression, or fragments thereof. An exemplary CD4 polynucleotide sequence is provided at Ensembl Accession No. ENSG00000010610. By “cluster of differentiation 4 transmembrane (CD4TM) polypeptide” is meant a polypeptide with at least about 85% amino acid sequence identity to the amino acid sequence MALIVLGGVAGLLLFIGLGIFF (SEQ ID NO: 433), or a fragment thereof capable of anchoring a polypeptide linked thereto to a cell membrane. By “CD4TM polynucleotide” is meant a nucleic acid molecule encoding a CD4TM polypeptide. A non-limiting example of a CD4TM polynucleotide is provided below. >CD4TM polynucleotide sequence ATGGCCCTGATCGTGCTGGGCGGCGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTT TTTC (SEQ ID NO: 515). The term “coding sequence” or “protein coding sequence” as used interchangeably herein refers to a segment of a polynucleotide that codes for a protein. Coding sequences can also be referred to as open reading frames. The region or sequence is bounded nearer the 5′ end by a start codon and nearer the 3′ end with a stop codon. Stop codons useful with the base editors described herein include the following: TAG, TAA, and TGA. By “complex” is meant a combination of two or more molecules whose interaction relies on inter-molecular forces. Non-limiting examples of inter-molecular forces include covalent and non-covalent interactions. Non-limiting examples of non-covalent interactions include hydrogen bonding, ionic bonding, halogen bonding, hydrophobic bonding, van der Waals interactions (e.g., dipole-dipole interactions, dipole-induced dipole interactions, and London dispersion forces), and π-effects. In an embodiment, a complex comprises polypeptides, polynucleotides, or a combination of one or more polypeptides and one or more polynucleotides. In one embodiment, a complex comprises one or more polypeptides that associate to form a base editor (e.g., base editor comprising a nucleic acid programmable DNA binding protein, such as Cas9, and a deaminase) and a polynucleotide (e.g., a guide RNA). In an embodiment, the complex is held together by hydrogen bonds. It should be appreciated that one or more components of a base editor (e.g., a deaminase, or a nucleic acid programmable DNA binding protein) may associate covalently or non-covalently. As one example, a base editor may include a deaminase covalently linked to a nucleic acid ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 programmable DNA binding protein (e.g., by a peptide bond). Alternatively, a base editor may include a deaminase and a nucleic acid programmable DNA binding protein that associate noncovalently (e.g., where one or more components of the base editor are supplied in trans and associate directly or via another molecule such as a protein or nucleic acid). In an embodiment, one or more components of the complex are held together by hydrogen bonds. By “cytosine” or “4-Aminopyrimidin-2(1H)-one” is meant a purine nucleobase with the molecular formula C4H5N3O, having the structure corresponding to CAS No.71-30-7. By “cytidine” is meant a cytosine molecule attached to a ribose sugar via a glycosidic bond, having the structure , and corresponding to CAS No.65-46-3. Its molecular formula is C9H13N3O5. By “Cytidine Base Editor (CBE)” is meant a base editor comprising a cytidine deaminase. By “Cytidine Base Editor (CBE) polynucleotide” is meant a polynucleotide encoding a CBE. By “cytidine deaminase” or “cytosine deaminase” is meant a polypeptide or fragment thereof capable of deaminating cytidine or cytosine. In embodiments, the cytidine or cytosine is present in a polynucleotide. In one embodiment, the cytidine deaminase converts cytosine to uracil or 5-methylcytosine to thymine. The terms “cytidine deaminase” and “cytosine deaminase” are used interchangeably throughout the application. Petromyzon marinus cytosine deaminase 1 (PmCDA1) (SEQ ID NO: 12-13), Activation-induced cytidine deaminase (AICDA) (SEQ ID NOs: 14-20), and APOBEC (SEQ ID NOs: 21-61) are exemplary cytidine deaminases. Further exemplary cytidine deaminase (CDA) sequences are provided in the Sequence Listing as SEQ ID NOs: 62-66 and SEQ ID NOs: 67-189. Non- ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 limiting examples of cytidine deaminases include those described in PCT / US20 / 16288, PCT / US2018 / 021878, 180802-021804 / PCT, PCT / US2018 / 048969, PCT / US2016 / 058344, PCT / US2020 / 062428, and PCT / US2019 / 033848, the disclosures of which are incorporated herein by reference in their entireties for all purposes. By “cytidine deaminase polynucleotide” is meant a polynucleotide encoding a cytidine deaminase. By “cytosine deaminase activity” is meant catalyzing the deamination of cytosine or cytidine. In one embodiment, a polypeptide having cytosine deaminase activity converts an amino group to a carbonyl group. In an embodiment, a cytosine deaminase converts cytosine to uracil (i.e., C to U) or 5-methylcytosine to thymine (i.e., 5mC to T). In some embodiments, a cytosine deaminase as provided herein has increased cytosine deaminase activity (e.g., at least 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold, 80-fold, 90-fold, 100-fold or more) relative to a reference cytosine deaminase. The term “deaminase” or “deaminase domain,” as used herein, refers to a protein or fragment thereof that catalyzes a deamination reaction. The term “detect” refers to identifying the presence, absence or amount of the analyte to be detected. In one embodiment, a sequence alteration in a polynucleotide or polypeptide is detected. In another embodiment, the presence of indels is detected. By “detectable label” is meant a composition that when linked to a molecule of interest renders the latter detectable, via spectroscopic, photochemical, biochemical, immunochemical, or chemical means. For example, useful labels include radioactive isotopes, magnetic beads, metallic beads, colloidal particles, fluorescent dyes, electron-dense reagents, enzymes (for example, as commonly used in an enzyme linked immunosorbent assay (ELISA)), biotin, digoxigenin, or haptens. By “disease” is meant any condition or disorder that damages or interferes with the normal function of a cell, tissue, or organ. In some embodiments, the disease is a neoplasia, such as a cancer (e.g., a hematological cancer or a solid tumor). In some instances, the disease is a disease that can be treated using the modified allogeneic T cells of the disclosure. In some embodiments, the disease is an autoimmune disease. By “dual editing activity” or “dual deaminase activity” is meant having adenosine deaminase and cytidine deaminase activity. In one embodiment, a base editor having dual editing activity has both A^G and C^T activity, wherein the two activities are approximately equal or are within about 10% or 20% of each other. In another embodiment, a dual editor has A^G activity that no more than about 10% or 20% greater than C^T ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 activity. In another embodiment, a dual editor has A^G activity that is no more than about 10% or 20% less than C^T activity. In some embodiments, the adenosine deaminase variant has predominantly cytosine deaminase activity, and little, if any, adenosine deaminase activity. In some embodiments, the adenosine deaminase variant has cytosine deaminase activity, and no significant or no detectable adenosine deaminase activity. Non-limiting examples of proteins having dual deaminase activity include those described in International Patent Application Publications No. WO 2024 / 040083 and WO 2022 / 204574, the disclosures of which are hereby incorporated by reference in their entireties for all purposes. By “effective amount” is meant the amount of an agent (e.g., a base editor, cell) as described herein, that is required to ameliorate the symptoms of a disease relative to an untreated patient or an individual without disease, i.e., a healthy individual, or is the amount of the agent sufficient to elicit a desired biological response. The effective amount of active compound(s) used to practice embodiments of the present disclosure for therapeutic treatment of a disease varies depending upon the manner of administration, the age, body weight, and general health of the subject. Ultimately, the attending physician or veterinarian will decide the appropriate amount and dosage regimen. Such amount is referred to as an “effective” amount. In one embodiment, an effective amount is the amount of a base editor of the disclosure sufficient to introduce an alteration in a gene of interest in a cell (e.g., a cell in vitro or in vivo). In one embodiment, an effective amount is the amount of a base editor required to achieve a therapeutic effect. Such therapeutic effect need not be sufficient to alter a pathogenic gene in all cells of a subject, tissue or organ, but only to alter the pathogenic gene in about 1%, 5%, 10%, 25%, 50%, 75% or more of the cells present in a subject, tissue or organ. In one embodiment, an effective amount is sufficient to ameliorate one or more symptoms of a disease. The term “exonuclease” refers to a protein or polypeptide capable of removing successive nucleotides from either the 5′ or 3′ end of a polynucleotide. The term “endonuclease” refers to a protein or polypeptide capable of catalyzing the cleavage of internal regions in a polynucleotide. By “fragment” is meant a portion of a polypeptide or nucleic acid molecule. This portion contains, at least about 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, or 90% of the entire length of the reference nucleic acid molecule or polypeptide. A fragment may contain 10, 20, 30, 40, 50, 60, 70, 80, 90, or 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 nucleotides or amino acids. In some embodiments, the fragment is a functional fragment. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 In general, a "gene" is a region on the genome that is capable of being transcribed to an RNA that either has a regulatory function, a catalytic function, and / or encodes a protein. An eukaryotic gene typically has introns and exons, which may organize to produce different RNA splice variants that encode alternative versions of a mature protein. The skilled artisan will appreciate that the present disclosure encompasses all transcripts encoding a polypeptide of interest, including splice variants, allelic variants and transcripts that occur because of alternative promoter sites or alternative poly-adenylation sites. A "full-length" gene or RNA therefore encompasses any naturally occurring splice variants, allelic variants, other alternative transcripts, splice variants generated by recombinant technologies which bear the same function as the naturally occurring variants, and the resulting RNA molecules. In some embodiments, the fragment is a functional fragment. “Graft versus host disease” (GVHD) refers to a pathological condition where transplanted cells of a donor generate an immune response against cells of the host. By “guide polynucleotide” is meant a polynucleotide or polynucleotide complex which is specific for a target sequence and can form a complex with a polynucleotide programmable nucleotide binding domain protein (e.g., Cas9 or Cpf1). In an embodiment, the guide polynucleotide is a guide RNA (gRNA). gRNAs can exist as a complex of two or more RNAs, or as a single RNA molecule. By “heterologous,” or “exogenous” is meant a polynucleotide or polypeptide that 1) has been experimentally incorporated into a polynucleotide or polypeptide sequence to which the polynucleotide or polypeptide is not normally found in nature; and / or 2) has been experimentally placed into a cell that does not normally comprise the polynucleotide or polypeptide. In some embodiments, “heterologous” means that a polynucleotide or polypeptide has been experimentally placed into a non-native context. In some embodiments, a heterologous polynucleotide or polypeptide is derived from a first species or host organism and is incorporated into a polynucleotide or polypeptide derived from a second species or host organism. In some embodiments, the first species or host organism is different from the second species or host organism. In some embodiments the heterologous polynucleotide is DNA. In some embodiments the heterologous polynucleotide is RNA. By “Human Leukocyte Antigen-E (HLA-E) polypeptide” is meant a protein having at least about 85% amino acid sequence identity to NCBI Accession No. NP_005507.3 (SEQ ID NO: 629), or a fragment thereof having immunomodulatory activity and / or capable of binding a cognate polypeptide. Exemplary HLA-E polypeptides are provided below. In various embodiments, the HLA-E polypeptide includes an amino acid alteration introducing a ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 new cysteine to the polypeptide (e.g., at position 83 relative to the below “HLA-E heavy chain” sequence, where position 83 is shown in bold, and where the N-terminal S is position 1). In various embodiments, the HLA-E polypeptide includes one or more amino acid alterations that reduce binding of a CD8 coreceptor to the HLA-E polypeptide. In some cases, the HLA-E polypeptide contains one or more mutations in an alpha3 domain that reduce immunogenicity of the HLA-E polypeptide and / or binding of a CD8 coreceptor to the HLA-E polypeptide relative to a reference HLA-E polypeptide lacking the one or more mutations. In some instances, the HLA-E polypeptide contains one or more of the following amino acid alterations: D227K, T228A, and A245V, where the amino acid positions are numbered relative to the following HLA-E heavy chain where the N-terminal S is position 2, and where the positions of the alterations are shown in bold in the below HLA-E heavy chain amino acid sequence. >HLA-E heavy chain SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 456). >HLA-E heavy chain having a cysteine at position 83, which is shown in bold SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGCYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 457). By “Human Leukocyte Antigen-E (HLA-E) polynucleotide” is meant a nucleic acid molecule encoding an HLA-E polypeptide, as well as the introns, exons, 3′ untranslated regions, 5′ untranslated regions, and regulatory sequences associated with its expression, or fragments thereof. An exemplary HLA-E polynucleotide is provided at NCBI Accession No. NM_005516.6 (SEQ ID NO: 630). The HLA-E gene corresponds to Ensembl: ENSG00000116815. Exemplary HLA-E polynucleotide sequences are provided below. >HLA-E heavy chain polynucleotide sequence AGCCATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATT CATCAGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCC CTAGAATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAG ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ACAAGAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTA CTACAACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGAC CTGACGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACC CTTAATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAA AAGCAACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAAT GGCTGCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACC CACGTTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTT CTACCCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCG AGCTGGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTG CCATCTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGT GACCCTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCC (SEQ ID NO: 458). >Polynucleotide sequence encoding an HLA-E heavy chain polypeptide having a cysteine at position 83 AGCCATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATT CATCAGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCC CTAGAATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAG ACAAGAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTG TTACAACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGAC CTGACGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACC CTTAATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAA AAGCAACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAAT GGCTGCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACC CACGTTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTT CTACCCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCG AGCTGGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTG CCATCTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGT GACCCTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATC (SEQ ID NO: 459). By “HLA-E*0.1:3 transmembrane and truncated cytoplasmic domain polypeptide” is meant a polypeptide with at least about 85% amino acid sequence identity to the amino acid sequence VGIIAGLVLLGSVVSGAVVAAVIWRKKSSGGKGGSYSKAEWSDSAQGSESHSL (SEQ ID NO: 619), or a fragment thereof capable of anchoring a polypeptide linked thereto to a cell membrane. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 By “HLA-E*0.1:3 transmembrane and truncated cytoplasmic domain polynucleotide” is meant a nucleic acid molecule encoding an HLA-E*0.1:3 transmembrane and truncated cytoplasmic domain polypeptide. “Host versus graft disease” (HVGD) refers to a pathological condition where the immune system of a host generates an immune response against transplanted cells of a donor. “Hybridization” means hydrogen bonding, which may be Watson-Crick, Hoogsteen or reversed Hoogsteen hydrogen bonding, between complementary nucleobases. For example, adenine and thymine are complementary nucleobases that pair through the formation of hydrogen bonds. By “major histocompatibility complex, class I, A (HLA-A) polypeptide” is meant an HLA class-I heavy chain polypeptide having at least about 85% amino acid sequence identity to GenBank Accession No. BAA07530.1, or a fragment thereof having antigen presenting activity. By “major histocompatibility complex, class I, A (HLA-A) polynucleotide” is meant a nucleic acid molecule encoding an HLA-A polypeptide, as well as the introns, exons, 3′ untranslated regions, 5′ untranslated regions, and regulatory sequences associated with its expression, or fragments thereof. An exemplary HLA-A polynucleotide sequence is provided at GenBank Accession No. D38525.1. The HLA-A gene corresponds to Ensemble ENSG00000206503. By “major histocompatibility complex, class I, B (HLA-B) polypeptide” is meant an HLA class-I heavy chain polypeptide having at least about 85% amino acid sequence identity to GenBank Accession No. CAD30340.1, or a fragment thereof having antigen presenting activity. By “major histocompatibility complex, class I, B (HLA-B) polynucleotide” is meant a nucleic acid molecule encoding an HLA-B polypeptide, as well as the introns, exons, 3′ untranslated regions, 5′ untranslated regions, and regulatory sequences associated with its expression, or fragments thereof. An exemplary HLA-B polynucleotide sequence is provided at GenBank Accession No. AJ458992.1. By “major histocompatibility complex, class I, C (HLA-C) polypeptide” is meant an HLA class-I heavy chain polypeptide having at least about 85% amino acid sequence identity to GenBank Accession No. BBO94058.1, or a fragment thereof having antigen presenting activity. By “major histocompatibility complex, class I, C (HLA-C) polynucleotide” is meant a nucleic acid molecule encoding an HLA-C polypeptide, as well as the introns, exons, 3′ ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 untranslated regions, 5′ untranslated regions, and regulatory sequences associated with its expression, or fragments thereof. An exemplary HLA-C polynucleotide sequence is provided at GenBank Accession No. LC508210.1. By “immune cell” is meant a cell of the immune system capable of generating an immune response. Exemplary immune cell include, but are not limited to, T cells, NK cells, B cells, or hematopoietic stem cells. By “immune effector cell” is meant a lymphocyte, once activated, capable of effecting an immune response upon a target cell. In some embodiments, immune effector cells are effector T cells. In some embodiments, the effector T cell is a naïve CD8+T cell, a cytotoxic T cell, a natural killer T (NKT) cell, a natural killer (NK) cell, or a regulatory T (Treg) cell. In some embodiments, immune effector cells are effector NK cells. In some embodiments, the effector T cells are thymocytes, immature T lymphocytes, mature T lymphocytes, resting T lymphocytes, or activated T lymphocytes. In some embodiments the immune effector cell is a CD4+CD8+T cell or a CD4- CD8- T cell. In some embodiments the immune effector cell is a T helper cell. In some embodiments the T helper cell is a T helper 1 (Th1), a T helper 2 (Th2) cell, or a helper T cell expressing CD4 (CD4+ T cell). By “immunomodulatory activity” is meant increasing, decreasing, or sustaining an immune response. In embodiments, the reduction in immune response is at least about 5%, 10%, 10%, 25%, 50%, 75%, 80%, 90%, 95% or 100%. In embodiments, a reduction in immune response is measured by detecting the expression, levels, or activity of granzyme B (GZMB), IFN-gamma, and TNF-alpha. In other embodiments, a reduction in immune response is measured by detecting a reduction in the killing of a target cell (e.g., modified immune cell) by an effector cell (e.g., CAR-T cell, T cell, NK cell). By “increases” is meant a positive alteration of at least 10%, 25%, 50%, 75%, or 100%, or about 1.5 fold, about 2 fold, about 3-fold, about 4-fold, about 5-fold, about 6-fold, about 7-fold, about 8-fold, about 9-fold, about 10-fold, about 15-fold, about 20-fold, about 25-fold, about 30-fold, about 35-fold, about 40-fold, about 45-fold, about 50-fold, or about 100-fold. The terms “inhibitor of base repair”, “base repair inhibitor”, “IBR” or their grammatical equivalents refer to a protein that is capable in inhibiting the activity of a nucleic acid repair enzyme, for example a base excision repair enzyme. An “intein” is a fragment of a protein that is able to excise itself and join the remaining fragments (the exteins) with a peptide bond in a process known as protein splicing. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 The terms “isolated,” “purified,” or “biologically pure” refer to material that is free to varying degrees from components which normally accompany it as found in its native state. “Isolate” denotes a degree of separation from original source or surroundings. “Purify” denotes a degree of separation that is higher than isolation. A “purified” or “biologically pure” protein is sufficiently free of other materials such that any impurities do not materially affect the biological properties of the protein or cause other adverse consequences. That is, a nucleic acid or peptide of this disclosure is purified if it is substantially free of cellular material, viral material, or culture medium when produced by recombinant DNA techniques, or chemical precursors or other chemicals when chemically synthesized. Purity and homogeneity are typically determined using analytical chemistry techniques, for example, polyacrylamide gel electrophoresis or high performance liquid chromatography. The term “purified” can denote that a nucleic acid or protein gives rise to essentially one band in an electrophoretic gel. For a protein that can be subjected to modifications, for example, phosphorylation or glycosylation, different modifications may give rise to different isolated proteins, which can be separately purified. By “isolated polynucleotide” is meant a nucleic acid molecule that is free of the genes which, in the naturally-occurring genome of the organism from which the nucleic acid molecule of the disclosure is derived, flank the gene. The term therefore includes, for example, a recombinant DNA that is incorporated into a vector; into an autonomously replicating plasmid or virus; or into the genomic DNA of a prokaryote or eukaryote; or that exists as a separate molecule (for example, a cDNA or a genomic or cDNA fragment produced by PCR or restriction endonuclease digestion) independent of other sequences. In addition, the term includes an RNA molecule that is transcribed from a DNA molecule, as well as a recombinant DNA that is part of a hybrid gene encoding additional polypeptide sequence. By an “isolated polypeptide” is meant a polypeptide of the disclosure that has been separated from components that naturally accompany it. Typically, the polypeptide is isolated when it is at least 60%, by weight, free from the proteins and naturally-occurring organic molecules with which it is naturally associated. In embodiments, the preparation is at least 75%, at least 90%, or at least 99%, by weight, a polypeptide of the disclosure. An isolated polypeptide of the disclosure may be obtained, for example, by extraction from a natural source, by expression of a recombinant nucleic acid encoding such a polypeptide; or by chemically synthesizing the protein. Purity can be measured by any appropriate method, for example, column chromatography, polyacrylamide gel electrophoresis, or by HPLC analysis. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 The term “linker”, as used herein, refers to a molecule that links two moieties. In one embodiment, the term “linker” refers to a covalent linker (e.g., covalent bond) or a non- covalent linker. In various embodiments, a linker is a linker peptide, such as a GS linker. In some cases, the GS linker includes an alteration so that the GS linker includes a cysteine amino acid. Non-limiting examples of GS linker amino acid sequences include the following sequences, or variants thereof having 1, 2, 3, 4, or 5 amino acid alterations: >GS linker 1 GGGGSGGGGSGGGGS (SEQ ID NO: 460). >GS linker with an alteration adding a cysteine amino acid, where the cysteine is shown in bold GCGGSGGGGSGGGGS (SEQ ID NO: 461). >GS linker 2 GGGGSGGGGSGGGGSGGGGSG (SEQ ID NO: 464). By “linker polynucleotide” is meant a nucleic acid molecule encoding a linker peptide, as well as the introns, exons, 3′ untranslated regions, 5′ untranslated regions, and regulatory sequences associated with its expression, or fragments thereof. Non-limiting examples of linker polynucleotide sequences are provided below. >GS linker polynucleotide sequence 1 GGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCGGCGGCAGC (SEQ ID NO: 462). >Polynucleotide sequence encoding a GS linker containing a cysteine amino acid encoded by the nucleotides shown in bold GGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCGGCGGCAGC (SEQ ID NO: 463). >GS linker polynucleotide sequence 2 GGCGGCGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGG A (SEQ ID NO: 465). By “marker” is meant any protein or polynucleotide having an alteration in expression, level, structure, or activity that is associated with a disease or disorder. The term “mutation,” as used herein, refers to a substitution of a residue within a sequence, e.g., a nucleic acid or amino acid sequence, with another residue, or a deletion or insertion of one or more residues within a sequence. Mutations are typically described herein by identifying the original residue followed by the position of the residue within the sequence and by the identity of the newly substituted residue. Various methods for making the amino acid substitutions (mutations) provided herein are well known in the art, and are provided by, ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 for example, Green and Sambrook, Molecular Cloning: A Laboratory Manual (4thed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (2012)). The terms “nucleic acid” and “nucleic acid molecule,” as used herein, refer to a compound comprising a nucleobase and an acidic moiety, e.g., a nucleoside, a nucleotide, or a polymer of nucleotides. Typically, polymeric nucleic acids, e.g., nucleic acid molecules comprising three or more nucleotides are linear molecules, in which adjacent nucleotides are linked to each other via a phosphodiester linkage. In some embodiments, “nucleic acid” refers to individual nucleic acid residues (e.g., nucleotides and / or nucleosides). In some embodiments, “nucleic acid” refers to an oligonucleotide chain comprising three or more individual nucleotide residues. As used herein, the terms “oligonucleotide” and “polynucleotide” can be used interchangeably to refer to a polymer of nucleotides (e.g., a string of at least three nucleotides). In some embodiments, “nucleic acid” encompasses RNA as well as single and / or double-stranded DNA. Nucleic acids may be naturally occurring, for example, in the context of a genome, a transcript, an mRNA, tRNA, rRNA, siRNA, snRNA, a plasmid, cosmid, chromosome, chromatid, or other naturally occurring nucleic acid molecule. On the other hand, a nucleic acid molecule may be a non-naturally occurring molecule, e.g., a recombinant DNA or RNA, an artificial chromosome, an engineered genome, or fragment thereof, or a synthetic DNA, RNA, DNA / RNA hybrid, or including non-naturally occurring nucleotides or nucleosides. Furthermore, the terms “nucleic acid,” “DNA,” “RNA,” and / or similar terms include nucleic acid analogs, e.g., analogs having other than a phosphodiester backbone. Nucleic acids can be purified from natural sources, produced using recombinant expression systems and optionally purified, chemically synthesized, etc. Where appropriate, e.g., in the case of chemically synthesized molecules, nucleic acids comprise nucleoside analogs such as analogs having chemically modified bases or sugars, and backbone modifications. A nucleic acid sequence is presented in the 5′ to 3′ direction unless otherwise indicated. In some embodiments, a nucleic acid is or comprises natural nucleosides (e.g. adenosine, thymidine, guanosine, cytidine, uridine, deoxyadenosine, deoxythymidine, deoxyguanosine, and deoxycytidine); nucleoside analogs (e.g., 2- aminoadenosine, 2-thiothymidine, inosine, pyrrolo-pyrimidine, 3-methyl adenosine, 5- methylcytidine, 2-aminoadenosine, C5-bromouridine, C5-fluorouridine, C5-iodouridine, C5- propynyl-uridine, C5-propynyl-cytidine, C5-methylcytidine, 2-aminoadenosine, 7- deazaadenosine, 7-deazaguanosine, 8-oxoadenosine, 8-oxoguanosine, O(6)-methylguanine, and 2-thiocytidine); chemically modified bases; biologically modified bases (e.g., methylated bases); intercalated bases; modified sugars (e.g., 2′-fluororibose, ribose, 2′-deoxyribose, ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 arabinose, and hexose); and / or modified phosphate groups (e.g., phosphorothioates and 5′-N- phosphoramidite linkages). The term “nuclear localization sequence,” “nuclear localization signal,” or “NLS” refers to an amino acid sequence that promotes import of a protein into the cell nucleus. Nuclear localization sequences are known in the art and described, for example, in Plank et al., International PCT application, PCT / EP2000 / 011690, filed November 23, 2000, published as WO / 2001 / 038547 on May 31, 2001, the contents of which are incorporated herein by reference for their disclosure of exemplary nuclear localization sequences. In other embodiments, the NLS is an optimized NLS described, for example, by Koblan et al., Nature Biotech.2018 doi:10.1038 / nbt.4172. In some embodiments, an NLS comprises the amino acid sequence KRTADGSEFESPKKKRKV (SEQ ID NO: 190),KRPAATKKAGQAKKKK (SEQ ID NO: 191),KKTELQTTNAENKTKKL (SEQ ID NO: 192),KRGINDRNFWRGENGRKTR (SEQ ID NO: 193),RKSGKIAAIVVKRPRK (SEQ ID NO: 194),PKKKRKV (SEQ ID NO: 195),MDSLLMNRRKFLYQFKNVRWAKGRRETYLC (SEQ ID NO: 196), PKKKRKVEGADKRTADGSEFESPKKKRKV (SEQ ID NO: 328), or RKSGKIAAIVVKRPRKPKKKRKV (SEQ ID NO: 329). The term “nucleobase,” “nitrogenous base,” or “base,” used interchangeably herein, refers to a nitrogen-containing biological compound that forms a nucleoside, which in turn is a component of a nucleotide. The ability of nucleobases to form base pairs and to stack one upon another leads directly to long-chain helical structures such as ribonucleic acid (RNA) and deoxyribonucleic acid (DNA). Five nucleobases – adenine (A), cytosine (C), guanine (G), thymine (T), and uracil (U) – are called primary or canonical. Adenine and guanine are derived from purine, and cytosine, uracil, and thymine are derived from pyrimidine. DNA and RNA can also contain other (non-primary) bases that are modified. Non-limiting exemplary modified nucleobases can include hypoxanthine, xanthine, 7-methylguanine, 5,6- dihydrouracil, 5-methylcytosine (m5C), and 5-hydromethylcytosine. Hypoxanthine and xanthine can be created through mutagen presence, both of them through deamination (replacement of the amine group with a carbonyl group). Hypoxanthine can be modified from adenine. Xanthine can be modified from guanine. Uracil can result from deamination of cytosine. A “nucleoside” consists of a nucleobase and a five carbon sugar (either ribose or deoxyribose). Examples of a nucleoside include adenosine, guanosine, uridine, cytidine, 5- methyluridine (m5U), deoxyadenosine, deoxyguanosine, thymidine, deoxyuridine, and deoxycytidine. Examples of a nucleoside with a modified nucleobase includes inosine (I), ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 xanthosine (X), 7-methylguanosine (m7G), dihydrouridine (D), 5-methylcytidine (m5C), and pseudouridine (Ψ). A “nucleotide” consists of a nucleobase, a five carbon sugar (either ribose or deoxyribose), and at least one phosphate group. Non-limiting examples of modified nucleobases and / or chemical modifications that a modified nucleobase may include are the following: pseudo-uridine, 5-Methyl-cytosine, 2′-O-methyl-3′-phosphonoacetate, 2′-O- methyl thioPACE (MSP), 2′-O-methyl-PACE (MP), 2′-fluoro RNA (2′-F-RNA), constrained ethyl (S-cEt), 2′-O-methyl (‘M’), 2′-O-methyl-3′-phosphorothioate (‘MS’), 2′-O-methyl-3′- thiophosphonoacetate (‘MSP’), 5-methoxyuridine, phosphorothioate, and N1- Methylpseudouridine. The term “nucleic acid programmable DNA binding protein” or “napDNAbp” may be used interchangeably with “polynucleotide programmable nucleotide binding domain” to refer to a protein that associates with a nucleic acid (e.g., DNA or RNA), such as a guide nucleic acid or guide polynucleotide (e.g., gRNA), that guides the napDNAbp to a specific nucleic acid sequence. In some embodiments, the polynucleotide programmable nucleotide binding domain is a polynucleotide programmable DNA binding domain. In some embodiments, the polynucleotide programmable nucleotide binding domain is a polynucleotide programmable RNA binding domain. In some embodiments, the polynucleotide programmable nucleotide binding domain is a Cas9 protein. A Cas9 protein can associate with a guide RNA that guides the Cas9 protein to a specific DNA sequence that is complementary to the guide RNA. In some embodiments, the napDNAbp is a Cas9 domain, for example a nuclease active Cas9, a Cas9 nickase (nCas9), or a nuclease inactive Cas9 (dCas9). Non-limiting examples of nucleic acid programmable DNA binding proteins include, Cas9 (e.g., dCas9 and nCas9), Cas12a / Cpfl, Cas12b / C2cl, Cas12c / C2c3, Cas12d / CasY, Cas12e / CasX, Cas12g, Cas12h, Cas12i, and Cas12j / CasΦ (Cas12j / Casphi). Non-limiting examples of Cas enzymes include Cas1, Cas1B, Cas2, Cas3, Cas4, Cas5, Cas5d, Cas5t, Cas5h, Cas5a, Cas6, Cas7, Cas8, Cas8a, Cas8b, Cas8c, Cas9 (also known as Csn1 or Csx12), Cas10, Cas10d, Cas12a / Cpfl, Cas12b / C2cl, Cas12c / C2c3, Cas12d / CasY, Cas12e / CasX, Cas12g, Cas12h, Cas12i, Cas12j / CasΦ, Cpf1, Csy1 , Csy2, Csy3, Csy4, Cse1, Cse2, Cse3, Cse4, Cse5e, Csc1, Csc2, Csa5, Csn1, Csn2, Csm1, Csm2, Csm3, Csm4, Csm5, Csm6, Cmr1, Cmr3, Cmr4, Cmr5, Cmr6, Csb1, Csb2, Csb3, Csx17, Csx14, Csx10, Csx16, CsaX, Csx3, Csx1, Csx1S, Csx11, Csf1, Csf2, CsO, Csf4, Csd1, Csd2, Cst1, Cst2, Csh1, Csh2, Csa1, Csa2, Csa3, Csa4, Csa5, Type II Cas effector proteins, Type V Cas effector proteins, Type VI Cas effector proteins, CARF, DinG, homologues thereof, or modified or engineered versions thereof. Other nucleic acid programmable DNA binding proteins are also ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 within the scope of this disclosure, although they may not be specifically listed in this disclosure. See, e.g., Makarova et al. “Classification and Nomenclature of CRISPR-Cas Systems: Where from Here?” CRISPR J.2018 Oct;1:325-336. doi: 10.1089 / crispr.2018.0033; Yan et al., “Functionally diverse type V CRISPR-Cas systems” Science.2019 Jan 4;363(6422):88-91. doi: 10.1126 / science.aav7271, the entire contents of each are hereby incorporated by reference. Exemplary nucleic acid programmable DNA binding proteins and nucleic acid sequences encoding nucleic acid programmable DNA binding proteins are provided in the Sequence Listing as SEQ ID NOs: 197-231, 232-245, 254-257, 260, and 378. In some embodiments, the napDNAbp is a (CRISPR-associated system) Cas9 endonuclease, for example, Cas9 (Csnl) from Streptococcus pyogenes (e.g., SEQ ID NO: 197), Cas9 from Neisseria meningitidis (NmeCas9; SEQ ID NO: 208), Nme2Cas9 (SEQ ID NO: 209), Streptococcus constellatus (ScoCas9), or derivatives thereof (e.g., a sequence with at least about 85% sequence identity to a Cas9, such as Nme2Cas9 or spCas9). Further non-limiting examples of nucleic acid programmable DNA binding proteins include those disclosed or referenced in Rufflow, et al., “Design of highly functional genome editors by modeling of the universe of CRISPR-Cas Sequences,” bioRxiv, posted April 22, 2024, doi: 10.1101 / 2024.04.22.590591, the disclosure of which is incorporated herein by reference in its entirety for all purposes, which were designed using artificial intelligence. In some embodiments, the napDNAbp is OpenCRISPR-1, or a variant thereof (e.g., a variant comprising a D10A amino acid alteration and / or lacking an N-terminal methionine). Further non-limiting examples of nucleic acid programmable DNA binding proteins include those disclosed in International Patent Application No. PCT / US2019 / 047996. The terms “nucleobase editing domain” or “nucleobase editing protein,” as used herein, refers to a protein or enzyme that can catalyze a nucleobase modification in RNA or DNA, such as cytosine (or cytidine) to uracil (or uridine) or thymine (or thymidine), and adenine (or adenosine) to hypoxanthine (or inosine) deaminations, as well as non-templated nucleotide additions and insertions. In some embodiments, the nucleobase editing domain is a deaminase domain (e.g., an adenine deaminase or an adenosine deaminase; or a cytidine deaminase or a cytosine deaminase). As used herein, “obtaining” as in “obtaining an agent” includes synthesizing, purchasing, or otherwise acquiring the agent. By “OpenCRISPR-1 polypeptide” is meant a protein with an amino acid sequence having at least about 85% amino acid sequence identity to SEQ ID NO: 536, or a fragment thereof that associates with a nucleic acid, such as a guide nucleic acid or guide ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 polynucleotide, that guides the napDNAbp to a specific nucleic acid sequence. Further details relating to the OpenCRISPR-1 polypeptide are disclosed in Rufflow, et al., “Design of highly functional genome editors by modeling of the universe of CRISPR-Cas Sequences,” bioRxiv, posted April 22, 2024, doi: 10.1101 / 2024.04.22.590591, the disclosure of which is incorporated herein by reference in its entirety for all purposes. By “OpenCRISPR-1 polynucleotide” is meant a nucleic acid molecule encoding an OpenCRISPR-1 polypeptide, as well as the introns, exons, 3′ untranslated regions, 5′ untranslated regions, and regulatory sequences associated with its expression, or fragments thereof. In embodiments, an OpenCRISPR-1 polynucleotide is the genomic sequence, cDNA, mRNA, or gene associated with and / or required for OpenCRISPR-1 expression. An exemplary OpenCRISPR-1 nucleotide sequence is provided at SEQ ID NO: 537. In various embodiments, a guide RNA suitable for use in combination with an OpenCRISPR-1 polypeptide contains a scaffold having at least 85% sequence identity to a nucleotide sequence selected from the following, or fragments thereof capable of binding to an OpenCRISPR-1 polypeptide: GUUUUAGAGCUGUGUUGAAAAACACAGCAAGUUAAAAUAAGGCUUUGUCCGUAUCCAACUUG AAAAAGUGAGCACCGAUUCGGUGC (SEQ ID NO: 538); GUUUUAGAGCUGGAAACAGCAAGUUAAAAUAAGGCUUUGUCCGUAUCCAACUUGAAAAAGUG AGCACCGAUUCGGUGC (SEQ ID NO: 539); and GUUUUAGAGCUAGAAAUAGCAAGUUAAAAUAAGGCUAGUCCGUUAUCAACUUGAAAAAGUGG CACCGAGUCGGUGC (SEQ ID NO: 540). By “subject” or “patient” is meant a mammal, including, but not limited to, a human or non-human mammal. In embodiments, the mammal is a bovine, equine, canine, ovine, rabbit, rodent, nonhuman primate, or feline. In an embodiment, “patient” refers to a mammalian subject with a higher than average likelihood of developing a disease or a disorder. Exemplary patients can be humans, non-human primates, cats, dogs, pigs, cattle, cats, horses, camels, llamas, goats, sheep, rodents (e.g., mice, rabbits, rats, or guinea pigs) and other mammalians that can benefit from the therapies disclosed herein. Exemplary human patients can be male and / or female. “Patient in need thereof” or “subject in need thereof” is referred to herein as a patient diagnosed with, at risk or having, predetermined to have, or suspected of having a disease or disorder. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 The terms “pathogenic mutation”, “pathogenic variant”, “disease causing mutation”, “disease causing variant”, “deleterious mutation”, or “predisposing mutation” refers to a genetic alteration or mutation that is associated with a disease or disorder or that increases an individual’s susceptibility or predisposition to a certain disease or disorder. In some embodiments, the pathogenic mutation comprises at least one wild-type amino acid substituted by at least one pathogenic amino acid in a protein encoded by a gene. In some embodiments, the pathogenic mutation is in a terminating region (e.g., stop codon). In some embodiments, the pathogenic mutation is in a non-coding region (e.g., intron, promoter, etc.). The terms “protein”, “peptide”, “polypeptide”, and their grammatical equivalents are used interchangeably herein, and refer to a polymer of amino acid residues linked together by peptide (amide) bonds. A protein, peptide, or polypeptide can be naturally occurring, recombinant, or synthetic, or any combination thereof. The term “fusion protein” as used herein refers to a hybrid polypeptide which comprises protein domains from at least two different proteins. The term “recombinant” as used herein in the context of proteins or nucleic acids refers to proteins or nucleic acids that do not occur in nature but are the product of human engineering. For example, in some embodiments, a recombinant protein or nucleic acid molecule comprises an amino acid or nucleotide sequence that comprises at least one, at least two, at least three, at least four, at least five, at least six, or at least seven mutations as compared to any naturally occurring sequence. By “reduces” is meant a negative alteration of at least 10%, 25%, 50%, 75%, or 100%. By “reference” is meant a standard or control condition. In one embodiment, the reference is a wild-type or healthy cell. In one embodiment, the reference is an unedited cell (e.g., an unmodified immune cell). In other embodiments and without limitation, a reference is an untreated cell that is not subjected to a test condition, or is subjected to placebo or normal saline, medium, buffer, and / or a control vector that does not harbor a polynucleotide of interest. In some cases, the reference is an unedited or wild type cell (e.g., a T cell). In some embodiments, the reference is a B2M KO T cell that does not encode a polypeptide or polypeptide variant of interest (e.g., an HLA-E single-chain trimer class-I single-chain trimer of the present disclosure) or encodes a polypeptide that lacks one or more amino acid alterations of the disclosure. A “reference sequence” is a defined sequence used as a basis for sequence comparison. A reference sequence may be a subset of or the entirety of a specified sequence; ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 for example, a segment of a full-length cDNA or gene sequence, or the complete cDNA or gene sequence. For polypeptides, the length of the reference polypeptide sequence will generally be at least about 16 amino acids, at least about 20 amino acids, at least about 25 amino acids, about 35 amino acids, about 50 amino acids, or about 100 amino acids. For nucleic acids, the length of the reference nucleic acid sequence will generally be at least about 50 nucleotides, at least about 60 nucleotides, at least about 75 nucleotides, about 100 nucleotides or about 300 nucleotides or any integer thereabout or therebetween. In some embodiments, a reference sequence is a wild-type sequence of a protein of interest. In other embodiments, a reference sequence is a polynucleotide sequence encoding a wild-type protein. The terms “RNA-programmable nuclease,” and “RNA-guided nuclease” refer to a nuclease that forms a complex with (e.g., binds or associates with) one or more RNA(s) that is not a target for cleavage. In some embodiments, an RNA-programmable nuclease, when in a complex with an RNA, may be referred to as a nuclease-RNA complex. Typically, the bound RNA(s) is referred to as a guide RNA (gRNA). By “specifically binds” is meant a nucleic acid molecule, polypeptide, polypeptide / polynucleotide complex, compound, or molecule that recognizes and binds a polypeptide and / or nucleic acid molecule of the disclosure, but which does not substantially recognize and bind other molecules in a sample, for example, a biological sample. By “substantially identical” is meant a polypeptide or nucleic acid molecule exhibiting at least 50% identity to a reference amino acid sequence. In one embodiment, a reference sequence is a wild-type amino acid or nucleic acid sequence. In another embodiment, a reference sequence is any one of the amino acid or nucleic acid sequences described herein. In one embodiment, such a sequence is at least about 60%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, 99.9%, or even 99.99%, identical at the amino acid level or nucleic acid level to the sequence used for comparison. Sequence identity is typically measured using sequence analysis software (for example, Sequence Analysis Software Package of the Genetics Computer Group, University of Wisconsin Biotechnology Center, 1710 University Avenue, Madison, Wis.53705, BLAST, BESTFIT, GAP, or PILEUP / PRETTYBOX programs). Such software matches identical or similar sequences by assigning degrees of homology to various substitutions, deletions, and / or other modifications. Conservative substitutions typically include substitutions within the following groups: glycine, alanine; valine, isoleucine, leucine; aspartic acid, glutamic acid, asparagine, glutamine; serine, threonine; lysine, arginine; and ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 phenylalanine, tyrosine. In various embodiments, a polypeptide or polynucleotide of the disclsoure comprises a sequence that is at least about 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 99.5% identical to a reference sequence. Nucleic acid molecules useful in the methods of the disclosure include any nucleic acid molecule that encodes a polypeptide of the disclosure or a functional fragment thereof. Such nucleic acid molecules need not be 100% identical with an endogenous nucleic acid sequence but will typically exhibit substantial identity. Polynucleotides having “substantial identity” to an endogenous sequence are typically capable of hybridizing with at least one strand of a double-stranded nucleic acid molecule. Nucleic acid molecules useful in the methods of the disclosure include any nucleic acid molecule that encodes a polypeptide of the disclosure or a functional fragment thereof. Such nucleic acid molecules need not be 100% identical with an endogenous nucleic acid sequence but will typically exhibit substantial identity. Polynucleotides having “substantial identity” to an endogenous sequence are typically capable of hybridizing with at least one strand of a double-stranded nucleic acid molecule. By “hybridize” is meant pair to form a double-stranded molecule between complementary polynucleotide sequences (e.g., a gene described herein), or portions thereof, under various conditions of stringency. (See, e.g., Wahl, G. M. and S. L. Berger (1987) Methods Enzymol.152:399; Kimmel, A. R. (1987) Methods Enzymol.152:507). By “split” is meant divided into two or more fragments. A “split polypeptide” or “split protein” refers to a protein that is provided as an N- terminal fragment and a C-terminal fragment translated as two separate polypeptides from a nucleotide sequence(s). The polypeptides corresponding to the N-terminal portion and the C- terminal portion of the split protein may be spliced in some embodiments to form a “reconstituted” protein. In embodiments, the split polypeptide is a nucleic acid programmable DNA binding protein (e.g. a Cas9) or a base editor. The term “target site” refers to a nucleotide sequence or nucleobase of interest within a nucleic acid molecule that is modified. In embodiments, the modification is deamination of a base. The deaminase can be a cytidine or an adenine deaminase. The fusion protein or base editing complex comprising a deaminase may comprise a dCas9-adenosine deaminase fusion protein, a Cas12b-adenosine deaminase fusion, or a base editor disclosed herein. As used herein, the terms “treat,” treating,” “treatment,” and the like refer to reducing or ameliorating a disorder and / or symptoms associated therewith or obtaining a desired pharmacologic and / or physiologic effect. It will be appreciated that, although not precluded, treating a disorder or condition does not require that the disorder, condition or symptoms ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 associated therewith be completely eliminated. In some embodiments, the effect is therapeutic, i.e., without limitation, the effect partially or completely reduces, diminishes, abrogates, abates, alleviates, reduces the intensity of, or cures a disease and / or adverse symptom attributable to the disease. In some embodiments, the effect is preventative, i.e., the effect protects or prevents an occurrence or reoccurrence of a disease or condition. To this end, the presently disclosed methods comprise administering a therapeutically effective amount of a composition as described herein. By “uracil glycosylase inhibitor” or “UGI” is meant an agent that inhibits the uracil- excision repair system. Base editors comprising a cytidine deaminase convert cytosine to uracil, which is then converted to thymine through DNA replication or repair. In various embodiments, a uracil DNA glycosylase (UGI) prevent base excision repair which changes the U back to a C. In some instances, contacting a cell and / or polynucleotide with a UGI and a base editor prevents base excision repair which changes the U back to a C. An exemplary UGI comprises an amino acid sequence as follows: >splP14739IUNGI_BPPB2 Uracil-DNA glycosylase inhibitor MTNLSDIIEKETGKQLVIQESILMLPEEVEEVIGNKPESDILVHTAYDESTDENVMLLTSDA PEYKPWALVIQDSNGENKIKML (SEQ ID NO: 231). In some embodiments, the agent inhibiting the uracil-excision repair system is a uracil stabilizing protein (USP). See, e.g., WO 2022015969 A1, incorporated herein by reference. As used herein, the term "vector" refers to a means of introducing a nucleic acid molecule into a cell, resulting in a transformed cell. Vectors include plasmids, transposons, phages, viruses, liposomes, lipid nanoparticles, and episomes. Ranges provided herein are understood to be shorthand for all of the values within the range. For example, a range of 1 to 50 is understood to include any number, combination of numbers, or sub-range from the group consisting 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, or 50. The recitation of a listing of chemical groups in any definition of a variable herein includes definitions of that variable as any single group or combination of listed groups. The recitation of an embodiment for a variable or aspect herein includes that embodiment as any single embodiment or in combination with any other embodiments or portions thereof. All terms are intended to be understood as they would be understood by a person skilled in the art. Unless defined otherwise, all technical and scientific terms used herein have ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 the same meaning as commonly understood by one of ordinary skill in the art to which the disclosure pertains In this application, the use of the singular includes the plural unless specifically stated otherwise. It must be noted that, as used in the specification, the singular forms “a,” “an” and “the” include plural referents unless the context clearly dictates otherwise. In this application, the use of “or” means “and / or” unless stated otherwise. Furthermore, use of the term “including” as well as other forms, such as “include”, “includes,” and “included,” is not limiting. As used in this specification and claim(s), the words “comprising” (and any form of comprising, such as “comprise” and “comprises”), “having” (and any form of having, such as “have” and “has”), “including” (and any form of including, such as “includes” and “include”) or “containing” (and any form of containing, such as “contains” and “contain”) are inclusive or open-ended. This wording indicates that specified elements, features, components, and / or method steps are present, but does not exclude the presence of other elements, features, components, and / or method steps. Any embodiments specified as “comprising” a particular component(s) or element(s) are also contemplated as “consisting of” or “consisting essentially of” the particular component(s) or element(s) in some embodiments. It is contemplated that any embodiment discussed in this specification can be implemented with respect to any method or composition of the present disclosure, and vice versa. Furthermore, compositions of the present disclosure can be used to achieve methods of the present disclosure. The term “about” or “approximately” means within an acceptable error range for the particular value as determined by one of ordinary skill in the art, which will depend in part on how the value is measured or determined, i.e., the limitations of the measurement system. Reference in the specification to “some embodiments,” “an embodiment,” “one embodiment” or “other embodiments” means that a particular feature, structure, or characteristic described in connection with the embodiments is included in at least some embodiments, but not necessarily all embodiments, of the present disclosures. BRIEF DESCRIPTION OF THE DRAWINGS FIG.1 provides a plot demonstrating that disruption of cluster of differentiation 58 (CD58) polypeptide expression and expression of an human leukocyte antigen E (HLA-E) single-chain trimer of the disclosure in human leukocyte antigen I (HLA-I) deficient T cells (i.e., T cells edited to knock out expression of beta-2-microglobulin (B2M)) reduced in vitro ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 natural killer (NK) cell-mediated lysis of the T cells. In FIG.1, the term “B2MKO” indicates T cells that were base edited to knock out expression of beta-2-microglobulin, the term “CD58KO” indicates T cells that were base edited to knock out expression of a cluster of differentiation 58 (CD58) polypeptide, and the term “HLA-E SCT” indicates T cells that express the HLA-E single-chain trimer polypeptide BTxCM525 (see Tables 8A, 8B, 9A, and 9B). In FIG.1, the y-axis indicates the percent of the T cells that were lysed at a particular effector (i.e., natural killer cells; “E”) to target (i.e., T cells; “T”) ratio indicated on the x-axis. FIGs.2A-2I provide schematics, a graph, bar graphs, histograms and fluorescence activated cell sorting (FACS) plots demonstrating that b2M-deficient T cells evaded T cell allorejection and were susceptible to NK cell lysis. FIG.2A provides a schematic demonstrating that the status of HLA class-I expression dictates susceptibility of allogeneic T cells to rejection by T cells or NK cells from an unrelated donor. FIG.2B provides a schematic showing use of a b2M-specific single guide (sg) RNA to disrupt the splice donor site at the exon-intron junction to knock out expression of b2M (b2MKO). FIG.2C provides a bar graph showing the frequency of on-target A>G nucleotide conversion by next- generation sequencing in primary human T cells base-edited using a base editor system containing ABE8.20 and b2M-specific sgRNA. Circles indicate 4 independent T cell donors. FIG.2D provides a histogram showing surface expression of HLA class-I in b2MKO and unmodified T cells. FIG.2E and FIG.2F provide the results of a T cell mixed leukocyte assay . FACS plots (FIG.2E) and summarized data (FIG.2F) are provided for the frequency of b2MKO and unmodified T cells 48 hours post-culture in triplicate with HLA-mismatched T cells at the indicated effector-to-target (E / T) ratios. FIG.2G provides a graph showing the frequency of CD107a+NK cells after stimulation with b2MKO and unmodified T cells.3 independent unrelated NK cell donors were graphed in duplicate, generating six lines. FIG. 2H and FIG.2I provide a FACS plot and a bar graph showing the results of an NK cell cytotoxicity assay. FACS plots show frequency (FIG.2H) and the bar graph presenting summarized data shows specific lysis (FIG.2I) of b2MKO and unmodified T cells 48 hours post-culture with NK cells at the indicated E / T ratios. Circles represent 4 independent NK cell donors in duplicate. For all data, bars represent mean and error bars indicate ±s.e.m. The nucleotide sequences shown in FIG.2B, in order of occurrence, are AGCCCAAGATAGTTAAGTGGGGTAAGTCT (SEQ ID NO: 622) and AGCCCAAGATAGTTAAGTGGGGCAAGTCT (SEQ ID NO: 623). ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 FIGs.3A-3J provide schematics, FACS plots, graphs, histograms and bar graphs demonstrating that CD4 domains augmented scHLA-E expression and inhibited NK cell lysis T cells. FIG.3A provides a schematic showing how expression of an HLA-E single-chain (sc) polypeptide in β2MKOT cells may inhibit NK cells by engaging the NKG2A / CD94 heterodimer. FIG.3B provides a schematic detailing components of scHLA- E fusion constructs, including scHLA-E dimer (D), scHLA-E trimer (T), and scHLA-E polypeptides containing the CD8 (8) and CD4 (4) transmembrane domain and truncated cytoplasmic regions. FIG.3C and FIG.3D show an analysis of β2MKOT cells transduced with an equivalent titer of lentivirus encoding unique scHLA-E variants and mDHFR. FACS plots (FIG.3C) and a bar graph presenting summarized data (FIG.3D) demonstrate cell- surface expression of the scHLA-E variants and fold-change in geometric median fluorescence intensity (GMFI) of HLA-E on transduced β2MKOT cells relative to unmodified T cells. HLA-E expression was quantified 11 days post-transduction. Circles represent 3 independent T cell donors in duplicate. Histograms (FIG.3E) and a bar graphs presenting summarized data (FIG.3F) show GMFI of scHLA-E variants bound to recombinant human NKG2A / CD94 heterodimer. Circles represent 3 independent T cell donors. Frequency of NKG2A+NK cells and total CD56+NK cells that upregulated expression of CD107a (FIG. 3G) and TNFα (FIG.3H) post-stimulation with β2MKOT cells that were non-transduced or expressed scHLA-E4. Circles represent 4 independent NK cell donors in duplicate. FIG.3I provides a graph showing the result of a NK cell cytotoxcity assay. In particular, the specific lysis of β2MKOT cells that were non-transduced or expressed scHLA-E4at 48-hours post- culture with NK cells at the indicated E / T ratios. Circles represent 3 independent NK cell donors in duplicate. FIG.3J provides a plot showing the percent change in frequency of NKG2A+ NK cells and percentage change in frequency of total responding NK cells following stimulation with scHLA-E4B2MKOT cells, where the percent changes are relative to stimulation with non-transduced B2MKO T cells. Symbols individually represent cells from each of 8 independent NK cell donors. For all data, bars represent mean and error bars indicate ±s.e.m. For FIGs.3D and FIGs.3G-3J, Wilcoxon matched-pairs signed rank test was used to calculate significance. The amino acid sequences shown in FIG.3B are GGGGSGGGGSGGGGSGGGGS ((G4S)4; SEQ ID NO: 624) and GGGGSGGGGSGGGGS ((G4S)3; SEQ ID NO: 625). FIGs.4A-4I provide schematics, FACS plots, bar graphs, and a heatmap demonstrating that VL9 epitope variants modulated surface expression and NK cell inhibitory ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 potential of scHLA-E4polypeptides. FIG.4A provides a schematic of a scHLA-E4polypeptide and VL9 epitope variants derived from signal sequences of HLA-G*01 and representative HLA class-Ia alleles. FIG.4B and FIG.4C present an analysis of b2MKOT cells transduced with an equivalent titer of lentivirus encoding each scHLA-E4VL9 variant and HLA-E cell-surface expression that were quantified 11 days post-transduction. FIG.4B provides FACS plots showing cell-surface expression of each scHLA-E4VL9 variant and corresponding GMFI of HLA-E on b2MKOT cells. FIG.4C provides a heatmap showing GMFI of HLA-E expression in b2MKOT cells expressing each scHLA-E4VL9 variant as well as non-transduced b2MKOT cells and unmodified T cells. Data represents the mean of 3 independent T cell donors in duplicate. FIGs.4D-4H provide an analysis of NK cells from unrelated donors that were stimulated with b2MKOT cells that were non-transduced or expressed unique scHLA-E4VL9 variants. FIG.4D provides FACS plots showing frequency of NKG2A+NK cells that expressed CD107a and TNFα post-stimulation with b2MKOT cells that were non-transduced or expressed scHLA-E4v4. FIGs.4E-4H provide bar graphs presenting summarized data that indicates the frequency of CD107a+(FIG.4E) and TNFα+(FIG.4F) NKG2A+NK cells, and total CD107a+(FIG.4G) and TNFα+(FIG.4H) CD56+NK cells. Symbols represent data from 5 (FIG.4E, FIG.4F) and 4 (FIG.4G, FIG.4H) independent NK cell donors in duplicate. FIG.4I provides the results of an NK cell cytotoxicity assay, in particular, specific lysis of b2MKOT cells that were non-transduced or expressed unique scHLA-E4VL9 variants at 48-hours post-culture with NK cells at the indicated E / T ratios. Circles represent 5 independent NK cell donors in duplicate. For all data, bars represent mean and error bars indicate ±s.e.m. For FIG.4C, Wilcoxon matched- pairs signed rank test was used to calculate significance. For FIGs.4E-I, statistical significance between b2MKOT cells that were non-transduced and each scHLA-E4VL9 variant was calculated using Wilcoxon matched-pairs signed rank test, while Friedman’s test with Dunn’s test for multiple comparisons calculated statistical significance between scHLA- E4VL9 variants. The amino acid sequences listed in FIG.4A, in order of occurrence, are VMAPRTLFL (SEQ ID NO: 605),VMAPRTLLL (SEQ ID NO: 434),VMAPRTLVL (SEQ ID NO: 435),VMAPRTLIL (SEQ ID NO: 436),VMAPRALLL (SEQ ID NO: 437),VTAPRTVLL (SEQ ID NO: 438),VMAPRTVLL (SEQ ID NO: 439), and VTAPRTLLL (SEQ ID NO: 440). FIGs.5A-5H provide schematics, graphs, and bar graphs showing that disulfide trap mutations improved surface expression and NK cell inhibitory potential of scHLA-E4variants. FIG.5A provides a schematic of a scHLA-E4polypeptide that was either non- ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 mutated or comprised disulfide trap (dt) mutations in the (G4S)3 (SEQ ID NO: 625) flexible linker and HLA-E heavy chain. FIG.5B presents a bar graph showing GMFI of HLA-E in b2MKOT cells that expressed a unique scHLA-E4VL9 variant or the corresponding dtHLA- E4VL9 variant. Circles represent 3 independent T cells donors in duplicate. FIG.5C and FIG.5D illustrate the frequency of CD107a+(FIG.5C) and TNFα+(FIG.5D) NKG2A+NK cells post-stimulation with b2MKOT cells that were non-transduced or expressed unique a dtHLA-E4VL9 variant. Circles represent 5 independent T cell donors in duplicate. FIG.5E shows the results of an NK cell cytotoxcity assay demonstrating specific lysis of b2MKOT cells that were non-transduced or expressed a unique dtHLA-E4VL9 variant at 48-hours post-culture with NK cells at the indicated E / T ratios. Circles represent 5 independent NK cell donors in duplicate. FIG.5F and FIG.5G provide the frequency of CD107a+(FIG.5F) and TNFα+(FIG.5G) NKG2A+NK cells post-stimulation with b2MKOT cells that expressed a unique scHLA-E4VL9 variant or the corresponding dtHLA-E4VL9 variant. Circles represent 5 independent T cell donors in duplicate. FIG.5H shows the results of an NK cell cytotoxcity assay demonstrating specific lysis of b2MKOT cells that expressed a unique scHLA-E4VL9 variant or the corresponding dtHLA-E4VL9 variant 48 hours post-culture with NK cells at the indicated E / T ratios. Circles represent 4 independent NK cell donors in duplicate. For all data, bars represent mean and error bars indicate ±s.e.m. For FIGs.5B-5H, Wilcoxon matched-pairs signed rank test was used to calculate significance. The amino acid sequences shown in FIG.5A are GGGGSGGGGSGGGGS ((G4S)3; SEQ ID NO: 625), GGGGSGGGGSGGGGSGGGGS ((G4S)4; SEQ ID NO: 624), and GCGGSGGGGSGGGGS ((GCGGS(G4S)2; SEQ ID NO: 461. FIGs.6A-6F provide a histogram, FACS plots, and graphs showing dtHLA-E4polypeptides bound to HLA-A and HLA-C derived VL9 epitopes mitigated activation of NKG2C+NK cells. FIG.6A provides a histogram which illustrates binding of recombinant human NKG2C / CD94 heterodimer to unmodified T cells and b2MKOT cells that expressed dtHLA-E4v1. FIG.6B and FIG.6C provide FACS plots (FIG.6B) and a bar graph presenting summarized data (FIG.6C) that show the frequency of CD107a+NKG2C+NK cells post-stimulation with b2MKOT cells that were non-transduced or expressed dtHLA-E VL9 variants. Circles represent 6 independent NK cell donors. FIG.6D and FIG.6E present FACS plots (FIG.6D) and a graph presenting summarized data (FIG.6E) that show the frequency of NKG2A and NKG2C expression of total NK cells from donors classified as NKG2Clowand NKG2Chighbased on frequency of NKG2C+NK cells being less or greater ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 than 10%, respectively. Each symbol represents an independent NK cell donor. FIG.6F provides a bar graph showing the results of an NK cell cytotoxcity assay demonstrating specific lysis of b2MKOT cells that were non-transduced or expressed a unique dtHLA-E4VL9 variant 48 hours post-culture with NK cells from NKG2Chighdonors at the indicated E / T ratios. Symbols represent 4 independent NK cell donors in duplicate. For all data, bars represent mean and error bars indicate ±s.e.m. For FIG.6C and FIG.6F, Wilcoxon matched- pairs signed rank test was used to calculate significance between non-transduced and dtHLA- E4variant expressing b2MKOT cells. For FIG.6C, Friedman’s test with Dunn’s test for multiple comparisons calculated statistical significance between dtHLA-E4VL9 variants. FIGs.7A-7J provide a schematic, FACS plots, and bar graphs showing hypoimmunogenic dtHLA-E4evaded HLA-E-reactive T cell responses. FIG.7A provides a bar graph showing the frequency of responding CD107a+and TNFα+CD8+T cells after in vitro stimulation with the indicated aAPC.dtHLA-E4variant. FIG.7B and FIG.7C show the results after T cells were stimulated aAPC cells expressing a unique dtHLA-E4variant and cultured for 1-week. FACS plots (FIG.7B) and a bar graph presenting summarized data (FIG.7C) show the frequency of CD107a+and TNFα+CD8+T cells post-restimulation with the appropriate aAPC and K.86 cell lines. FIGs.7D-7F present graphs showing the results after T cells were stimulated with K.86 cells, aAPC.hypoA2 and aAPC.scA2 cells and then cultured for 1-week. FIG.7D presents a graph showing the total CD8+T cells enumerated after 7-days. Dotted line indicates average CD8+T cell count when cultured in the absence of K-562 cells. FIG.7E and FIG.7F present graphs showing the frequency of CD107a+(FIG. 7E) and TNFα+(FIG.7F) CD8+T cells post-restimulation with aAPC.scA2 and aAPC.hypoA2 cells. Circles represents 9 independent T cell donors. FIG.7G provides a schematic showing amino acid alignment of the a3 domain region for the indicated HLA class-I alleles. FIG.7H and FIG.7I show the results for T cells stimulated with aAPC.dtHLA-E4v4cells for 1-week in culture. FACS plots (FIG.7H) and a graph presenting summarized data (FIG.7I) show the frequency of CD107a+and TNFα+CD8+T cells post- restimulation with aAPC.dtHLA-E4v4and aAPC.hypoHLA-E4v4cells. FIG.7J presents a graph of data from an NK cell cytotoxcity assay showing specific lysis of b2MKOT cells that were non-transduced or expressed dtHLA-E4v4or hypoHLA-E4v4. Circles represent mean of 3 independent NK cell donors in duplicate. For FIGs.7A, 7C, and 7I, symbols represent 9 independent donors in duplicate. For FIGs.7A, 7C, 7E, 7F, and 7I, values are background subtracted from restimulation with K.86 cells. For FIGs.7E, 7F, and 7I, Wilcoxon matched- pairs signed rank test was used to calculate significance. For all data, bars represent mean and ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 error pars indicate ±s.e.m. The amino acid sequence shown in FIG.7G is GEDQTQDTELVETRPAGDGTFQKWAAVVV (SEQ ID NO: 626). FIGs.8A-8D provide graphs showing that CD4 transmembrane domain andcytoplasmic regions enhanced surface expression of scHLA-E4. T cells weretransduced with an equivalent titer of lentiviral vector encoding single-chain (sc) HLA-E dimer (D), scHLA-E trimer (T), or scHLA-E constructs comprising the transmembrane domain and truncated cytoplasmic regions of CD8α (8) or CD4 (4) coreceptors. FIG.8A provides a bar graph showing the geometric median fluorescence intensity (GMFI) of HLA-E surface expression on transduced T cells at 8-days post-transduction. FIG.8B provides agraph showing the fold-change in HLA-E GMFI over unmodified T cells of T cellsexpressing a scHLA-E variant at 4-, 6-, and 8-days post-transduction. FIG.8C provides agraph showing the fold-change in HLA-E GMFI over unmodified T cells of CD8+and CD4+T cells expressing a scHLA-E variant at 11-days post-transduction. FIG. 8Dprovides a plot showing the frequency of scHLA-E4-positive ß2MKOT cells 4-days aftermethotrexate (MTX) addition. Circles indicate 3 independent T cell donors. For FIGs.8A- 8C, circles indicate 3 independent T cell donors in duplicate, bars and lines represent mean, and error bars show ±s.e.m. Wilcoxon matched pairs-signed rank test was used to calculate significance. FIGs.9A-9E provide graphs showing that VL9 epitope stabilization enhanced scHLA-E4NK cell inhibitory function without increasing NKG2C+NK cell stimulation. FIGs.9A-9D provide bar graphs and graphs showing the frequency of total NK cells that upregulated expression of CD107a (FIG.9A and FIG.9C) and TNFα (FIG.9B and FIG. 9D) post-stimulation with b2MKOT cells that were non-transduced or expressed unique disulfide trap (dt) HLA-E4VL9 variants (FIG.9A and FIG.9B) or the corresponding scHLA-E4VL9 variant (FIG.9C and FIG.9D). Circles represent 5 independent T cell donors in duplicate. FIG.9E provides a graph showing the frequency of CD107a+NKG2C+NK cells post-stimulation with b2MKOT cells that expressed unique disulfide trap (dt) HLA- E4VL9 variants or the corresponding scHLA-E4VL9 variants. Circles represent 3 independent T cell donors in duplicate for dt- and sc-HLA-E4v1, and 4 independent T cell donors in duplicate for all other polypeptides. Bars indicate mean and error bars show ±s.e.m. Wilcoxon matched pairs-signed rank test was used to calculate significance. FIGs.10A-10E provide histograms and graphs showing that CD4+ T cells did not react against aAPCs. FIGs.10A and 10B provide histograms showing K-562 cells transduced ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 with lentiviral constructs encoding CD86 and the indicated scHLA polypeptide. Histograms show cell-surface expression of b2M (FIG.10A), which denotes the scHLA polypeptide, and CD86 (FIG.10B) relative to non-transduced K-562 cells (black line). FIGs.10C and 10D present bar graphs presenting data for Bulk T cells first stimulated with aAPC.dtHLA-E4variants and then restimulated with their respective aAPC or K.86 control cells. The bar graphs show frequency of CD107a+(FIG.10C) and TNFα+(FIG.10D) CD4+T cells after restimulation. Data represent 9 independent T cell donors in duplicate and values are background subtracted from restimulation with K.86 cells. Bars indicate mean and error bars show ±s.e.m. FIG.10E provides a graph showing bulk T cells stimulated for 1-week in culture with aAPC.scA2, aAPC.hypoA2 or K.86 cell lines. Total CD4+T cells were quantified following the activation period by flow cytometry. Symbols represent 9 independent T cell donors that were either HLA-A*02+or HLA-A*02-. DETAILED DESCRIPTION The present disclosure features genetically modified allogeneic cells (e.g., immune cells, such as T- or NK-cells), and methods for producing and using these modified cells (e.g., T cells or NK cells) for the treatment of disease (e.g., neoplasia, autoimmune disease, etc.). The disclosure is based, at least in part, on the discovery described further in the Examples provided herein that resistance to lysis by natural killer (NK) cells by T cells deficient in expression of HLA class-I polypeptides is increased by modifying the cells to knock out endogenous expression of CD58 and / or express an HLA-E single-chain tetramer (SCT) of the disclosure. Further, the disclosure is also based, at least in part, on the discovery that the HLA-E single-chain tetramers containing a cognate peptide selected from those listed in Table 1 may facilitate increased resistance to lysis by NK cells relative to single-chain tetramers containing alternative cognate peptides previously available to the skilled practitioner. HUMAN LEUKOCYTE ANTIGEN (HLA) SINGLE-CHAIN TRIMERS (SCTs) The present disclosure provides human leukocyte antigen (HLA) single-chain trimers (SCTs) (e.g., HLA-E single chain trimers). In some instances, the HLA single chain trimers comprise an HLA-E domain (see, e.g., Tables 8A, 8B, 9A, and 9B and Example 1), a beta-2- microglobulin domain, and a cognate peptide (cPep) (alternatively referred to as a “loading peptide”). In some embodiments, the HLA single-chain trimer is membrane-bound (e.g., the ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 HLA single-chain trimer contains a transmembrane domain, such as a transmembrane domain derived from CD4) or the HLA single-chain trimer is secreted by a cell. Expression of the HLA SCTs in an immune cell (e.g., a B2M knock-out (KO) immune cell) results in increased resistance to lysis by alloreactive T cells. In some instances, a modified immune cell expressing an HLA single chain trimer includes modifications to reduce or eliminate endogenous expression of β2M and / or CD58. The various domains of an HLA construct can be connected by linkers, such as those provided herein. The length of the linkers may be elongated or truncated by about or at least about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, or 50 amino acids. In various instances, the linker is a Gly / Ser-linker (GS-linker). The length of the linkers may be about, at least about, or no more than about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 75, or 100 amino acids. In some embodiments, the GS-linker is altered to include a cysteine amino acid. In some embodiments, a GS-linker adjacent to and N-terminal or C-terminal to the cognate peptide contains a cysteine amino acid and the HLA-E domain contains a cysteine amino acid capable of forming a disulfide bridge with the cysteine in the GS-linker. In embodiments, formation of this disulfide bridge constitutes the formation of a “disulfide trap” as described by, e.g., Hansen, et al. Trends Immunol 31:363-369 (2010), the disclosure of which is incorporated herein in its entirety for all purposes, that mediates the sustained insertion (alternatively “stapling” or “trapping”) of the cognate peptide within a major histocompatibility complex I (MHCI) groove of the HLA-E domain. In various embodiments, the GS linker comprises the amino acid sequence provided at 3b of Table 9A and / or the HLA-E domain comprises the amino acid sequence provided at 6b of Table 9A. In some instances, the HLA SCT comprises an N-terminal signal peptide (e.g., a β2M signal peptide). Any signal peptide known in the art and suitable for secretion and / or membrane-localization of a polypeptide is suitable in the HLA single chain trimers provided herein. In some instances, the HLA single chain trimer contains a transmembrane domain (e.g., a Type I or Type II transmembrane domain; a CD4 transmembrane domain; an HLA heavy chain transmembrane domain, such as a heterologous HLA heavy chain transmembrane domain), optionally at an N-terminal or C-terminal portion thereof. In some embodiments, the HLA single trimer contains a Type II transmembrane domain. In some instances, the HLA-E domain is derived from an HLA-E polypeptide from which a transmembrane domain has been deleted. In some instances, the HLA single-chain trimer ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 contains a wild-type HLA heavy chain transmembrane domain. As described in Chou and Elrod, Proteins: Structure, Function, and Genetics 34:137-153 (1999), a Type I membrane protein is a single-pass transmembrane protein having an extracellular (or luminal) N- terminus and a cytoplasmic C terminus for a cell (or organelle) membrane, and a Type I membrane protein is a single-pass transmembrane protein having an extracellular (or luminal) C-terminus and a cytoplasmic N-terminus for a cell (or organelle) membrane. In embodiments, an HLA construct contains any one or more of the domains described in 9A and / or in Example 1, functional fragments thereof, or extensions thereof, where the functional fragment may correspond to an N-terminal and / or C-terminal truncation by about, at least about, and / or no more than about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, or 25 amino acids, and where the extension may correspond to an N-terminal and / or C-terminal extension by about, at least about, and / or no more than about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, or 25 amino acids. In some embodiments, the HLA single-chain trimer contains one of the following domain arrangements from N-terminus to C-terminus: signal peptide-cPep-linker-B2M domain-linker-HLA-E domain; signal peptide-cPep-linker-B2M domain-linker-HLA-X domain-transmembrane domain. In some instances, any one of these domain arrangements can be modified to not include any β2M domain. Non-limiting examples of cognate peptide (cPep) amino acid sequences include those listed in Tables 1 and 8A. In some cases, the cPep assists in trimerization of a HLA single- chain trimer. In various instances, trimerization of the HLA single-chain trimer increases inhibition of lysis of a cell by an NK cell. Table 1. Representative cognate peptide (cPep) amino acid sequences. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 The transmembrane domain traverses a cell’s lipid bilayer cellular membrane. In some embodiments, this domain is derived from a receptor (e.g., an antigen receptor) having a transmembrane domain, while in other embodiments, this domain is synthetic. In some cases, the transmembrane domain is an HLA-A, -B, -C, or -E transmembrane domain (e.g., a wild-type HLA-A, -B. -C, or -E transmembrane domain). In some embodiments, the transmembrane domain may be derived from a non-human transmembrane domain and, in some embodiments, humanized. By “humanized” is meant having the sequence of the nucleic acid encoding the transmembrane domain optimized such that it is more reliably or efficiently expressed in a human subject. In some embodiments, the transmembrane domain is derived from another transmembrane protein expressed in a human immune effector cell. Examples of such proteins include, but are not limited to, subunits of the T cell receptor (TCR) complex, PD1, or any of the Cluster of Differentiation proteins (e.g., CD4), or other proteins, that are expressed in the immune effector cell and that have a transmembrane domain. In some embodiments, the transmembrane domain will be synthetic, and such sequences will comprise many hydrophobic residues. Transmembrane domains for use in the disclosed HLA constructs can include at least the transmembrane region(s) of) the alpha, beta or zeta chain of the T-cell receptor, CD28, CD3 epsilon, CD45, CD4, CD5, CD8, CD9, CD16, CD22, CD33, CD37, CD64, CD80, CD86, CD134, CD137, CD154. In some embodiments, the transmembrane domain is derived from CD4, CD8α, CD28 and CD3ζ. In embodiments, the HLA single-chain trimers further comprise an effector domain that functions to improve inhibition of alloreactive T cells and / or NK cells. The HLA single chain trimers fused to the effector domain can be referred to as “functionalized” single-chain ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 trimers. In some cases, the effector domain is fused to the N-terminus or C-terminus of a HLA single-chain trimer. Non-limiting examples of effector domains include PD-L1 or CTLA4 extracellular domains or a CD47 polypeptide. Further non-limiting examples of effector domains include additional single-chain trimers, which in some instances do not contain any transmembrane domain. In some instances, the effector domain is a membrane- bound domain or a transmembrane domain. If the effector domain is a transmembrane domain or contains a transmembrane domain, it can be advantageous to delete a transmembrane domain from the HLA single-chain trimer to which the effector domain is fused (e.g., delete a transmembrane domain from the HLA heavy-chain domain). In some cases, the effector domain is fused to the single-chain trimer via a linker peptide. In some embodiments, the fusion polypeptide further comprises a tag or marker (e.g., a fluorescent protein, such as green fluorescent protein, a His tag, or a FLAG tag). Non- limiting examples of peptide tags include an ALFA-tag, an AviTag, a C-tag, a Calmodulin- tag, an iCap Tag™, a polyglutamate tag, a polyarginine tag, an E-tag, a FLAG-tag, an HA- tag, a His-tag, a Myc-tag, an NE-tag, a RHO1D4-tag, an S-tag, an SBP-tag, a Softag 1, a Softag 3, a Spot-tag, a Strep-tag, a T7-tag, a Ty-tag, a TC-tag, a V5-tag, a VSV-tag, an Xpress-tag, Isopeptag, SpyTag, SnoopTag, DogTag, SdyTag, BCCP, a glutathione-S- transferase-tag, a GFP-tag, a HaloTag, a SNAP-tag, a CLIP-tag, a HUH-tag, a maltose- binding protein-tag, a Nus-tag, a thioredoxin-tag, an Fc-tag, and a carbohydrate recognition domain tag. CAR-T CELL THERAPIES The present disclosure provides immune cells (e.g., T- or NK-cells) modified using nucleobase editors and / or nucleases described herein. The modified immune cells may express chimeric antigen receptors (CARs) (e.g., CAR-T cells). Modification of immune cells to express a chimeric antigen receptor can enhance an immune cell’s immunoreactive activity, wherein the chimeric antigen receptor has an affinity for an epitope on an antigen, wherein the antigen is associated with an altered fitness of an organism. For example, the chimeric antigen receptor can have an affinity for an epitope on a protein expressed in a diseased cell. In embodiments, the immune cells contain a kill switch (e.g., RQR8 or an antibody- drug conjugate target). In some cases, a chimeric antigen receptor expressed by the cell contains the kill switch. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Some aspects of the present disclosure provide for immune cells comprising a chimeric antigen receptor (CAR) and an altered endogenous gene that provides increased persistence, resistance to fratricide, enhances immune cell function, resistance to immunosuppression or inhibition, or a combination thereof. In some embodiments, the altered endogenous gene may be created by base editing. In some embodiments, the base editing may reduce or attenuate the gene expression. In some embodiments, the base editing may reduce or attenuate the gene activation. In some embodiments, the base editing may reduce or attenuate the functionality of the gene product. In some other embodiments, the base editing may activate or enhance the gene expression. In some embodiments, the base editing may increase the functionality of the gene product. In some embodiments, the altered endogenous gene may be modified or edited in an exon, an intron, an exon-intron injunction, or a regulatory element thereof. The modification may be edit to a single nucleobase in a gene or a regulatory element thereof. The modification may be in a exon, more than one exons, an intron, or more than one introns, or a combination thereof. The modification may be in an open reading frame of a gene. The modification may be in an untranslated region of the gene, for example, a 3'-UTR or a 5'-UTR. In some embodiments, the modification is in a regulatory element of an endogenous gene. In some embodiments, the modification is in a promoter, an enhancer, an operator, a silencer, an insulator, a terminator, a transcription initiation sequence, a translation initiation sequence (e.g., a Kozak sequence), or any combination thereof. In some embodiments, each edited gene may comprise a single base edit. In some embodiments, each edited gene may comprise multiple base edits at different regions of the gene. In some embodiments, a single modification event (such as electroporation), may introduce one or more gene edits. In some embodiments at least one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, twenty or more edits may be introduced in one or more genes simultaneously. In some embodiments, an immune cell, including but not limited to any immune cell comprising an edited gene selected from any of the aforementioned gene edits, can be edited to generate mutations in other genes that enhance the CAR-T’s function or reduce immunosuppression or inhibition of the cell. In some embodiments, an immune cell of the disclosure comprises a chimeric antigen receptor and one or more edited genes. The one or more genes may be selected from beta-2- microglobulin and cluster of differentiation 58. An edited gene may be an immune response regulation gene, an immunogenic gene, a checkpoint inhibitor gene, a gene involved in ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 immune responses, a cell surface marker, e.g., a T cell surface marker, or any combination thereof. In some embodiments, an immune cell comprises a chimeric antigen receptor and an edited gene that is associated with activated T cell proliferation, alpha-beta T cell activation, gamma-delta T cell activation, positive regulation of T cell proliferation, negative regulation of T-helper cell proliferation or differentiation, or their regulatory elements thereof, or combinations thereof. In embodiments, one or more genes are modified in an immune effector cell so that the modified immune cell has a reduced level of, lacks, or have virtually undetectable levels of beta-2-microglobulin and / or one or more of the following polypeptides relative to an unmodified immune cell: B cell leukemia / lymphoma 11b (Bcl11b); B cell leukemia / lymphoma 2 related protein A1d (Bcl2a1d); B cell leukemia / lymphoma 6 (Bcl6); butyrophilin-like 6 (Btnl6); CD151 antigen (Cd151); chemokine (C-C motif) receptor 7 (Ccr7); discs large MAGUK scaffold protein 5 (Dlg5); erythropoietin( Epo); G protein- coupled receptor 18 (Gpr18); interferon alpha 15 (Ifna15); interleukin 6 signal transducer (Il6st); interleukin 7 receptor (Il7r); Janus kinase 3 (Jak3); membrane associated ring-CH- type finger 7 (Marchf7); NCK associated protein 1 like (Nckap1l); phospholipase A2, group IIF (Pla2g2f); runt related transcription factor 3 (Runx3); Signal-regulatory protein beta 1B (Sirpb1b); transforming growth factor, beta 1 (Tgfb1); tumor necrosis factor (ligand) superfamily, member 14 (Tnfsf14); tumor necrosis factor (ligand) superfamily, member 18 (Tnfsf18); tumor necrosis factor (ligand) superfamily, member 8 (Tnfsf8); zinc finger CCCH type containing 8 (Zc3h8); (Rac family small GTPase 2); (Slc4a1); 5-azacytidine induced gene 2 (Azi2); a disintegrin and metalloprotease domain 17 (Adam 17); a disintegrin and metalloprotease domain 8 (Adam8); Acetyl-CoA Acetyltransferase 1 (ACAT1); ACLY; adapter related protein complex 3 beta 1 sububit (Ap3b1); adapter related protein complex 3 delta 1 sububit (Ap3d1); adenosine A2a receptor (Adora2a); adenosine deaminase (Ada); adenosine kinase (Adk); adenosine regulating molecule 1 (Adrm1); advanced glycosylation end product-specific receptor (Ager) allograft inflammatory factor 1 (Aif1); AKT1; AKT2; amyloid beta (A4) precursor protein-binding family B member 1 interacting protein (Apbb1ip); ankyrin repeat and LEM domain (Ankle1); annecin A1 (Anxa1); arginase liver (Arg 1); arginase type II (Arg 2); AtPase Cu++ transporting, alpha polypeptide (Atp7a); autoimmune regulator (Aire); autophagy related 5 (Atg5); AXL; B and T Lymphocyte Associated (BTLA); B and T lymphocyte associated (Btla); B cell leukemia / lymphoma 10 (Bcl10); B cell leukemia / lymphoma 11a (Bcl11a); B cell leukemia / lymphoma 2 (Bcl2); B cell leukemia / lymphoma 3 (Bcl3); basic leucine zipper transcription factor, ATF-like (Batf); ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 BCL2-associated X protein (Bax); BCL2L11; beta 2 microglobulin (B2m); BL2-associated agonist of cell dealth (Bad); BLIMP1; Bloom syndrome, RecQ like helicase (Blm); Bmi1 polycomb ring finger oncogene (Bmi1); Bone morphogenic protein 4 (Bmp4); Braf transforming gene (Braf); butyrophilin, subfamily 2, member A1 (Btn2a1); butyrophilin, subfamily 2, member A2 (Btn2a2); butyrophilin-like 1 (Btnl1); butyrophilin-like 2 (Btnl2); c- abl oncogene 1 (Abl1); c-abl oncogene 2 (Abl2); cadherin-like 26(Cdh26); calcium channel, voltage dependent, beta 4 subunit (Cacnb4); CAMK2D; capping protein regulator and myosin 1 linker 2 (Carmil2); carcinoembryonic antigen-related cell adhesion molecule (Ceacam1); Casitas B-lineage lymphoma b (Cblb); CASP8; Caspase 3 (Casp3); caspase recruitment domain family member 11 (Card11); catenin (cadherin associated protein), beta 1 (Ctnnb1); caveolin 1 (Cav1); CBL-B; CCAAT / enhancer binding protein (C / EBP), beta (Cebpb); CCR10; CCR4; CCR5; CCR6; CCR9; CD103; CD11a; CD122; CD123; CD127; CD130; CD132; CD160 antigen (Cd160); CD161; CD19; CD1d1 antigen (Cd1d1); CD1d2 antigen (CD1d2); CD2 antigen (CD2); CD209e antigen (Cd209e); CD23; CD244 molecule A (Cd244a); CD24a antigen (Cd24a); CD27 antigen (CD27); CD274 antigen (Cd274); CD276 antigen (Cd276); CD28 antigen (Cd28); CD3 delta; CD3 epsilon; CD3 gamma; CD30; CD300A molecule (Cd300a); CD33; CD38; CD4 antigen (Cd4); CD40 ligand (Cd40lg); CD44 antigen (Cd44); CD46 antigen, complement regulatory protein (Cd46); CD47 antigen (Rh-related antigen, integrin-associated signal transducer) (Cd47); CD48 antigen (Cd48); CD5 antigen (Cd5); CD52; CD58; CD59b antigen (Cd59b); CD6 antigen (Cd6); CD69; CD7; CD70; CD74 antigen (Cd74); CD8; CD8 antigen (Cd8); CD80 antigen (Cd80); CD81 antigen (Cd81); CD82; CD83 antigen (Cd83); CD86; CD86 antigen (Cd86); CD8A; CD96; CD99; CDK4; CDK8; CDKN1B; chemokine (C motif) ligand 1 (Xcl1); chemokine (C-C motif) ligand 19 (Ccl19); chemokine (C-C motif) ligand 2 (Ccl2); chemokine (C-C motif) ligand 20 (Ccl20); chemokine (C-C motif) ligand 5 (Ccl5); chemokine (C-C motif) receptor 2 (Ccr2); chemokine (C-C motif) receptor 6 (Ccr6); chemokine (C-C motif) receptor 9 (Ccr9); chemokine (C-X-C motif) ligand 12 (Cxcl12); chemokine (C-X-C motif) receptor (Cxcr4); Chitinase 3 Like 1 (Chi3l1); cholinergic receptor, nicotinic, alpha polypeptide 7 (Chrna7); chromodomain helicase DNA binding protein 7 (Chd7); CLA; Class II Major Histocompatibility Complex Transactivator (CIITA); cleft lip and palate associated transmembrane protein 1 (Clptm1); Cluster of Differentiation 123 (CD123); Cluster of Differentiation 3 (CD3); Cluster of Differentiation 33 (CD33); Cluster of Differentiation 52 (CD52); Cluster of Differentiation 7 (CD7); Cluster of Differentiation 96 (CD96); coagulation factor II (thrombin) receptor-like 1 (F2rl1); coil-coil domain containing 88B ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 (Ccdc88b); core-binding factor beta (Cbfb); coronin, actin binding protein 1A (Coro1a); coxsackie virus and adenovirus receptor (Cxadr); CS-1; CSF2CSK; c-src tyrosine kinase (Csk); C-type lectin domain family 2, member i (Clec2i); C-type lectin domain family 4, member a2 (Clec4a2); C-type lectin domain family 4, member d (Clec4d); C-type lectin domain family 4, member e (Clec4e); C-type lectin domain family 4, member f (Clec4f); C- type lectin domain family 4, member g (Clec4g); CUL3; CXCR3; cyclic GMP-AMP synthase (Cgas); cyclin D3 (Ccnd3); cyclin dependent kinase inhibitor 2A (Cdkn2a); cyclin- dependent kinase (Cdk6); CYLD lysine 63 deubiquitinase (Cyld); cysteine-rich protein 3 (Crip3); cytidine 5'-triphosphate synthase (Ctps); Cytochrome P450 Family 11 Subfamily A Member 1 (Cyp11a1); cytochrome P450, family 26, subfamily b, polypeptide (Cyp26b1); Cytokine Inducible SH2 Containing Protein (CISH); cytotoxic T lymphocyte-associated protein 2 alpha (Ctla2a); Cytotoxic T-Lymphocyte Associated Protein 4 (CTLA-4); DCK; dedicator of cytokinesis 2 (Dock2); dedicator of cytokinesis 8 (Dock8); delta like canonical Notch ligand 4 (Dll4); deltex 1, E3 ubiquitin ligase (Dtx1); deoxyhypusine synthase (Dhps); DGKA; DGKZ; DHX37; dicer 1, ribonuclease type III (Dicer1); dipeptidylpeptidase 4 (Dpp4); discs large MAGUK scaffold protein 1 (Dlg1); DnaJ heat shock protein family (Hsp40) member A3 (Dnaja3); dolichyl-di-phosphooligosaccharide-protein glycotransferase (Ddost); double homeobox B-like 1 (Duxbl1); drosha, ribonuclease type III (Drosha); dual specificity phosphatase 10 (Dusp10); dual specificity phosphatase 22 (Dusp22); dual specificity phosphatase 3 (Dusp3); E74-like factor 4 (Elf4); early growth response 1(Egr1); early growth response 3 (Egr3); ELOB (TCEB2); ENTPD1 (CD39); eomesodermin (Eomes); Eph receptor B4 (Ephb4); Eph receptor B6 (Ephb6); ephrin B1 (Efnb1); ephrin B2 (Efnb2); ephrin B3 (Efnb3); Epstein-Barr virus induced gene 3 (Ebi3); erb-b2 receptor tyrosine kinase (Erbb2); eukaryotic translation initiation factor 2 alpha kinase 4 (Eif2ak4); FADD; family with sequence similarity 49, member B (Fam49b); Fanconi anemia, complementation group A (Fanca); Fanconi anemia, complementation group D2 (Fancd2); Fas (TNF receptor superfamily member 6) (Fas); Fas (TNFRSF6)-associated via death domain (Fadd); Fas Cell Surface Death Receptor (FAS); Fc receptor, IgE, high affinity I, gamma polypeptide (Fcer1g); fibrinogen-like protein 1 (Fgl1); fibrinogen-like protein 2 (Fgl2); FK506 binding protein 1a (Fkbp1a); FK506 binding protein 1b ((Fkbp1b); flotillin 2 (Flot2); FMS-like tyrosine kinase (Flt3); forkhead box J1 (Foxj1); forkhead box N1 (Foxn1); forkhead box P1 (Foxp1); forkhead box P3 (Foxp3); frizzled class receptor 5 (Fzd5); frizzled class receptor 7 (Fzd7); frizzled class receptor 8 (Fzd8); fucosyltransferase 7 (Fut7); Fyn proto-oncogene (Fyn); gap junction protein, alpha 1 (Gja1); GATA binding protein 3 (GATA3); GCN2 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 kinase (IDO pathway); gelsolin (Gsn); GLI-Kruppel family member GLI3 (Gli3); glycerol-3- phosphate acyltransferase, mitochondrial (Gpam); growth arrest and DNA-damage-inducible 45 gamma (Gadd45g); GTPase, IMAP family member 1 (Gimap1); H1TET2; H2.0-like homeobox (Hlx); haematopoietic 1(hem1); HCLS1 binding protein 3 (Hs1bp3); heat shock 105kDa / 110kDa protein 1(Hsph1); heat shock protein 1 (chaperonin) (Hspd1); heat shock protein 90, alpha (cytosolic), class A member 1 (Hsp90aa1); hematopoietic SH2 domain containing (Hsh2d); hepatitis A virus cellular receptor 2 (Havcr2); hes family bHLH transcription factor 1 (Hes1); histocompatibility 2, class II antigen A, alpha (H2-Aa); histocompatibility 2, class II antigen A, beta 1 (H2-Ab1); histocompatibility 2, class II, locus DMa (H2-DMa); histocompatibility 2, M region locus 3(H3-M3); histocompatibility 2, O region alpha locus (H2-Oa); histocompatibility 2, T region locus 23 (H2-T23); HLA-DR; homeostatic iron regulator (Hfe); icos ligand (Icosl); IKAROS family zinc finger 1 (Ikzf1); IL10; IL10RA; IL2 inducible T cell kinase (Itk); IL6R; Indian hedgehog (Ihh); indoleamine 2,3-dioxygenase 1 (Ido1); inducible T cell co-stimulator (Icos); inositol 1,4,5-trisphosphate 3- kinase B (Itpkb); insulin II (Ins2); insulin-like growth factor 1 (Igf1); insulin-like growth factor 2 (Igf2); insulin-like growth factor binding protein 2 (Igfbp2); integrin alpha L (Itgal); integrin alpha M (Itgam); integrin alpha V (Itgav); integrin alpha X (Itgax); integrin beta 2 (Itgb2); integrin, alpha D (Itgad); intercellular adhesion molecule 1 (Icam1); interferon (alpha and beta) receptor 1(Ifnar1); interferon alpha 1 (Ifna1); interferon alpha 11 (Ifna11); interferon alpha 12 (Ifna12); interferon alpha 13 (Ifna13); interferon alpha 14 (Ifna14); interferon alpha 16 (Ifna16); interferon alpha 2 (Ifna2); interferon alpha 4 (Ifna4); interferon alpha 5 (Ifna5); interferon alpha 6 (Ifna6); interferon alpha 7 (Ifna7); interferon alpha 9 (Ifna9); interferon alpha B (Ifnab); interferon beta 1 (Ifnb1); interferon gamma (IFNg); interferon kappa (Ifnk); interferon regulatory factor 1 (Irf1); interferon regulatory factor 4 (Irf4); interferon zeta (Ifnz); interleukin 1 beta (Il1b; interleukin 1 family, member 8 (Il1f8); interleukin 1 receptor-like 2 (Il1rl2); interleukin 12 receptor, beta1 (Il12rb1); interleukin 12a (Il12a); interleukin 12b (Il12b); interleukin 15 (Il15); interleukin 18 (Il18); interleukin 18 receptor 1 (Il18r1); interleukin 2 (Il2); interleukin 2 receptor, alpha chain (Il2ra); interleukin 2 receptor, gamma chain (Il2rg); interleukin 20 receptor beta (Il20rb); interleukin 21 (Il21); interleukin 23, alpha subunit p19 (Il23a); interleukin 27 (Il27); interleukin 4 (Il4); interleukin 4 receptor, alpha (Il4ra); interleukin 6 (Il6); interleukin 7 (Il7); IRF8; itchy, E3 ubiquitin protein ligase (Itch); jagged 2 (Jag2); jumonji domain containing 6 (Jmjd6); JUNB; junction adhesion molecule like 9 (Jam9); K(lysine) acetyltransferase 2A (Kat2a); KDEL (Lys-Asp- Glu-Leu) endoplasmic reticulum protein retention receptor 1 (Kdelr1); KIT proto-oncogene ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 receptor tyrosine kinase (Kit); LAG-3; LAIR-1 (CD305); LDHA; lectin, galactose binding, soluble 1 (Lgals1); lectin, galactose binding, soluble 3 (Lgals3); lectin, galactose binding, soluble 8 (Lgals8); lectin, galactose binding, soluble 9 (Lgals9); leptin (Lep); leptin receptor (Lepr); leucine rich repeat containing 32 (Lrrc32); leukocyte immunoglobulin-like receptor, subfamily B, member 4A (Lilrb4a); LFNG O-fucosylpeptide 3-beta-N- acetylglucosaminyltransferase (Lfng); LIF; ligase IV, DNA, ATP-dependent (Lig4); LIM domain only 1 (Lmo1); limb region 1 like (Lmbrl); linker for activation of T cells (Lat); lymphocyte antigen 9 (Ly9); lymphocyte cytosolic protein 1 (Lcp1); lymphocyte protein tyrosine kinase (Lck); lymphocyte transmembrane adaptor 1 (Lax1); lymphocyte-activation gene 3 (Lag3); lymphoid enhancer binding factor 1 (Lef1); LYN; lysyl oxidase-like 3 (Loxl3); MAD1 mitotic arrest deficient 1-like 1 (Mad1l1); MALT1 paracaspase (Malt1); MAP4K4; MAPK14; MCJ; mechanistic target of rapamycin kinase (Mtor); MEF2D; Methylation-Controlled J Protein (MCJ); methyltransferase like 3 (Mettl3); MGAT5; MHC I like leukocyte 2 (Mill2); midkine (Mdk); mitogen-activated protein kinase 8 interacting protein 1 (Mapk8ip10); moesin (Msn); myelin protein zero-like 2 (Mpzl2); myeloblastosis oncogene (Myb); myosin, heavy polypeptide 9, non-muscle (Myh9); Nedd4 family interacting protein 1 (Ndfip1); neural precursor cell expressed, developmentally down- regulated 4 (Nedd4); NFATc1; NFATC2; NFATC4; NFKB activating protein (Nkap); nicastrin (Ncstn); NK2 homeobox 3 (Nkx2-3); NLR family, CARD domain containing 3 (Nlrc3); NLR family, pyrin domain containing 3 (Nlrp3); non-catalytic region of tyrosine kinase adaptor protein 1 (Nck1); non-catalytic region of tyrosine kinase adaptor protein 2 (Nck2); non-homologous end joining factor 1 (Nhej1); non-SMC condensin II complex, subunit H2 (Ncaph2); Notch-regulated ankyrin repeat protein (Nrarp); NT5E (CD73); nuclear factor of activated T cells, cytoplasmic, calcineurin dependent (Nfatc3); nuclear factor of kappa light polypeptide gene enhancer in B cells inhibitor, delta (Nfkbid); nuclear receptor co-repressor 1 (Ncor1); Nuclear Receptor Subfamily 4 Group A Member 1 (NR4A1); Nuclear Receptor Subfamily 4 Group A Member 2 (NR4A2); Nuclear Receptor Subfamily 4 Group A Member 3 (NR4A3); ODC1; OTU domain containing 5 (Otud5); OTULINL (FAM105A); paired box 1 (Pax1); PDCD1 (PD1; PD-1); PDIA3; pellino 1 (Peli1); peroxiredoxin 2 (Prdx2); PHD1 (EGLN2); PHD2 (EGLN1); PHD3 (EGLN3); phosphodiesterase 5A, cGMP-specific (Pde5a); phosphoinositide-3-kinase regulatory subunit (Pik3r6); phospholipase A2, group IIA (Pla2g2a); phospholipase A2, group IID (Pla2g2d);; phospholipase A2, group IIE (Pla2g2e); phosphoprotein associated with glycosphingolipid microdomains 1 (Pag1); PIK3CD; PIKFYVE; POZ (BTB) and AT hook containing zinc ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 finger 1 (Patz1); PPARa; PPARd; PR domain containing 1, with ZNF domain (Prdm1); presenilin 1 (Psen1); presenilin 2 (Psen2); PRKACA; PRKC, apoptosis, WT1, regulator (Pawr); programmed cell death 1 ligand 2 (Pdcd1lg2); prosaposin (Psap); prostaglandin E receptor 4 (subtype EP4) (Ptger4); protein kinase C, theta 2 (Prkcq); protein kinase C, zeta (Prkcz); protein kinase, cAMP dependent regulatory, type I, alpha (Prkar1a); protein kinase, DNA activated, catalytic polypeptide (Prkdc); protein phosphatase 3, catalytic subunit, beta isoform (Ppp3cb); protein tyrosine phosphatase, non-receptor type 2 (Ptpn2); protein tyrosine phosphatase, non-receptor type 22 (lymphoid) (Ptpn22); protein tyrosine phosphatase, non- receptor type 6 (Ptpn6); protein tyrosine phosphatase, receptor type, C (Ptprc); PTEN; PTPN11; purine-nucleoside phosphorylase (Pnp); purinergic receptor P2X, ligand-gated ion channel, 7 (P2rx7); PVR Related Immunoglobulin Domain Containing (PVRIG; CD112R); PYD and CARD domain containing 7 (Pycard); RAB27A, member RAS oncogene family (Rab27a); RAB29, member RAS oncogene family (Rab29); radical S-adenosyl methionine domain containing 2 (Rsad2); RAR-related orphan receptor alpha (Rora); RAR-related orphan receptor gamma (Ror); RAS guanyl releasing protein 1 (Rasgrp1); ras homolog family member A (Rhoa); ras homolog family member H (Rhoh); RAS protein activator like 3 (Rasal3); RASA2; receptor (TNFRSF)-interacting serine-threonine kinase 2 (Ripk2); recombination activating gene 1 ( Rag1); recombination activating gene 2 (Rag2); Regulatory Factor X Associated Ankyrin Containing Protein (RFXANK); RHO family interacting cell polarization regulator 2 (Ripor2); ribosomal protein L22 (Rpl 22); ribosomal protein S6 (Rps6); RING CCCH (C3H) domains 1 (Rc3h1); ring finger and CCCH-type zinc finger domains 2 (Rc3h2); RNF2; runt related transcription factor 1 (Runx1); runt related transcription factor 2 (Runx2); SAM and SH3 domain containing 3 (Sash3); schlafen 1; Selectin P Ligand / P-Selectin Glycoprotein Ligand-1 (SELPG / PSGL1) polypeptide; selenoprotein K (Selenok); sema domain immunoglobulin domain (Ig), transmembrane domain (TM) and short cytoplasmic domain, (semaphorin) 4A (Sema4a); serine / threonine kinase 11 (Stk11); SH3 domain containing ring finger 1 (Sh3rf1); SHP1; sialophorin (Spn); SIGLEC15; signal transducer and activator of transcription 3 (Stat3); signal transducer and activator of transcription 5A (Stat5A); signal transducer and activator of transcription 5B (Stat5B); signal-regulatory protein alpha (Sirpa); Signal-regulatory protein beta 1A (Sirpb1a); Signal-regulatory protein beta 1C (Sirpb1c); SLA; SLAM family member 6 (Slamf6); SLAMF7; SMAD family member 3 (Smad3); SMAD family member 7 (Smad7); SMARCA4; solute carrier family 11 (proton-coupled divalent metal ion transporters), member 1 (Slc11a1); solute carrier family 4 (anion exchanger), member 1; solute carrier ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 family 46, member 2 (Slc46a2); sonic hedgehog (Shh); SOS Ras / Rac guanine nucleotide exchange factor 1 (Sos1); SOS Ras / Rac guanine nucleotide exchange factor 2 (Sos2); special AT-rich sequence binding protein 1 (Satb1); spleen tyrosine kinase (Syk); Sprouty RTK Signaling Antagonist 1 (Spry1); Sprouty RTK Signaling Antagonist 2 (Spry2); squamous cell carcinoma antigen recognized by T cells (Sart1); src homology 2 domain-containing transforming protein B (Shb); Src-like-adaptor 2 (Sla2); SRY (sex determining region Y)-box 4 (Sox4); STK4; suppression inducing transmembrane adaptor 1 (Sit1); suppressor of cytokine signaling 1 (Socs1); suppressor of cytokine signaling 5 (Socs5); suppressor of cytokine signaling 6 (Socs6); surfactant associated protein D (Sftpd); SUV39; syndecan 4 (Sdc4); syntaxin 11 (Stx11); T Cell Immunoglobulin Mucin 3 (Tim-3); T cell immunoreceptor with Ig and ITIM domains (Tigit); T cell receptor alpha joining 18 (Traj18); T Cell Receptor Beta Constant 1 (TRBC1); T Cell Receptor Beta Constant 2 (TRBC2); T cell, immune regulator 1, ATPase, H+ transporting, lysosomal V0 protein A3 (Tcirg1); T cell-interacting, activating receptor on myeloid cells 1 (Tarm1); T-box 21 (Tbx21); TCR; TCR alpha; TCR beta; TCR complex gene sequence; Tet Methylcytosine Dioxygenase 2 (TET2); TGFbRII; TGFbRII (TGFBR2); three prime repair exonuclease 1 (Trex1); thymocyte selection associated (Themis); thymus cell antigen 1, theta (Thy1); TMEM222; TNF receptor-associated factor 6 (Traf6); TNFAIP3; TNFRSF10B; TNFRSF8 (CD30); TOX; TOX2; TRAC; transformation related protein 53 (Trp53); Transforming Growth Factor Beta Receptor II (TGFbRII); transforming growth factor, beta receptor II (Tgfbr2); transmembrane 131 like (Tmem131l); transmembrane protein 98 (Tmem98); triggering receptor expressed on myeloid cells-like 2 (Trem12); TSC complex subunit 1 (Tsc1); tumor necrosis factor (ligand) superfamily, member 11 (Tnfsf11); tumor necrosis factor (ligand) superfamily, member 13b (Tnfsf13b); tumor necrosis factor (ligand) superfamily, member 4 (Tnfsf4); tumor necrosis factor (ligand) superfamily, member 9 (Tnfsf9); tumor necrosis factor receptor superfamily, member 13c (Tnfrsf13c); tumor necrosis factor receptor superfamily, member 4 (Tnfrsf4); tumor necrosis factor, alpha-induced protein 8-like 2 (Tnfa1p8l2); twisted gastrulation BMP signaling modulator 1 (Twsg1); UBASH3A; vanin 1 (Vnn1); vascular cell adhesion molecule 1 (Vcam1); VHL; v-maf musculoaponeurotic fibrosarcoma oncogene family, protein B (avian) (Mafb); V-set and immunoglobulin domain containing 4 (Vsig4); V-Set Immunoregulatory Receptor (VISTA); WD repeat and FYVE domain containing 4 (Wdfy4); wingless-type MMTV integration site family, member 1 (Wnt1); wingless-type MMTV integration site family, member 4 (Wnt4); WNT signaling pathway regulator (Apc); WW domain containing E3 ubiquitin protein ligase 1 (Wwp1); XBP1; YAP1; ZAP70; ZC3H12A; ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 zfp35; zinc finger and BTB domain containing 1 (Zbtb1); zinc finger and BTB domain containing 7B (Zbtb7B); zinc finger CCCH type containing 12A (Zc3h12a); zinc finger CCCH type containing 12D (Zc3h12d); zinc finger E-box binding homeobox 1 (Zeb1); zinc finger protein 36, C3H type (Zfp36); zinc finger protein 36, C3H type-like 1 (Zfp36L1); zinc finger protein 36, C3H type-like 2 (Zfp36L2); and zinc finger protein 683 (Zfp683). Immune cells and / or immune effector cells can be isolated or purified from a sample collected from a subject or a donor using standard techniques known in the art. For example, immune effector cells can be isolated or purified from a whole blood sample by lysing red blood cells and removing peripheral mononuclear blood cells by centrifugation. The immune effector cells can be further isolated or purified using a selective purification method that isolates the immune effector cells based on cell-specific markers such as CD25, CD3, CD4, CD8, CD28, CD45RA, or CD45RO. In one embodiment, CD4+is used as a marker to select T cells. In one embodiment, CD8+is used as a marker to select T cells. In one embodiment, CD4+and CD8+are used as a marker to select regulatory T cells. In another embodiment, the present disclosure provides T cells that have targeted gene knock-outs at the TCR constant region (TRAC), which is responsible for TCRαβ surface expression. TCRαβ-deficient CAR-T cells are compatible with allogeneic immunotherapy (Qasim et al., Sci. Transl. Med.9, eaaj2013 (2017); Valton et al., Mol Ther. 2015 Sep; 23(9): 1507–1518). If desired, residual TCRαβ T cells are removed using CliniMACS magnetic bead depletion to minimize the risk of GVHD. In another embodiment, the present disclosure provides donor T cells selected ex vivo to recognize minor histocompatibility antigens expressed on recipient hematopoietic cells, thereby minimizing the risk of graft-versus-host disease (GVHD), which is the main cause of morbidity and mortality after transplantation (Warren et al., Blood 2010;115(19):3869-3878). A technique for isolating or purifying immune effector cells is flow cytometry. In fluorescence activated cell sorting a fluorescently labelled antibody with affinity for an immune effector cell marker is used to label immune effector cells in a sample. A gating strategy appropriate for the cells expressing the marker is used to segregate the cells. For example, T lymphocytes can be separated from other cells in a sample by using, for example, a fluorescently labeled antibody specific for an immune effector cell marker (e.g., CD4, CD8, CD28, CD45) and corresponding gating strategy. In one embodiment, a CD4 gating strategy is employed. In one embodiment, a CD8 gating strategy is employed. In one embodiment, a CD4 and CD8 gating strategy is employed. In some embodiments, a gating strategy for other ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 markers specific to an immune effector cell is employed instead of, or in combination with, the CD4 and / or CD8 gating strategy. In embodiments, the immune effector cells contemplated in the present disclosure are effector T cells. In some embodiments, the effector T cell is a naïve CD8+T cell, a cytotoxic T cell, a natural killer T (NKT) cell, a natural killer (NK) cell, or a regulatory T (Treg) cell. In some embodiments, the effector T cells are thymocytes, immature T lymphocytes, mature T lymphocytes, resting T lymphocytes, or activated T lymphocytes. In some embodiments the immune effector cell is a CD4+CD8+T cell or a CD4- CD8- T cell. In some embodiments the immune effector cell is a T helper cell. In some embodiments the T helper cell is a T helper 1 (Th1), a T helper 2 (Th2) cell, or a helper T cell expressing CD4 (CD4+ T cell). In some embodiments, immune effector cells are effector NK cells. In some embodiments, the immune effector cell is any other subset of T cells. The modified immune effector cell may express, in addition to the chimeric antigen receptor (CAR), an exogenous cytokine, a different chimeric receptor, or any other agent that would enhance immune effector cell signaling or function. For example, co-expression of the chimeric antigen receptor and a cytokine may enhance the CAR-T cell’s ability to lyse a target cell. Provided herein are also polynucleotides that encode the chimeric antigen receptors (CARs) described herein. In some embodiments, the nucleic acid molecule is isolated or purified. Delivery of the nucleic acid molecules ex vivo can be accomplished using methods known in the art. For example, immune cells obtained from a subject may be transformed with a nucleic acid vector encoding the chimeric antigen receptor. The vector may then be used to transform recipient immune cells so that these cells will then express the chimeric antigen receptor. Efficient means of transforming immune cells include transfection and transduction. Such methods are well known in the art. For example, applicable methods for delivery the nucleic acid molecule encoding the chimeric antigen receptor (and the nucleic acid(s) encoding the base editor) can be found in International Application No. PCT / US2009 / 040040 and US Patent Nos.8,450,112; 9,132,153; and 9,669,058, each of which is incorporated herein in its entirety. Additionally, those methods and vectors described herein for delivering the nucleic acid encoding the base editor are applicable to delivering the nucleic acid encoding the chimeric antigen receptor. HUMAN LEUKOCYTE ANTIGEN (HLA) POLYPEPTIDES The HLA system (also referred to as the major histocompatibility complex (MHC) system) is composed of three regions. The class I region corresponds to the genes coding for ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 molecules HLA-A, -B, and -C. The class I region also contains other loci called HLA-E, -L, - J, -K, -H, and -G, which encode the non-classical HLA molecules. In addition, the class II region encodes HLA-DR, -DQ, and –DP. Finally, the class III region, in which genes are encoding for proteins of the complement system and TNF family genes. The function of HLA-encoded class I and class II molecules is to bind peptide antigens and display them for recognition by antigen-specific T lymphocytes. Peptide antigens associated with HLA class I molecules are recognized by CD8+T Cells while HLA class II molecules are recognized by CD4+T Cells. HLA class I polypeptides are expressed on the surface of almost all nucleated cells. HLA class I polypeptides contain glycosylated heavy chains encoded by the HLA class I genes (HLA-A, -B, and -C) and noncovalently bound extracellular beta-2- microglobulin (B2M). Human B2M is invariant and its gene maps to chromosome 15. The class I heavy chain has three extracellular domains (α1, α2, and α3), a transmembrane region, and an intracytoplasmic domain. The α1 and α2 domains contain variable amino acid sequences, and these domains determine the antigenic specificities of the HLA class I molecules. The α3and B2M domains together form immunoglobulin constant domain-like folds. The heavy chain α1and α2domains form a unique structure consisting of a platform of eight antiparallel β strands and two antiparallel α-helices on top of the platform. A groove is formed by the two α-helices and the β-pleated floor, and this is the binding site for processed peptide antigen. The class I peptide binding groove accommodates a processed peptide (e.g., a cognate peptide (cPep)) of 8 to 10 (predominantly nonamers) amino acid residues. The structure of HLA-E is similar to that of the HLA class I polypeptides (see, e.g., O’Callaghan and Bell, Immunol Rev.163:129-38 (1998), the disclosure of which is incorporated herein by reference in its entirety for all purposes), but the peptide-binding groove is highly adapted for the specific binding of a cPep. This is different from class I molecules, which have highly promiscuous peptide-binding grooves. Not intending to be bound by theory, the HLA-E groove makes full use of all the available pockets and imposes specificity along the entire length of the peptide. EDITING OF TARGET GENES In general, base editing is carried out to induce therapeutic changes (e.g., knocking out of expression of beta-2-microglobulin, CD58, and / or another polypeptide(s) listed herein) in the genome of a cell (e.g., immune cell (e.g., T- or NK-cell)). In some embodiments, the therapeutic change includes reducing or eliminating expression of an HLA class I gene. In ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 some embodiments, the HLA class I gene is HLA-A, HLA-B, or HLA-C. Base editing can be carried out in vitro or in vivo. In various embodiments, base editing can be used to introduce a stop codon to a gene or to disrupt a splice motif (e.g., a acceptor site, or a splice donor site). In some embodiments, cells (e.g., immune cell (e.g., T- or NK-cell)) are collected from a subject or a donor. In some embodiments, base editing is carried out to induce therapeutic changes in the genome of an immune cell (e.g., T- or NK-cell). In some embodiments, base editing is carried out to induce therapeutic changes in the genome of an allogeneic immune cell (e.g., T- or NK-cell) of a subject. In some embodiments, base editing is carried out to induce therapeutic changes in the genome of an allogeneic CAR-T cell. To produce the gene edits described herein, immune cells may be collected from a subject and / or contacted with one or more guide RNAs, or one or more polynucleotides encoding the guide RNAs, and a nucleobase editor polypeptide comprising a nucleic acid programmable DNA binding protein (napDNAbp) and a cytidine deaminase or adenosine deaminase, or comprising one or more deaminases with cytidine deaminase and / or adenosine deaminase activity (e.g., a “dual deaminase” which has cytidine and adenosine deaminase activity), or one or more polynucleotides encoding the nucleobase editor polypeptide. In some embodiments, the gRNA comprises nucleotide analogs. These nucleotide analogs can inhibit degradation of the gRNA from cellular processes. In some instances, the gRNA is added directly to a cell. Table 2 provides representative spacer sequences to be used for gRNAs. In some embodiments, immune cells (e.g., T- or NK-cell) of the present disclosure, are contacted with one or more guide RNAs and a nucleobase editor polypeptide comprising a nucleic acid programmable DNA binding protein (napDNAbp) (e.g., Cas9) domain and a deaminase (e.g., cytidine deaminase and / or adenosine deaminase) domain. In some embodiments, immune cells (e.g., T- or NK-cell) of the present disclosure, are contacted with one or more guide RNAs and a nucleobase editor polypeptide comprising a nucleic acid programmable DNA binding protein (napDNAbp) (e.g., Cas9) domain and an adenosine deaminase domain. In some embodiments, immune cells (e.g., T- or NK-cell) of the present disclosure, are contacted with one or more guide RNAs and a nucleobase editor polypeptide comprising a nucleic acid programmable DNA binding protein (napDNAbp) (e.g., Cas9) domain and a cytidine deaminase domain. In some embodiments, immune cells (e.g., T- or NK-cell) of the present disclosure, are contacted with one or more guide RNAs and a nucleobase editor polypeptide comprising a nucleic acid programmable DNA binding protein (napDNAbp) (e.g., Cas9) domain and an adenosine / cytidine deaminase domain. In some ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 embodiments, the at least one nucleic acid molecule encoding one or more guide RNAs and a nucleobase editor polypeptide is delivered to cells by one or more vectors (e.g., AAV vector). In some embodiments, one or more vectors (e.g., AAV vector) comprise at least one nucleic acid molecule encoding one or more guide RNAs and a nucleobase editor polypeptide, which comprises a nucleic acid programmable DNA binding protein (napDNAbp) (e.g., Cas9) domain and a deaminase (e.g., cytidine deaminase and / or adenosine deaminase) domain. In some embodiments, one or more vectors (e.g., AAV vector) comprise at least one nucleic acid molecule encoding one or more guide RNAs, which direct a nucleobase editor polypeptide to edit a site in the genome of a cell (e.g., immune cell (e.g., T- or NK-cell)). The present disclosure provides one or more guide RNAs that direct a nucleobase editor polypeptide to edit a site in the genome of the cell (e.g., immune cell (e.g., T- or NK- cell)). In some embodiments, the present disclosure provides guide RNAs that target components of the peptide loading complex (PLC) (e.g., β2M, TAP1, TAP2, Tapasin) and / or CD58 in an immune cell (e.g., T- or NK-cell). In some embodiments, the present disclosure provides guide RNAs that target β2M, TAP1, TAP2, Tapasin, and / or CD58. In some embodiments, the gRNA comprises nucleotide analogs. These nucleotide analogs can inhibit degradation of the gRNA from cellular processes. Exemplary guide spacer sequences are provided in the following Table2. A non-limiting example of a gRNA scaffold sequence includes the following: GUUUUAGAGCUAGAAAUAGCAAGUUAAAAUAAGGCUAGUCCGUUAUCAACUUGAAAAAGUGG CACCGAGUCGGUGCUUUU (SEQ ID NO: 317). Variants of the spacer sequences listed in Table 2 comprising 1, 2, 3, 4, or 5 nucleobase alterations are contemplated. For example, variation of a target polynucleotide sequence within a population (e.g., single nucleotide polymorphisms) may require said alterations to a spacer sequence to allow the spacer to better bind a variant of a target sequence in a subject. In various instances, it is advantageous for a spacer sequence to include a 5' and / or a 3' “G” nucleotide. In some cases, for example, any spacer sequence or guide polynucleotide provided herein comprises or further comprises a 5' “G”, where, in some embodiments, the 5' “G” is or is not complementary to a target sequence. In some embodiments, the 5' “G” is added to a spacer sequence that does not already contain a 5' “G.” For example, it can be advantageous for a guide RNA to include a 5' terminal “G” when the guide RNA is expressed under the control of a U6 promoter or the like because the U6 promoter prefers a “G” at the ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 transcription start site (see Cong, L. et al. “Multiplex genome engineering using CRISPR / Cas systems. Science 339:819-823 (2013) doi: 10.1126 / science.1231143). In some cases, a 5' terminal “G” is added to a guide polynucleotide that is to be expressed under the control of a promoter, but is optionally not added to the guide polynucleotide if or when the guide polynucleotide is not expressed under the control of a promoter. Exemplary guide RNA and spacer sequences suitable for use in methods of the disclosure include those listed in PCT / US22 / 75021, filed August 16, 2022, the disclosure of which is incorporated herein in its entirety for all purposes. Table 2. Representative spacer sequences. NUCLEOBASE EDITORS Useful in the methods and compositions described herein are nucleobase editors that edit, modify or alter a target nucleotide sequence of a polynucleotide. Nucleobase editors described herein typically include a polynucleotide programmable nucleotide binding domain and a nucleobase editing domain (e.g., adenosine deaminase, cytidine deaminase, or a dual deaminase). A polynucleotide programmable nucleotide binding domain, when in conjunction with a bound guide polynucleotide (e.g., gRNA), can specifically bind to a target polynucleotide sequence and thereby localize the base editor to the target nucleic acid sequence desired to be edited. Polynucleotide Programmable Nucleotide Binding Domain Polynucleotide programmable nucleotide binding domains bind polynucleotides (e.g., RNA, DNA). A polynucleotide programmable nucleotide binding domain of a base editor can itself comprise one or more domains (e.g., one or more nuclease domains). In some embodiments, the nuclease domain of a polynucleotide programmable nucleotide binding domain comprises an endonuclease or an exonuclease. Disclosed herein are base editors comprising a polynucleotide programmable nucleotide binding domain comprising all or a portion (e.g., a functional portion) of a CRISPR protein (i.e., a base editor comprising as a domain all or a portion (e.g., a functional portion) of a CRISPR protein (e.g., a Cas protein), also referred to as a “CRISPR protein- ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 derived domain” of the base editor). A CRISPR protein-derived domain incorporated into a base editor can be modified compared to a wild-type or natural version of the CRISPR protein. A CRISPR protein-derived domain can comprise one or more mutations, insertions, deletions, rearrangements and / or recombinations relative to a wild-type or natural version of the CRISPR protein. Cas proteins that can be used herein include class 1 and class 2. Non-limiting examples of Cas proteins include Cas1, Cas1B, Cas2, Cas3, Cas4, Cas5, Cas5d, Cas5t, Cas5h, Cas5a, Cas6, Cas7, Cas8, Cas9 (also known as Csn1 or Csx12), Cas10, Csy1 , Csy2, Csy3, Csy4, Cse1, Cse2, Cse3, Cse4, Cse5e, Csc1, Csc2, Csa5, Csn1, Csn2, Csm1, Csm2, Csm3, Csm4, Csm5, Csm6, Cmr1, Cmr3, Cmr4, Cmr5, Cmr6, Csb1, Csb2, Csb3, Csx17, Csx14, Csx10, Csx16, CsaX, Csx3, Csx1, Csx1S, Csf1, Csf2, CsO, Csf4, Csd1, Csd2, Cst1, Cst2, Csh1, Csh2, Csa1, Csa2, Csa3, Csa4, Csa5, Cas12a / Cpf1, Cas12b / C2c1 (e.g., SEQ ID NO: 232), Cas12c / C2c3, Cas12d / CasY, Cas12e / CasX, Cas12g, Cas12h, Cas12i, and Cas12j / CasΦ, CARF, DinG, Turbo Cas9 (i.e., an SpCas9 with the amino acid alterations Q844R, V842L, F846Y, L847M, and I852F), homologues thereof, or modified versions thereof. A CRISPR enzyme can direct cleavage of one or both strands at a target sequence, such as within a target sequence and / or within a complement of a target sequence. For example, a CRISPR enzyme can direct cleavage of one or both strands within about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 50, 100, 200, 500, or more base pairs from the first or last nucleotide of a target sequence. A vector that encodes a CRISPR enzyme that is mutated to with respect to a corresponding wild-type enzyme such that the mutated CRISPR enzyme lacks the ability to cleave one or both strands of a target polynucleotide containing a target sequence can be used. A Cas protein (e.g., Cas9, Cas12) or a Cas domain (e.g., Cas9, Cas12) can refer to a polypeptide or domain with at least or at least about 50%, 60%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% sequence identity and / or sequence homology to a wild-type exemplary Cas polypeptide or Cas domain. Cas (e.g., Cas9, Cas12) can refer to the wild-type or a modified form of the Cas protein that can comprise an amino acid change such as a deletion, insertion, substitution, variant, mutation, fusion, chimera, or any combination thereof. In some embodiments, a CRISPR protein-derived domain of a base editor can include all or a portion (e.g., a functional portion) of Cas9 from Corynebacterium ulcerans (NCBI Refs: NC_015683.1, NC_017317.1); Corynebacterium diphtheria (NCBI Refs: NC_016782.1, NC_016786.1); Spiroplasma syrphidicola (NCBI Ref: NC_021284.1); Prevotella intermedia ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 (NCBI Ref: NC_017861.1); Spiroplasma taiwanense (NCBI Ref: NC_021846.1); Streptococcus iniae (NCBI Ref: NC_021314.1); Belliella baltica (NCBI Ref: NC_018010.1); Psychroflexus torquis (NCBI Ref: NC_018721.1); Streptococcus thermophilus (NCBI Ref: YP_820832.1); Listeria innocua (NCBI Ref: NP_472073.1); Campylobacter jejuni (NCBI Ref: YP_002344900.1); Neisseria meningitidis (NCBI Ref: YP_002342100.1), Streptococcus pyogenes, or Staphylococcus aureus. Some aspects of the disclosure provide high fidelity Cas9 domains. High fidelity Cas9 domains are known in the art and described, for example, in Kleinstiver, B.P., et al. “High- fidelity CRISPR-Cas9 nucleases with no detectable genome-wide off-target effects.” Nature 529, 490-495 (2016); and Slaymaker, I.M., et al. “Rationally engineered Cas9 nucleases with improved specificity.” Science 351, 84-88 (2015); the entire contents of each of which are incorporated herein by reference. An Exemplary high fidelity Cas9 domain is provided in the Sequence Listing as SEQ ID NO: 233. In some embodiments, any of the Cas9 fusion proteins or complexes provided herein comprise one or more of a D10A, N497X, a R661X, a Q695X, and / or a Q926X mutation, or a corresponding mutation in any of the amino acid sequences provided herein, wherein X is any amino acid.. Typically, Cas9 proteins, such as Cas9 from S. pyogenes (spCas9), require a “protospacer adjacent motif (PAM)” or PAM-like motif, which is a 2-6 base pair DNA sequence immediately following the DNA sequence targeted by the Cas9 nuclease in the CRISPR bacterial adaptive immune system. The presence of an NGG PAM sequence is required to bind a particular nucleic acid region, where the “N” in “NGG” is adenosine (A), thymidine (T), or cytosine (C), and the G is guanosine. In some embodiments, any of the fusion proteins or complexes provided herein may contain a Cas9 domain that is capable of binding a nucleotide sequence that does not contain a canonical (e.g., NGG) PAM sequence. Cas9 domains that bind to non-canonical PAM sequences have been described in the art and would be apparent to the skilled artisan. For example, Cas9 domains that bind non-canonical PAM sequences have been described in Kleinstiver, B. P., et al., “Engineered CRISPR-Cas9 nucleases with altered PAM specificities” Nature 523, 481-485 (2015); and Kleinstiver, B. P., et al., “Broadening the targeting range of Staphylococcus aureus CRISPR-Cas9 by modifying PAM recognition” Nature Biotechnology 33, 1293-1298 (2015); the entire contents of each are hereby incorporated by reference. In some embodiments, the napDNAbp is a circular permutant (e.g., SEQ ID NO: 238). ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 In some embodiments, the polynucleotide programmable nucleotide binding domain comprises a nickase domain. Herein the term “nickase” refers to a polynucleotide programmable nucleotide binding domain comprising a nuclease domain that is capable of cleaving only one strand of the two strands in a duplexed nucleic acid molecule (e.g., DNA). For example, where a polynucleotide programmable nucleotide binding domain comprises a nickase domain derived from Cas9, the Cas9-derived nickase domain can include a D10A mutation and a histidine at position 840. In another example, a Cas9-derived nickase domain comprises an H840A mutation, while the amino acid residue at position 10 remains a D. In some embodiments, a Cas9 nuclease has an inactive (e.g., an inactivated) DNA cleavage domain, that is, the Cas9 is a nickase, referred to as an “nCas9” protein (for “nickase” Cas9; SEQ ID NO: 201). The Cas9 nickase may be a Cas9 protein that is capable of cleaving only one strand of a duplexed nucleic acid molecule (e.g., a duplexed DNA molecule). In some embodiments the Cas9 nickase comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% identical to any one of the Cas9 nickases provided herein. Additional suitable Cas9 nickases will be apparent to those of skill in the art based on this disclosure and knowledge in the field and are within the scope of this disclosure. Also provided herein are base editors comprising a polynucleotide programmable nucleotide binding domain which is catalytically dead (i.e., incapable of cleaving a target polynucleotide sequence). For example, in the case of a base editor comprising a Cas9 domain, the Cas9 can comprise both a D10A mutation and an H840A mutation. In further embodiments, a catalytically dead polynucleotide programmable nucleotide binding domain comprises a point mutation (e.g., D10A or H840A) as well as a deletion of all or a portion (e.g., a functional portion) of a nuclease domain. dCas9 domains are known in the art and described, for example, in Qi et al., “Repurposing CRISPR as an RNA-guided platform for sequence-specific control of gene expression.” Cell.2013; 152(5):1173-83, the entire contents of which are incorporated herein by reference. The term “protospacer adjacent motif (PAM)” or PAM-like motif refers to a 2-6 base pair DNA sequence immediately following the DNA sequence targeted by a nucleic acid programmable DNA binding protein. In some embodiments, the PAM can be a 5′ PAM (i.e., located upstream of the 5′ end of the protospacer). In other embodiments, the PAM can be a 3′ PAM (i.e., located downstream of the 5′ end of the protospacer). The PAM sequence can be any PAM sequence known in the art. Suitable PAM sequences include, but are not limited ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 to, NGG, NGA, NGC, NGN, NGT, NGTT, NGCG, NGAG, NGAN, NGNG, NGCN, NGCG, NGTN, NNGRRT, NNNRRT, NNGRR(N), TTTV, TYCV, TYCV, TATV, NNNNGATT, NNAGAAW, or NAAAAC. Y is a pyrimidine; N is any nucleotide base; W is A or T. A base editor provided herein may comprise a CRISPR protein-derived domain that is capable of binding a nucleotide sequence that contains a canonical or non-canonical protospacer adjacent motif (PAM) sequence. In some embodiments, the PAM is an “NRN” PAM where the “N” in “NRN” is adenine (A), thymine (T), guanine (G), or cytosine (C), and the R is adenine (A) or guanine (G); or the PAM is an “NYN” PAM, wherein the “N” in NYN is adenine (A), thymine (T), guanine (G), or cytosine (C), and the Y is cytidine (C) or thymine (T), for example, as described in R.T. Walton et al., 2020, Science, 10.1126 / science.aba8853 (2020), the entire contents of which are incorporated herein by reference. Several PAM variants are described in Table 3 below. Table 3. Cas9 proteins and corresponding PAM sequences. N is A, C, T, or G; and V is A, C, or G. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 In some embodiments, the PAM is NGC. In some embodiments, the NGC PAM is recognized by a Cas9 variant. In some embodiments, the NGC PAM Cas9 variant includes one or more amino acid substitutions selected from D1135M, S1136Q, G1218K, E1219F, A1322R, D1332A, R1335E, and T1337R (collectively termed “MQKFRAER”) of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, the Cas9 variant contains one or more amino acid substitutions selected from D1135V, G1218R, R1335Q, and T1337R (collectively termed VRQR) of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, the Cas9 variant contains one or more amino acid substitutions selected from D1135V, G1218R, R1335E, and T1337R (collectively termed VRER) of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, the Cas9 variant contains one or more amino acid substitutions selected from E782K, N968K, and R1015H (collectively termed KHH) of saCas9 (SEQ ID NO: 218). In some embodiments, the Cas9 variant includes one or more amino acid substitutions selected from D1135M, S1136Q, G1218K, E1219S, R1335E, and T1337R (collectively termed “MQKSER”) of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some cases, a Cas9 variant has specificity for the PAM 5′-NGC-3′. In some embodiments, a Cas9 variant includes one or more amino acid substitutions selected from D1135M, S1136Y, G1218K, E1219F, A1322R, D1332A, R1335E, and T1337K of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, the a Cas9 variant includes one or more amino acid substitutions selected from D1135L, S1136Y, G1218K, E1219F, A1322R, D1332A, R1335E, and T1337R of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, a Cas9 variant includes one or more amino acid substitutions selected from D1135M, S1136Y, G1218K, E1219F, A1322R, D1332A, R1335E, and T1337K of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, a Cas9 variant includes one or more amino acid substitutions selected from D1135L, S1136Y, G1218K, E1219F, A1283D, A1322R, D1332A, R1335E, and T1337K of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, a Cas9 variant includes one or more amino acid substitutions selected from A61R, L1111R, D1135L, S1136W, G1218K, E1219Q, N1317R, A1322R, R1333P, R1335Q, and T1337R of spCas9 (SEQ ID No: 197) (SpRY), or a corresponding mutation in another Cas9. In some embodiments, a Cas9 variant includes one or more amino acid substitutions selected from D1135L, S1136Q, G1218K, E1219F, ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 E1250K, A1283D, A1322R, D1332A, R1335E, and T1337K of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, a Cas9 variant includes one or more amino acid substitutions selected from D1135M, S1136Y, G1218K, E1219F, E1250K, A1283D, A1322R, D1332A, R1335E, and T1337R of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, a Cas9 variant includes one or more amino acid substitutions selected from R765A, Q768A, D1135L, S1136Y, G1218K, A1283D, E1219F, A1322R, D1332A, R1335E, and T1337K of spCas9 (SEQ ID No: 197), or a corresponding mutation in another Cas9. In some embodiments, any of the Cas9 proteins provided herein, including an SpCas9 comprises any one, two, three, four, five, six, seven, eight, nine, or ten of the following amino acid substitutions in a corresponding residue: R765A, Q768A, W1126R, R1359W, E1250K, A1239T, A1239V, A1283D, R1335D, D1135L, D1135M, D1135R, D1135W, S1136H, S1136Q, S1136Y, G1218D, G1218K, G1218R, G1218E, G1218L, E1219F, E1219K, E1219N, A1322A, A1322R, A1322K, D1332A, R1335V, T1337K, T1337T, D1332A, D1135V and T1337R. In some embodiments, a CRISPR protein-derived domain of a base editor comprises all or a portion (e.g., a functional portion) of a Cas9 protein with a canonical PAM sequence (NGG). In other embodiments, a Cas9-derived domain of a base editor can employ a non- canonical PAM sequence. Such sequences have been described in the art and would be apparent to the skilled artisan. For example, Cas9 domains that bind non-canonical PAM sequences have been described in Kleinstiver, B. P., et al., “Engineered CRISPR-Cas9 nucleases with altered PAM specificities” Nature 523, 481-485 (2015); and Kleinstiver, B. P., et al., “Broadening the targeting range of Staphylococcus aureus CRISPR-Cas9 by modifying PAM recognition” Nature Biotechnology 33, 1293-1298 (2015); R.T. Walton et al. “Unconstrained genome targeting with near-PAMless engineered CRISPR-Cas9 variants” Science 10.1126 / science.aba8853 (2020); Hu et al. “Evolved Cas9 variants with broad PAM compatibility and high DNA specificity,” Nature, 2018 Apr.5, 556(7699), 57-63; Miller et al., “Continuous evolution of SpCas9 variants compatible with non-G PAMs” Nat. Biotechnol., 2020 Apr;38(4):471-481; the entire contents of each are hereby incorporated by reference. Fusion Proteins or Complexes Comprising a NapDNAbp and a Cytidine Deaminase and / or Adenosine Deaminase Some aspects of the disclosure provide fusion proteins or complexes comprising a Cas9 domain or other nucleic acid programmable DNA binding protein (e.g., Cas12) and one ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 or more cytidine deaminase, adenosine deaminase, or cytidine adenosine deaminase domains. It should be appreciated that the Cas9 domain may be any of the Cas9 domains or Cas9 proteins (e.g., dCas9 or nCas9) provided herein. In some embodiments, any of the Cas9 domains or Cas9 proteins (e.g., dCas9 or nCas9) provided herein may be fused with any of the cytidine deaminases and / or adenosine deaminases provided herein. The domains of the base editors disclosed herein can be arranged in any order. In some embodiments, the fusion proteins or complexes comprising a cytidine deaminase or adenosine deaminase and a napDNAbp (e.g., Cas9 or Cas12 domain) do not include a linker sequence. In some embodiments, a linker is present between the cytidine or adenosine deaminase and the napDNAbp. In some embodiments, cytidine or adenosine deaminase and the napDNAbp are fused via any of the linkers provided herein. For example, in some embodiments the cytidine or adenosine deaminase and the napDNAbp are fused via any of the linkers provided herein. It should be appreciated that the fusion proteins or complexes of the present disclosure may comprise one or more additional features. For example, in some embodiments, the fusion protein or complex may comprise inhibitors, cytoplasmic localization sequences, export sequences, such as nuclear export sequences, or other localization sequences, as well as sequence tags that are useful for solubilization, purification, or detection of the fusion proteins or complexes. Suitable protein tags provided herein include, but are not limited to, biotin carboxylase carrier protein (BCCP) tags, myc-tags, calmodulin-tags, FLAG-tags, hemagglutinin (HA)-tags, polyhistidine tags, also referred to as histidine tags or His-tags, maltose binding protein (MBP)-tags, nus-tags, glutathione-S- transferase (GST)-tags, green fluorescent protein (GFP)-tags, thioredoxin-tags, S-tags, Softags (e.g., Softag 1, Softag 3), strep-tags , biotin ligase tags, FlAsH tags, V5 tags, and SBP-tags. Additional suitable sequences will be apparent to those of skill in the art. In some embodiments, the fusion protein or complex comprises one or more His tags. Exemplary, yet nonlimiting, fusion proteins are described in International PCT Application Nos. PCT / US2017 / 045381, PCT / US2019 / 044935, and PCT / US2020 / 016288, each of which is incorporated herein by reference for its entirety. Fusion Proteins or Complexes with Internal Insertions Provided herein are fusion proteins or complexes comprising a heterologous polypeptide fused to a nucleic acid programmable nucleic acid binding protein, for example, a napDNAbp. The heterologous polypeptide can be fused to the napDNAbp at a C-terminal ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 end of the napDNAbp, an N-terminal end of the napDNAbp, or inserted at an internal location of the napDNAbp. In some embodiments, the heterologous polypeptide is a deaminase (e.g., cytidine or adenosine deaminase) or a functional fragment thereof. For example, a fusion protein may comprise a deaminase flanked by an N- terminal fragment and a C-terminal fragment of a Cas9 or Cas12 (e.g., Cas12b / C2c1), polypeptide. The deaminase can be a circular permutant deaminase. In some embodiments, the deaminase is a circular permutant TadA, circularly permutated at amino acid residue 116, 136, or 65 as numbered in a TadA reference sequence. The fusion protein or complexes can comprise more than one deaminase. The fusion protein or complex can comprise, for example, 1, 2, 3, 4, 5 or more deaminases. The deaminases in a fusion protein or complex can be adenosine deaminases, cytidine deaminases, or a combination thereof. In some embodiments, the napDNAbp in the fusion protein or complex contains a Cas9 polypeptide or a fragment thereof. The Cas9 polypeptide can be a variant Cas9 polypeptide. The Cas9 polypeptide can be a circularly permuted Cas9 protein. The heterologous polypeptide (e.g., deaminase) can be inserted in the napDNAbp (e.g., Cas9 or Cas12 (e.g., Cas12b / C2c1)) at a suitable location, for example, such that the napDNAbp retains its ability to bind the target polynucleotide and a guide nucleic acid. A deaminase (e.g., adenosine deaminase, cytidine deaminase, or adenosine deaminase and cytidine deaminase (dual deaminase)) can be inserted into a napDNAbp without compromising function of the deaminase (e.g., base editing activity) or the napDNAbp (e.g., ability to bind to target nucleic acid and guide nucleic acid). In some embodiments, the deaminase (e.g., adenosine deaminase, cytidine deaminase, or adenosine deaminase and cytidine deaminase) is inserted in regions of the Cas9 polypeptide comprising higher than average B-factors (e.g., higher B factors compared to the total protein or the protein domain comprising the disordered region). Cas9 polypeptide positions comprising a higher than average B-factor can include, for example, residues 768, 792, 1052, 1015, 1022, 1026, 1029, 1067, 1040, 1054, 1068, 1246, 1247, and 1248 as numbered in SEQ ID NO: 197. Cas9 polypeptide regions comprising a higher than average B-factor can include, for example, residues 792-872, 792-906, and 2-791 as numbered in SEQ ID NO: 197. In some embodiments, a heterologous polypeptide (e.g., deaminase) is inserted in a flexible loop of a Cas9 polypeptide. The flexible loop portions can be selected from the group consisting of 530-537, 569-570, 686-691, 943-947, 1002-1025, 1052-1077, 1232-1247, or ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 1298-1300 as numbered in SEQ ID NO: 197, or a corresponding amino acid residue in another Cas9 polypeptide. The flexible loop portions can be selected from the group consisting of: 1-529, 538-568, 580-685, 692-942, 948-1001, 1026-1051, 1078-1231, or 1248- 1297 as numbered in SEQ ID NO: 197, or a corresponding amino acid residue in another Cas9 polypeptide. A heterologous polypeptide (e.g., adenine deaminase) can be inserted into a Cas9 polypeptide region corresponding to amino acid residues: 1017-1069, 1242-1247, 1052-1056, 1060-1077, 1002 – 1003, 943-947, 530-537, 568-579, 686-691, 1242-1247, 1298 – 1300, 1066-1077, 1052-1056, or 1060-1077 as numbered in SEQ ID NO: 197, or a corresponding amino acid residue in another Cas9 polypeptide. A heterologous polypeptide (e.g., adenine deaminase) can be inserted in place of a deleted region of a Cas9 polypeptide. The deleted region can correspond to an N-terminal or C-terminal portion of the Cas9 polypeptide. Exemplary internal fusions base editors are provided in Table 4A below: Table 4A: Insertion loci in Cas9 proteins A heterologous polypeptide (e.g., deaminase) can be inserted within a structural or functional domain of a Cas9 polypeptide. A heterologous polypeptide (e.g., deaminase) can be inserted between two structural or functional domains of a Cas9 polypeptide. A ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 heterologous polypeptide (e.g., deaminase) can be inserted in place of a structural or functional domain of a Cas9 polypeptide, for example, after deleting the domain from the Cas9 polypeptide. The structural or functional domains of a Cas9 polypeptide can include, for example, RuvC I, RuvC II, RuvC III, Rec1, Rec2, PI, or HNH. A fusion protein may comprise a linker between the deaminase and the napDNAbp polypeptide. The linker can be a peptide or a non-peptide linker. For example, the linker can be an XTEN, (GGGS)n(SEQ ID NO: 246),SGGSSGGS (SEQ ID NO: 330), (GGGGS)n(SEQ ID NO: 247), (G)n, (EAAAK)n (SEQ ID NO: 248), (GGS)n,SGSETPGTSESATPES (SEQ ID NO: 249). In some embodiments, the fusion protein comprises a linker between the N- terminal Cas9 fragment and the deaminase. In some embodiments, the fusion protein comprises a linker between the C-terminal Cas9 fragment and the deaminase. In some embodiments, the N-terminal and C-terminal fragments of napDNAbp are connected to the deaminase with a linker. In some embodiments, the N-terminal and C-terminal fragments are joined to the deaminase domain without a linker. In some embodiments, the fusion protein comprises a linker between the N-terminal Cas9 fragment and the deaminase but does not comprise a linker between the C-terminal Cas9 fragment and the deaminase. In some embodiments, the fusion protein comprises a linker between the C-terminal Cas9 fragment and the deaminase but does not comprise a linker between the N-terminal Cas9 fragment and the deaminase. In some embodiments, the napDNAbp in the fusion protein or complex is a Cas12 polypeptide, e.g., Cas12b / C2c1, or a functional fragment thereof capable of associating with a nucleic acid (e.g., a gRNA) that guides the Cas12 to a specific nucleic acid sequence. The Cas12 polypeptide can be a variant Cas12 polypeptide. In other embodiments, the N- or C- terminal fragments of the Cas12 polypeptide comprise a nucleic acid programmable DNA binding domain or a RuvC domain. In other embodiments, the fusion protein contains a linker between the Cas12 polypeptide and the catalytic domain. In other embodiments, the amino acid sequence of the linker isGGSGGS (SEQ ID NO: 250) or GSSGSETPGTSESATPESSG (SEQ ID NO: 251). In other embodiments, the linker is a rigid linker. In other embodiments of the above aspects, the linker is encoded byGGAGGCTCTGGAGGAAGC (SEQ ID NO: 252) orGGCTCTTCTGGATCTGAAACACCTGGCACAAGCGAGAGCGCCACCCCTGAGAGCTCTGGC (SEQ ID NO: 253). In other embodiments, the fusion protein or complex contains a nuclear localization signal (e.g., a bipartite nuclear localization signal). In other embodiments, the amino acid ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 sequence of the nuclear localization signal is MAPKKKRKVGIHGVPAA (SEQ ID NO: 261). In other embodiments of the above aspects, the nuclear localization signal is encoded by the following sequence: ATGGCCCCAAAGAAGAAGCGGAAGGTCGGTATCCACGGAGTCCCAGCAGCC (SEQ ID NO: 262). In other embodiments, the Cas12b polypeptide contains a mutation that silences the catalytic activity of a RuvC domain. In other embodiments, the Cas12b polypeptide contains D574A, D829A and / or D952A mutations. In some embodiments, the fusion protein or complex comprises a napDNAbp domain (e.g., Cas12-derived domain) with an internally fused nucleobase editing domain (e.g., all or a portion (e.g., a functional portion) of a deaminase domain, e.g., an adenosine deaminase domain). In some embodiments, the napDNAbp is a Cas12b. In some embodiments, the base editor comprises a BhCas12b domain with an internally fused TadA*8 domain inserted at the loci provided in Table 4B below. Table 4B: Insertion loci in Cas12b proteins In some embodiments, the base editing system described herein is an ABE with TadA inserted into a Cas9. Polypeptide sequences of relevant ABEs with TadA inserted into a Cas9 are provided in the attached Sequence Listing as SEQ ID NOs: 263-308. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Exemplary, yet nonlimiting, fusion proteins are described in International PCT Application Nos. PCT / US2020 / 016285 and U.S. Provisional Application Nos.62 / 852,228 and 62 / 852,224, the contents of which are incorporated by reference herein in their entireties. A to G Editing In some embodiments, a base editor described herein comprises an adenosine deaminase domain. Such an adenosine deaminase domain of a base editor can facilitate the editing of an adenine (A) nucleobase to a guanine (G) nucleobase by deaminating the A to form inosine (I), which exhibits base pairing properties of G. In some embodiments, an A-to- G base editor further comprises an inhibitor of inosine base excision repair, for example, a uracil glycosylase inhibitor (UGI) domain or a catalytically inactive inosine specific nuclease. Without wishing to be bound by any particular theory, the UGI domain or catalytically inactive inosine specific nuclease can inhibit or prevent base excision repair of a deaminated adenosine residue (e.g., inosine), which can improve the activity or efficiency of the base editor. A base editor comprising an adenosine deaminase can act on any polynucleotide, including DNA, RNA and DNA-RNA hybrids. In an embodiment an adenosine deaminase domain of a base editor comprises all or a portion (e.g., a functional portion) of an ADAT comprising one or more mutations which permit the ADAT to deaminate a target A in DNA. For example, the base editor can comprise all or a portion (e.g., a functional portion) of an ADAT from Escherichia coli (EcTadA) comprising one or more of the following mutations: D108N, A106V, D147Y, E155V, L84F, H123Y, I156F, or a corresponding mutation in another adenosine deaminase. Exemplary ADAT homolog polypeptide sequences are provided in the Sequence Listing as SEQ ID NOs: 1 and 309-315. The adenosine deaminase can be derived from any suitable organism (e.g., E. coli). In some embodiments, the adenosine deaminase is from Escherichia coli, Staphylococcus aureus, Salmonella typhi, Shewanella putrefaciens, Haemophilus influenzae, Caulobacter crescentus, or Bacillus subtilis. In some embodiments, the adenine deaminase is a naturally- occurring adenosine deaminase that includes one or more mutations corresponding to any of the mutations provided herein (e.g., mutations in ecTadA). The corresponding residue in any homologous protein can be identified by e.g., sequence alignment and determination of homologous residues. The mutations in any naturally-occurring adenosine deaminase (e.g., having homology to ecTadA) that correspond to any of the mutations described herein (e.g., any of the mutations identified in ecTadA) can be generated accordingly. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 In some embodiments, the adenosine deaminase comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% identical to any one of the amino acid sequences set forth in any of the adenosine deaminases provided herein. It should be appreciated that adenosine deaminases provided herein may include one or more mutations (e.g., any of the mutations provided herein). The disclosure provides any deaminase domains with a certain percent identify plus any of the mutations or combinations thereof described herein. In some embodiments, the adenosine deaminase comprises an amino acid sequence that has 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 21, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, or more mutations compared to a reference sequence, or any of the adenosine deaminases provided herein. It should be appreciated that any of the mutations provided herein (e.g., based on a TadA reference sequence, such as TadA*7.10 (SEQ ID NO: 1)) can be introduced into other adenosine deaminases, such as E. coli TadA (ecTadA), S. aureus TadA (saTadA), or other adenosine deaminases (e.g., bacterial adenosine deaminases). In some embodiments, the TadA reference sequence is TadA*7.10 (SEQ ID NO: 1). It would be apparent to the skilled artisan that additional deaminases may similarly be aligned to identify homologous amino acid residues that can be mutated as provided herein. Thus, any of the mutations identified in a TadA reference sequence can be made in other adenosine deaminases (e.g., ecTada) that have homologous amino acid residues. It should also be appreciated that any of the mutations provided herein can be made individually or in any combination in a TadA reference sequence or another adenosine deaminase. In some embodiments, the adenosine deaminase comprises an alteration or set of alterations selected from those listed in Tables 5A-5E below: Table 5A. Adenosine Deaminase Variants. Residue positions in the E. coli TadA variant (TadA*) are indicated. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Table 5B. TadA*8 Adenosine Deaminase Variants. Residue positions in the E. coli TadA variant (TadA*) are indicated. Alterations are referenced to TadA*7.10 (first row). Table 5C. TadA*9 Adenosine Deaminase Variants. Alterations are referenced to TadA*7.10. Additional details of TadA*9 adenosine deaminases are described in International PCT Application No. PCT / US2020 / 049975, which is incorporated herein by reference in its entirety for all purposes. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 In some embodiments, the adenosine deaminase comprises a TadA*8.20 adenosine deaminase variant further comprising an F149Y amino acid alteration. In some embodiments, the adenosine deaminase comprises a TadA*8.20 adenosine deaminase variant further comprising the amino acid alterations R147D, F149Y, T166I, and D167N (TadA*8.10+). In some embodiments, the adenosine deaminase comprises a TadA*8.20 adenosine deaminase variant further comprising the amino acid alterations S82T and F149Y (TadA*9v1). In some embodiments, the adenosine deaminase comprises a TadA*8.20 adenosine deaminase variant further comprising the amino acid alterations Y147D, F149Y, T166I, D167N and S82T (TadA*9v2). In some embodiments, the adenosine deaminase comprises one or more of M1I, M1S, S2A, S2E, S2H, S2R, S2L, E3L, V4D, V4E, V4M, V4K, V4S, V4T, V4A, E5K, F6S, F6G, F6H, F6Y, F6I, F6E, S7K, H8E, H8Y, H8H, H8Q, H8E, H8G, H8S, E9Y, E9K, E9V, E9E, Y10F, Y10W, Y10Y, M12S, M12L, M12R, M12W, R13H, R13I, R13Y, R13R, R13G, R13S, H14N, A15D, A15V, A15L, A15H, T17T, T17A, T17W, T17L, T17F, T17R, T17S, L18A, L18E, L18N, L18L, L18S, A19N, A19H, A19K, A19A, A19D, A19G, A19M, R21N, K20K, K20A, K20R, K20E, K20G, K20C, K20Q R21A, R21R, R21N, R21Y, R21C G22P, A22W, A22R, W23D, R23H, W23G, W23Q, W23L, W23R, W23H W23D W23M, W23W, W23I, D24E, D24G, D24W, D24D, D24R, E25F, E25M, E25D, E25A, E25G, E25R, E25E, E25H E25V, E25S, E25Y, R26D, R26E, R26G, R26N, R26Q, R26C, R26L, R26K, R26W, R26C, R26P, R26R, R26A, R26H, E27E, E27Q, E27H, E27C, E27G, E27K, E27S, E27P, E27R, E27L, E27V, E27D, V28V, V28A, V28C, V28G, V28P, V28S, V28T, P29V, P29P, P29A, P29G, P29K, P29L, V30V, V30I, V30L, V30F, V30G, V30A, V30M, L34S, L34V, L34L, L34M, L34W, L34G, H36E, H36V, L36H, H36L, H36N, N37N, N37H, N37R, N37T, N37S, N38G, N38R, N38N, N38E, V40I, W45A, W45W, W45R, W45L, W45N, N46N, N46M, N46P, N46G, N46L, N46R, N46V, R46W, R46F, R46Q, R46M, R47A, R47Q, R47F, R47K, R47P, R47W, R47M, R47R, R47G, R47S, R47V, R47H, P48T, P48L, P48A, P48I, P48S, P48R, P48K, P48D, P48E, P48H, P48G, P48P, P48N, I49G, I49H, I49V, I49F, I49H, I49I, I49M, I49N, I49K, I49Q, I49T, G50L, G50S, G50R, G50G, R51H, R51L, R51N, ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 L51W, R51Y, R51G, R51V, R51R, H52D, H52Y, H52I, H52H, D53D, D53E, D53G, D53P, P54C, P54T, P54P, P54E, A55H, T55A, T55I, T55V, T55G, T55T, A56A, A56H, A56W, A56E, A56S, H57P, H57A, H57H, H57N, A58G, A58E, A58A, A58R, E59A, E59G, E59I, E59Q, E59W, E59E, E59T, E59H, E59P, M61A, M61I, M61L, M61V, M61P, M61G, M61I, L63S, L63V, L63T, L63R, L63H, L63A, R64A, R64Q, R64R, R64D, Q65V, Q65H, Q65G, Q65P, Q65F, Q65Q, Q65R, G66V, G66E, G66T, G66G, G66C, G67G, G67W, G67I, G67A, G67D, G67L, G67V, L68Q, L68M, L68V, L68H, L68L, L68G,V69A, V69M, V69V, M70V, M70L, E70A, M70A, M70M, M70E, M70T, M70v, Q71M, Q71N, Q71L, Q71R, Q71Q, Q71I, N72A, N72K, N72S, N72D, N72Y, N72N, N72H, N72G, N72M, Y73G, Y73I, Y73K, Y73R, Y73S, Y73Y, Y73H, Y73A, R74A, R74Q, R74G, R74K, R74L, R74N, R74G, R74K, R74R, I76H, I76R, I76W, I76Y, I76V, I76Q, I76L, I76D, I76F, I76I, I76N, I76T, I76Y, D77G, D77D, D77A, D77Q, A78Y, A78T, A78G, A78A, A78I, T79M, T79R, T79L, T79T, L80M, L80Y, L80I, L80V, L80L, Y81D, Y81V, Y81Y, Y81M, V82A, V82S, V82G, V82T, V82V, V82Q, V82Y, T83L, T83F, T83T, T83N, L84E, L84F, L84Y, L84I, L84L, L84M, L84A, L84T, L84S, E85K, E85G, E85P, E85S, E85E, E85F, E85V, E85R, P86T, P86C, P86P, P86L, P86N, P86K, P86H, C87M, C87I, C87S, C87N, C87P, S87C, S87L, S87V, V88A, V88M, V88V, V88T, V88E, V88D, V88S, C90S, C90P, C90A, C90T, C90M, A91A, A91G, A91S, A91V, A91T, A91C, A91L, G92T, G92M, G92A, G92Y, G92G, A93I, A93C, A93M, A93V, A93A, M94M, M94T, M94A, M94V, M94L, M94I, M94H, I95S, I95G, I95L, I95H, I95V, H96A, H96L, H96R, H96S, H96H, H96N, H96E, S97C, S97G, S97I, S97M, S97R, S97S, S97P, R98K, R98I, R98N, R98Q, R98G, R98H, R98C, R98L, R98R, G100R, G100V, G100K, G100A, G100S, G100M, G100I, R101V, R101R, R101S, R101C, V102A, V102F, V102I, V102V, D103A, V103A, V103G, V103F, V103V, F104G, D104N, F104V, F104I, F104L, F104A, F104F, F104R, G105V, G105W, G105G, G105M, G105A, A106T, V106Q, V106F, V106W, V106M, A106A, A106Q, A106F, A106G, A106W, A106M, A106V, A106R, A106L, A106S, A106B, A106I, R107C, R107G, R107P, R107K, R107A, R107N, R107W, R107H, R107S, R107R, R107F, D108N, D108F, D108G, D108V, D108A, D108Y, D108H, D108I, D108K, D108L, D108M, D108Q, N108Q, N108F, N108W, N108M, N108K, D108K, D108F, D108M, D108Q, D108R, D108W, D108S, D108E, D108T, D108R, D108D, A109H, A109K, A109R, A109S, A109T, A109V, A109A, A109D, K110G, K110H, K110I, K110R, K110T, K110K, K110A, K110l, T111A, T111G, T111H, T111R, T111T, T111K, G112A, G112G, G112H, G112T, G112R, A113N, A114G, A114H, A114V, A114C, A114S, A114A, G115S, G115G, G115M, G115L, G115A, G115F, L117M, L117L, L117W, L117A, L117S, L117N, L117V, M118D, M118G, ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 M118K, M118N, M118V, M118M, M118L, M118R, D119L, D119N, D119S, D119V, D119D, V120H, V120L, V120V, V120T, V120A, V120E, V120G, V120D, L121D, L121M, L121N, L121K, L121L, H122H, H122N, H122P, H122R, H122S, H122Y, H122G, H122T, H122L, H123C, H123G, H123P, H123V, H123Y, Y123H, H123Y, H123H, P124P, P124H, P124A, P124Y, P124D, P124G, P124I, P124L, P124W, G125H, G125I, G125A, G125M, G125K, G125G, G125P, M126D, M126H, M126K, M126I, M126N, M126O, M126S, M126Y, M126M, M126G, N127H, N127S, N127D, N127K, N127R, N127N, N127I, N127P, N127M, H128R, H128N, H128L, H128H, R129H, R129Q, R129V, R129I, R129E, R129V, R129R, R129M, R129P, V130R, V130V, V130E, V130D, E131E, E131I, E131V, E131K, I132I, I132F, I132T, I132L, I132V, I132E, T133V, T133E, T133G, T133K, T133T, T133A, T133H, T133F, T133I, E134A, E134E, E134G, E134I, E134H, E134K, E134T, G135G, G135V, G135I, G135P, G135E, I136G, I136L, I136T, I136I , l137A, l137D, l137E, L137M, l137S, L137L, L137I , A138D, A138E, A138G, S138A, A138N, A138S, A138T, A138V, A138Y, A138A, A138M, A138L, D139E, D139I, D139C, D139L, D139M, D139D, D139G, D139H, D139A, E140A, E140C, E140L, E140R, E140K, E140E, E140D, C141S, C141A, C141C, C141V, C141E, A142N, A142D, A142G, A142A, A142L, A142S, A142T, A142N, A142S, A142V, A142E, A142C, A143D, A143E, A143G, , A143D, A143G, A143E, A143L, A143W, A143M, A143S, A143Q, A143R, A143A, A143I, L144S, L144L, L144T, L144A, L145A, L145F, L145G, L145D, L145L, L145C, L145E, L145s, C146R, S146A, S146C, S146D, S146F, S146R, S146T, S146D, S146G, S146S, S146L, D147D, D147L, D147F, D147G, D147Y, Y147T, Y147R, Y147D, D147R, D147Y, D147A, D147T, D147H, D147F, D147U, D147V, D147I, D147C, F148L, F148F, F148R, F148Y, F148A, F148T, F149C, F149M, F149R, F149Y, F149N, F149F, F149A, F149T, F149V R150R, R150M, R150D, R150F, M151F, M151P, M151R, M151V, M151M, M151E, R152C, R152F, R152H, R152P, R152R, R152P, R152Q, R152M, R152O, R153C, R153Q, R153R, R153V, R153E, R153A, R153P, Q154E, Q154H, Q154M, Q154R, Q154L, Q154S, Q154V, Q154Q, Q154F, Q154I, Q154A, Q154K, E155F, E155G, E155I, E155K, E155P, E155V, E155D, E155E, E155L, E155Q, I156V, I156A, I156I, I156L, I156F, I156D, I156K, I156N, I156R, I156Y, E157A, E157F, E157I, E157P, E157T, E157V, N157K, K157N, K157V, K157P, K157I, K157F, K157F, K157T, K157A, K157S, K157R, A158Q, A158K, A158V, A158A, A158D, A158S, A158T, A158N, Q159S, Q159Q, Q159A, Q159F, Q159K, Q159L, Q159N, K160A, K160S, K160E, K160K, K160N, K160F, K160Q, K161T, K161K, K161R, K161I, K161A, K161N, K161Q, K161S, K161T, A162D, A162Q, R162H, R162P, A162S, A162A, A162N, A162M, A162K, Q163G, Q163S, Q163Q, Q163A, Q163H, Q163N, Q163R, S164F, S164S, S164Q, ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 S164I, S164R, S164Y, S165S, S165P, S165Q, S165A, S165D, S165I, S165T, S165Y, T166T, T166Q, T166E, T166S, T166D, T166K, T166I, T166N, T166P, T166R, D167S D167D, D167I, D167G, D167T, D167A and / or D167N mutation in a TadA reference sequence (e.g., TadA*7.10,ecTadA, or TadA8e), and any alternative mutation at the corresponding position,or one or more corresponding mutations in another adenosine deaminase. Additional mutations are described in U.S. Patent Application Publication No. 2022 / 0307003 A1 U.S. Patent No.11,155,803, and International Patent Application Publications No. WO 2023 / 288304 A2, PCT / CN2022 / 143408, WO 2018 / 027078 A1, WO 2021 / 158921 A1 and WO 2023 / 034959 A2, the disclosures of which are incorporated herein by reference in their entirety for all purposes. In various embodiments, an adenosine deaminase of the disclosure lacks an N- terminal methionine. In some embodiments, the disclosure provides TadA variants comprising an alteration at an amino acid selected from one or more of L36, I76, V82, Y147, Q154, and N157 compared to TadA*7.10. In some embodiments, the disclosure provides TadA variants comprising one or more of the following alterations relative to TadA*7.10: L36H, I76Y, V82T, Y147T, Q154S, and N157K. In some embodiments, the disclosure provides TadA variants comprising the following alterations relative to TadA*7.10: L36H, I76Y, V82T, Y147T, Q154S, and N157K. In some embodiments, the disclosure provides TadA variants comprising the following alterations relative to TadA*7.10: F84Y, A109L, A109V, A109I, A109F, A109S, A109T, A109N, V155S, V155T, V155N, F156Y, F156W, F156R, F156N, and F156Q. In some embodiments, the disclosure provides TadA variants comprising the following alterations relative to TadA*7.10: E3N, E3K, E3G, F6A, H14D, L18A, W23I, W23R, P29T, P29Y, P29Q, V35Q, L36S, N38D, G42M, N46Y, P48A, G50A, H52L, A62V, L63R, L63F, Q65R, G67N, L68V, M70I, N72Y, T79H, Y81V, V82S, M94R, G100V, V102E, V102S, R107A, A114C, G115E, M118L, D119L, H122T, P124H, P124K, P124Q, H128R, V130F, I132K, I132T, E140L, A142N, A142S, L144Q, L145R, L145N, Y147A, F149A, R152P, F156N, and K160E. In some embodiments, the disclosure provides TadA variants comprising a V82T, Y147T, and / or a Q154S mutation. In some embodiments, the disclosure provides TadA variants comprising a V82T, Y147T, and / or a Q154S mutation. In some embodiments, the disclosure provides TadA*8.8 further comprising a V82T mutation. In some embodiments, the disclosure provides TadA*8.8 further comprising a V82T, a Y147T, and a Q154S mutation. In some embodiments, the disclosure provides TadA*8.17 further comprising a ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 V82T mutation. In some embodiments, the disclosure provides TadA*8.17 further comprising a V82T, a Y147T, and a Q154S mutation. In some embodiments, the disclosure provides TadA*8.20 further comprising a V82T mutation. In some embodiments, the disclosure provides TadA*8.20 further comprising a V82T, a Y147T, and a Q154S mutation. In embodiments, a variant of TadA*7.10 comprises one or more alterations selected from any of those alterations provided herein. In particular embodiments, an adenosine deaminase heterodimer comprises a TadA*8 domain and an adenosine deaminase domain selected from Staphylococcus aureus (S. aureus) TadA, Bacillus subtilis (B. subtilis) TadA, Salmonella typhimurium (S. typhimurium) TadA, Shewanella putrefaciens (S. putrefaciens) TadA, Haemophilus influenzae F3031 (H. influenzae) TadA, Caulobacter crescentus (C. crescentus) TadA, Geobacter sulfurreducens (G. sulfurreducens) TadA, or TadA*7.10. In some embodiments, the TadA*8 is a variant as shown in Table 5D. Table 5D shows certain amino acid position numbers in the TadA amino acid sequence and the amino acids present in those positions in the TadA-7.10 adenosine deaminase. Table 5D also shows amino acid changes in TadA variants relative to TadA-7.10 following phage-assisted non- continuous evolution (PANCE) and phage-assisted continuous evolution (PACE), as described in M. Richter et al., 2020, Nature Biotechnology, doi.org / 10.1038 / s41587-020- 0453-z, the entire contents of which are incorporated by reference herein. In some embodiments, the TadA*8 is TadA*8a, TadA*8b, TadA*8c, TadA*8d, or TadA*8e. In some embodiments, the TadA*8 is TadA*8e. In one embodiment, an adenosine deaminase is a TadA*8 that comprises or consists essentially of SEQ ID NO: 316 or a fragment thereof having adenosine deaminase activity. Table 5D. Select TadA*8 Variants ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 In some embodiments, the TadA variant is a variant as shown in Table 5E. Table 5E shows certain amino acid position numbers in the TadA amino acid sequence and the amino acids present in those positions in the TadA*7.10 adenosine deaminase. In some embodiments, the TadA variant is MSP605, MSP680, MSP823, MSP824, MSP825, MSP827, MSP828, or MSP829. In some embodiments, the TadA variant is MSP828. In some embodiments, the TadA variant is MSP829. Table 5E. TadA Variants Table 5F. TadA Variants ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Table 5F (CONTINUED). TadA Variants In particular embodiments, the fusion proteins or complexes comprise a single (e.g., provided as a monomer) TadA* (e.g., TadA*8 or TadA*9). Throughout the present disclosure, an adenosine deaminase base editor that comprises a single TadA* domain is indicates using the terminology ABEm or ABE#m, where “#” is an identifying number (e.g., ABE8.20m), where “m” indicates “monomer.” In some embodiments, the TadA* is linked to a Cas9 nickase. In some embodiments, the fusion proteins or complexes of the disclosure comprise as a heterodimer of a wild-type TadA (TadA(wt)) linked to a TadA*. Throughout the present disclosure, an adenosine deaminase base editor that comprises a single TadA* domain and a TadA(wt) domain is indicates using the terminology ABEd or ABE#d, where “#” is an identifying number (e.g., ABE8.20d), where “d” indicates “dimer.” In other embodiments, the fusion proteins or complexes of the disclosure comprise as a heterodimer of a TadA*7.10 linked to a TadA*. In some embodiments, the base editor is ABE8 comprising a TadA* variant monomer. In some embodiments, the base editor is ABE comprising a heterodimer of a TadA* and a TadA(wt). In some embodiments, the base editor is ABE comprising a heterodimer of a TadA* and TadA*7.10. In some embodiments, the base editor is ABE comprising a heterodimer of a TadA*. In some embodiments, the TadA* is selected from Tables 5A-5E. In some embodiments, the adenosine deaminase is expressed as a monomer. In other embodiments, the adenosine deaminase is expressed as a heterodimer. In some embodiments, the deaminase or other polypeptide sequence lacks a methionine, for example when included ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 as a component of a fusion protein. This can alter the numbering of positions. However, the skilled person will understand that such corresponding mutations refer to the same mutation. Any of the mutations provided herein and any additional mutations (e.g., based on the ecTadA amino acid sequence) can be introduced into any other adenosine deaminases. Any of the mutations provided herein can be made individually or in any combination in a TadA reference sequence or another adenosine deaminase (e.g., ecTadA). Details of A to G nucleobase editing proteins are described in International PCT Application No. PCT / US2017 / 045381 (WO2018 / 027078) and Gaudelli, N.M., et al., “Programmable base editing of A•T to G•C in genomic DNA without DNA cleavage” Nature, 551, 464-471 (2017), the entire contents of which are hereby incorporated by reference. C to T Editing In some embodiments, a base editor disclosed herein comprises a fusion protein or complex comprising cytidine deaminase capable of deaminating a target cytidine (C) base of a polynucleotide to produce uridine (U), which has the base pairing properties of thymine. In some embodiments, for example where the polynucleotide is double-stranded (e.g., DNA), the uridine base can then be substituted with a thymidine base (e.g., by cellular repair machinery) to give rise to a C:G to a T:A transition. In other embodiments, deamination of a C to U in a nucleic acid by a base editor cannot be accompanied by substitution of the U to a T. The deamination of a target C in a polynucleotide to give rise to a U is a non-limiting example of a type of base editing that can be executed by a base editor described herein. In another example, a base editor comprising a cytidine deaminase domain can mediate conversion of a cytosine (C) base to a guanine (G) base. For example, a U of a polynucleotide produced by deamination of a cytidine by a cytidine deaminase domain of a base editor can be excised from the polynucleotide by a base excision repair mechanism (e.g., by a uracil DNA glycosylase (UDG) domain), producing an abasic site. The nucleobase opposite the abasic site can then be substituted (e.g., by base repair machinery) with another base, such as a C, by for example a translesion polymerase. Although it is typical for a nucleobase opposite an abasic site to be replaced with a C, other substitutions (e.g., A, G or T) can also occur. Accordingly, in some embodiments a base editor described herein comprises a deamination domain (e.g., cytidine deaminase domain) capable of deaminating a target C to a U in a polynucleotide. Further, as described below, the base editor can comprise additional ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 domains which facilitate conversion of the U resulting from deamination to, in some embodiments, a T or a G. For example, a base editor comprising a cytidine deaminase domain can further comprise a uracil glycosylase inhibitor (UGI) domain to mediate substitution of a U by a T, completing a C-to-T base editing event. In another example, the base editor may comprise a uracil stabilizing protein as described herein. In another example, a base editor can incorporate a translesion polymerase to improve the efficiency of C-to-G base editing, since a translesion polymerase can facilitate incorporation of a C opposite an abasic site (i.e., resulting in incorporation of a G at the abasic site, completing the C-to-G base editing event). A base editor comprising a cytidine deaminase as a domain can deaminate a target C in any polynucleotide, including DNA, RNA and DNA-RNA hybrids. In some embodiments, a cytidine deaminase of a base editor comprises all or a portion (e.g., a functional portion) of an apolipoprotein B mRNA editing complex (APOBEC) family deaminase. APOBEC is a family of evolutionarily conserved cytidine deaminases. Members of this family are C-to-U editing enzymes. The N-terminal domain of APOBEC like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalytic domain. More specifically, the catalytic domain is a zinc dependent cytidine deaminase domain and is important for cytidine deamination. APOBEC family members include APOBEC1, APOBEC2, APOBEC3A, APOBEC3B, APOBEC3C, APOBEC3D (“APOBEC3E” now refers to this), APOBEC3F, APOBEC3G, APOBEC3H, APOBEC4, and Activation-induced (cytidine) deaminase. Other exemplary deaminases that can be fused to Cas9 according to aspects of this disclosure are provided below. In embodiments, the deaminases are activation-induced deaminases (AID). It should be understood that, in some embodiments, the active domain of the respective sequence can be used, e.g., the domain without a localizing signal (nuclear localization sequence, without nuclear export signal, cytoplasmic localizing signal). Some aspects of the present disclosure are based on the recognition that modulating the deaminase domain catalytic activity of any of the fusion proteins or complexes described herein, for example by making point mutations in the deaminase domain, affect the processivity of the fusion proteins (e.g., base editors) or complexes. For example, mutations that reduce, but do not eliminate, the catalytic activity of a deaminase domain within a base editing fusion protein or complexes can make it less likely that the deaminase domain will catalyze the deamination of a residue adjacent to a target residue, thereby narrowing the deamination window. The ability to narrow the deamination window can prevent unwanted ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 deamination of residues adjacent to specific target residues, which can reduce or prevent off- target effects. In some embodiments, an APOBEC deaminase incorporated into a base editor can comprise one or more mutations selected from the group consisting of R33A, K34A, E63A, H102P, D104N, H121R, H122R, H122L, D124N; R126A, R126E, R118A, W90A, W90Y, and R132E of rAPOBEC1; D316R, D317R, R320A, R320E, R313A, W285A, W285Y, and R326E of hAPOBEC3G; and any alternative mutation at the corresponding position, or one or more corresponding mutations in another APOBEC deaminase. In some embodiments, an APOBEC deaminase incorporated into a base editor can comprise one or more combinations of mutations selected from K34A, H122L, and D124N (AALN); H102P and D104N (evoFERNY derived from FERNY); W90Y and R126E (YE1); W90Y and R132E (YE2); R126E and R132E (EE); W90Y, R126E, and R132E (YEE), or rAPOBEC1; and any alternative mutation at the corresponding positions, or one or more corresponding mutations in another APOBEC deaminase. A number of modified cytidine deaminases are commercially available, including, but not limited to, SaBE3, SaKKH-BE3, VQR-BE3, EQR-BE3, VRER-BE3, YE1-BE3, EE-BE3, YE2-BE3, and YEE-BE3, which are available from Addgene (plasmids 85169, 85170, 85171, 85172, 85173, 85174, 85175, 85176, 85177). In some embodiments, a deaminase incorporated into a base editor comprises all or a portion (e.g., a functional portion) of an APOBEC1 deaminase. In some embodiments, the fusion proteins or complexes of the disclosure comprise one or more cytidine deaminase domains. In some embodiments, the cytidine deaminases provided herein are capable of deaminating cytosine or 5-methylcytosine to uracil or thymine. In some embodiments, the cytidine deaminases provided herein are capable of deaminating cytosine in DNA. The cytidine deaminase may be derived from any suitable organism. In some embodiments, the cytidine deaminase is a naturally-occurring cytidine deaminase that includes one or more mutations corresponding to any of the mutations provided herein. One of skill in the art will be able to identify the corresponding residue in any homologous protein, e.g., by sequence alignment and determination of homologous residues. Accordingly, one of skill in the art would be able to generate mutations in any naturally-occurring cytidine deaminase that corresponds to any of the mutations described herein. In some embodiments, the cytidine deaminase is from a prokaryote. In some embodiments, the cytidine deaminase is from a bacterium. In some embodiments, the cytidine deaminase is from a mammal (e.g., human). ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 In some embodiments, the cytidine deaminase comprises an amino acid sequence that is at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% identical to any one of the cytidine deaminase amino acid sequences set forth herein. It should be appreciated that cytidine deaminases provided herein may include one or more mutations (e.g., any of the mutations provided herein). Some embodiments provide a polynucleotide molecule encoding the cytidine deaminase nucleobase editor polypeptide of any previous aspect or as delineated herein. In some embodiments, the polynucleotide is codon optimized. In embodiments, a fusion protein of the disclosure comprises two or more nucleic acid editing domains. Details of C to T nucleobase editing proteins are described in International PCT Application No. PCT / US2016 / 058344 (WO2017 / 070632) and Komor, A.C., et al., “Programmable editing of a target base in genomic DNA without double-stranded DNA cleavage” Nature 533, 420-424 (2016), the entire contents of which are hereby incorporated by reference. Further non-limiting examples of C to T nucleobase editing proteins are described in PCT Applications No. PCT / US2020 / 062428 and PCT / US2019 / 033848, the entire contents of which are hereby incorporated by reference. Cytidine Adenosine Base Editors (CABEs) In some embodiments, a base editor described herein comprises an adenosine deaminase variant that has increased cytidine deaminase activity. Such base editors may be referred to as “cytidine adenosine base editors (CABEs)” or “cytosine base editors derived from TadA* (CBE-Ts),” and their corresponding deaminase domains may be referred to as “TadA* acting on DNA cytosine (TADC)” domains or TadA-derived cytidine deaminases (TadA-CD). Base editors containing adenosine deaminase variants having both cytidine deamianse and adenosine deaminase activity (i.e., TadA-Dual deaminases) may be referred to as TadA-based dual editors (TadDE). In some instances, an adenosine deaminase variant has both adenine and cytosine deaminase activity (i.e., is a dual deaminase). In some embodiments, the adenosine deaminase variants deaminate adenine and cytosine in DNA. In some embodiments, the adenosine deaminase variants deaminate adenine and cytosine in single-stranded DNA. In some embodiments, the adenosine deaminase variants deaminate adenine and cytosine in RNA. In some embodiments, the adenosine deaminase variant predominantly deaminates cytosine in DNA and / or RNA (e.g., greater than 30%, 40%, 50%, ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 60%, 70%, 80%, 90%, 95%, or 99% of all deaminations catalyzed by the adenosine deaminase variant, or the number of cytosine deaminations catalyzed by the variant is about or at least about 2-fold, 3-fold, 4-fold, 5-fold, 6-fold, 7-fold, 8-fold, 9-fold, 10-fold, 25-fold, 50-fold, 75-fold, 100-fold, 500-fold, or 1,000-fold greater than the number adenine deaminations catalyzed by the variant). In some embodiments, the adenosine deaminase variant has approximately equal cytosine and adenosine deaminase activity (e.g., the two activities are within about 10% or 20% of each other). In some embodiments, the adenosine deaminase variant has predominantly cytosine deaminase activity, and little, if any, adenosine deaminase activity. In some embodiments, the adenosine deaminase variant has cytosine deaminase activity, and no significant or no detectable adenosine deaminase activity. In some embodiments, the target polynucleotide is present in a cell in vitro or in vivo. In some embodiments, the cell is a bacteria, yeast, fungi, insect, plant, or mammalian cell. Examples of adenosine deaminase variants having increased cytidine deaminase activity include those described in International Patent Application Publications No. WO 2024 / 040083 and WO 2022 / 204574, the disclosures of which are hereby incorporated by reference in their entireties for all purposes. In some embodiments, the CABE comprises a bacterial TadA deaminase variant (e.g., ecTadA). In some embodiments, the CABE comprises a truncated TadA deaminase variant. In some embodiments, the CABE comprises a fragment of a TadA deaminase variant. In some embodiments, the CABE comprises a TadA*8.20 variant. In some embodiments, an adenosine deaminase variant of the disclosure is a TadA adenosine deaminase comprising one or more alterations that increase cytosine deaminase activity (e.g., at least about 10-fold, 20-fold, 30-fold, 40-fold, 50-fold, 60-fold, 70-fold or more increase) while maintaining adenosine deaminase activity (e.g., at least about 30%, 40%, 50% or more of the activity of a reference adenosine deaminase (e.g., TadA*8.20 or TadA*8.19)). In some instances, the adenosine deaminase variant comprises one or more alterations that increase cytosine deaminase activity (e.g., at least about 10-fold, 20-fold, 30- fold, 40-fold, 50-fold, 60-fold, 70-fold or more increase) relative to the activity of a reference adenosine deaminase and comprise undetectable adenosine deaminase activity or adenosine deaminase activity that is less than 30%, 20%, 10%, or 5% of that of a reference adenosine deaminase. In some embodiments, the reference adenosine deaminase is TadA*8.20 or TadA*8.19. In some embodiments, the adenosine deaminase variant is an adenosine deaminase comprising two or more alterations at an amino acid position selected from the group ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 consisting of 2, 4, 6, 8, 13, 17, 23, 27, 29, 30, 47, 48, 49, 67, 76, 77, 82, 84, 96, 100, 107, 112, 114, 115, 118, 119, 122, 127, 142, 143, 147, 149, 158, 159, 162165, 166, and 167, of an amino acid sequence having at least about 70%, 75%, 80%, 85%, 90%, 95%, 98%, 99% or greater identity to SEQ ID NO: 1, or a corresponding alteration in another deaminase. I In some embodiments, the adenosine deaminase variant is an adenosine deaminase comprising one or more alterations selected from the group consisting of S2H, V4K, V4S, V4T, V4Y, F6G, F6H, F6Y, H8Q, R13G, T17A, T17W, R23Q, E27C, E27G, E27H, E27K, E27Q, E27S, E27G, P29A, P29G, P29K, V30F, V30I, R47G, R47S, A48G, I49K, I49M, I49N, I49Q, I49T, G67W, I76H, I76R, I76W, Y76H, Y76R, Y76W, F84A, F84M, H96N, G100A, G100K, T111H, G112H, A114C, G115M, M118L, H122G, H122R, H122T, N127I, N127K, N127P, A142E, R147H, A158V, Q159S, A162C, A162N, A162Q, and S165P of an amino acid sequence having at least about 70%, 75%, 80%, 85%, 90%, 95%, 98%, 99% or greater identity to SEQ ID NO: 1, or a corresponding alteration in another deaminase. In some embodiments, the adenosine deaminase variant is an adenosine deaminase comprising an amino acid alteration or combination of amino acid alterations selected from those listed in any of Tables 6A-6F. The residue identity of exemplary adenosine deaminase variants that are capable of deaminating adenine and / or cytidine in a target polynucleotide (e.g., DNA) is provided in Tables 6A-6F below. Further examples of adenosine deaminase variants include the following variants of 1.17 (see Table 6A): 1.17+E27H; 1.17+E27K; 1.17+E27S; 1.17+E27S+I49K; 1.17+E27G; 1.17+I49N; 1.17+E27G+I49N; and 1.17+E27Q. In some embodiments, any of the amino acid alterations provided herein are substituted with a conservative amino acid. Additional mutations known in the art can be further added to any of the adenosine deaminase variants provided herein. In some embodiments, the base editor systems comprising a CABE provided herein have at least about a 30%, 40%, 50%, 60%, 70% or more C to T editing activity in a target polynucleotide (e.g., DNA). In some embodiments, a base editor system comprising a CABE as provided herein has an increased C to T base editing activity (e.g., increased at least about 30-fold, 40-fold, 50-fold, 60-fold, 70-fold or more) relative to a reference base editor system comprising a reference adenosine deaminase (e.g., TadA*8.20 or TadA*8.19). ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Table 6A. Adenosine Deaminase Variants. Mutations are indicated with reference to TadA*8.20. “S” indicates “Surface,” and “NAS” indicates “Near Active Site.” Table 6A (continued). Adenosine Deaminase Variants. Mutations are indicated with reference to TadA*8.20. “I” indicates “Internal,” “S” indicates “Surface,” and “NAS” indicates “Near Active Site.” ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Table 6B. Adenosine deaminase variants. Mutations are indicated with reference to TadA*8.20. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Table 6C. Adenosine deaminase variants. Mutations are indicated with reference to variant 1.2 (Table 6A) . ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Table 6C. (CONTINUED) ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Table 6D. Adenosine deaminase variants. Mutations are indicated with reference to TadA*8.20. ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 Table 6E. Hybrid constructs. Mutations are indicated with reference to TadA*7.10. Table 6F. Base editor variants. Mutations are indicated with reference to TadA*8.19 / 8.20. A TadA-derived cytidine deaminase (e.g., TadA-CD), according to certain embodiments, comprises an amino acid sequence that is at least 80% identical, at least 85% identical, at least 90% identical, at least 95% identical, at least 98% identical, at least 99% ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 identical, and at least 99.5% identical to the amino acid sequence of SEQ ID NO: 541, wherein residue 27 of SEQ ID NO: 541541 is any amino acid expect for E (glutamic acid). TadA-CDs with other sequence homologies are also possible. For example, in certain embodiments, the TadA-derived cytidine deaminase (e.g., TadA-CD) comprises an amino acid sequence that is at least 80% identical, at least 85% identical, at least 90% identical, at least 95% identical, at least 98% identical, at least 99% identical, and at least 99.5% identical to the amino acid sequence of SEQ ID NO: 541, wherein residue 28 of SEQ ID NO: 541 is any amino acid expect for V (valine). In another exemplary embodiment, the TadA-derived cytidine deaminase is at least 80% identical, at least 85% identical, at least 90% identical, at least 95% identical, at least 98% identical, at least 99% identical, and at least 99.5% identical to the amino acid sequence of SEQ ID NO: 541, wherein residue 96 of SEQ ID NO: 541 is any amino acid expect for H (histidine). In another exemplary embodiment, the TadA-derived cytidine deaminase is at least 80% identical, at least 85% identical, at least 90% identical, at least 95% identical, at least 98% identical, at least 99% identical, and at least 99.5% identical to the amino acid sequence of SEQ ID NO: 541, wherein residue 26 of SEQ ID NO: 541 is any amino acid expect for R (arginine). In various embodiments, the TadA-derived cytidine deaminase comprises an alteration at one or more of positions 26, 27, 28, 48, 73, or 96 compared to SEQ ID NO: 541. As will be appreciated by those of skill in the art, TadA-derived cytidine deaminases (e.g., TadA-CD) may comprise a plurality of mutations relative to the parent adenosine deaminase (e.g., TadA-8e). In some embodiments, the deaminase of the instant application (e.g., TadA-CD) comprises mutations at residues E27, V28, and H96. In some embodiments, the disclosed deaminase further comprises at least one mutation at a residue selected from R26, M61, Y73, I76, M151, Q154, and A158, in the amino acid s...

Claims

ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CLAIMS What is claimed:

1. A fusion polypeptide comprising a cognate peptide (cPep), a human leukocyte antigen E (HLA-E) polypeptide, or a fragment thereof, and a beta-2-microglobulin (B2M) polypeptide, or a fragment thereof, wherein the cPep comprises an amino acid sequence selected from the group consisting of: VMAPRTLFL (SEQ ID NO: 605); NMPARTVLF (SEQ ID NO: 444); VMAPRTLLL (SEQ ID NO: 434); VMAPRTLVL (SEQ ID NO: 435); VMAPRTLIL (SEQ ID NO: 436); VMAPRALLL (SEQ ID NO: 437); VTAPRTVLL (SEQ ID NO: 438); VMAPRTVLL (SEQ ID NO: 439); VTAPRTLLL (SEQ ID NO: 440); SAPLKTRFL (SEQ ID NO: 441); TGPWRSLWI (SEQ ID NO: 442); and TAPARTMFL (SEQ ID NO: 443).

2. The fusion polypeptide of claim 1, wherein the fusion polypeptide comprises from N- terminus to C-terminus: a) the cPep, the B2M polypeptide or fragment thereof, and the HLA-E polypeptide or fragment thereof; b) the cPep, the HLA-E polypeptide or fragment thereof, and the B2M polypeptide or functional fragment thereof; c) the B2M polypeptide or fragment thereof, the cPep, and the HLA-E polypeptide or fragment thereof; or d) the HLA-E polypeptide or fragment thereof, the cPep, the B2M polypeptide or fragment thereof.

3. The fusion polypeptide of claim 1 or claim 2 further comprising an N-terminal signal peptide.ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 4. The fusion polypeptide of claim 3, wherein the signal peptide is a B2M signal peptide.

5. The fusion polypeptide of claim 4, wherein the signal peptide comprises the amino acid sequenceMSRSVALAVLALLSLSGLEA (SEQ ID NO: 428).

6. The fusion polypeptide of claim 1 or claim 2, wherein the fusion polypeptide comprises one or more linkers.

7. The fusion polypeptide of claim 6, wherein the one or more linkers comprise the amino acid sequence (GGGGS)n (SEQ ID NO: 247), or the amino acid sequence (GGGGS)n (SEQ ID NO: 247) modified to include a cytidine amino acid.

8. The fusion polypeptide of claim 7, wherein n is between 1 and 5.

9. The fusion polypeptide of claim 8, wherein the linker comprises an amino acid sequence selected from the group consisting of: GGGGSGGGGSGGGGS (SEQ ID NO: 460); GCGGSGGGGSGGGGS (SEQ ID NO: 461); and GGGGSGGGGSGGGGSGGGGSG (SEQ ID NO: 464).

10. The fusion polypeptide of claim 1 or claim 2, wherein the fusion polypeptide comprises a linker connecting the cPep to the B2M polypeptide, or the fragment thereof.

11. The fusion polypeptide of claim 10, wherein the linker connecting the cPep to the B2M polypeptide, or the fragment thereof, comprises a cytidine amino acid, and wherein the HLA-E polypeptide, or the fragment thereof, comprises a cytidine amino acid capable of forming a disulfide bridge with the cytidine amino acid in the linker connecting the cPep to the B2M polypeptide.

12. The fusion polypeptide of claim 11, wherein the formation of the disulfide bridge mediates stable binding of the cPep by a binding groove of the HLA-E polypeptide, or the fragment thereof.ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 13. The fusion polypeptide of claim 11, wherein the linker connecting the cPep to the B2M polypeptide comprises the amino acid sequence GCGGSGGGGSGGGGS (SEQ ID NO: 461) and the HLA-E polypeptide comprises the amino acid sequence SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGCYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 457), or a functional fragment thereof.

14. The fusion polypeptide of claim 1 or claim 2, wherein the fusion polypeptide comprises a linker connecting the B2M polypeptide, or the fragment thereof, to the HLA-E polypeptide, or the fragment thereof.

15. The fusion polypeptide of claim 14, wherein the linker connecting the B2M polypeptide, or the fragment thereof, to the HLA-E polypeptide, or the fragment thereof, comprises the amino acid sequence GGGGSGGGGSGGGGSGGGGSG (SEQ ID NO: 464), or a fragment thereof.

16. The fusion polypeptide of claim 1 or claim 2, wherein the HLA-E polypeptide, or fragment thereof, comprises one or more amino acid alterations that reduce binding of a CD8 coreceptor to the fusion polypeptide.

17. The fusion polypeptide of claim 16, wherein the one or more amino acid alterations are selected from the group consisting of D227K, T228A, and A245V referenced to the following amino acid sequence, where the N-terminal S is position 2: SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 456).ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 18. The fusion polypeptide of claim 17, wherein the HLA-E polypeptide further comprises a Y83C amino acid alteration referenced to SEQ ID NO: 456, where the N- terminal S is position 1.

19. The fusion polypeptide of any one of claims 16 to 18, wherein the fusion polypeptide has reduced immunogenicity relative to a fusion polypeptide comprising an HLA-E polypeptide lacking one or more of the amino acid alterations.

20. The fusion polypeptide of claim 1 or claim 2, wherein the HLA-E polypeptide, or fragment thereof, comprises an amino acid sequence having at least 85% sequence identity to one of the following sequences, or a fragment thereof: SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGYYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 456); SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGCYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 457); and SHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRE TRSARDTAQIFRVNLRTLRGCYNQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLT LNEDLRSWTAVDTAAQISEQKSNDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKT HVTHHPISDHEATLRCWALGFYPAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVV PSGEEQRYTCHVQHEGLPEPVTLRWKPASQPTIPI (SEQ ID NO: 618).

21. The fusion polypeptide of claim 1 or claim 2, wherein the B2M polypeptide, or fragment thereof, comprises an amino acid sequence having at least 85% sequence identity to the following sequence, or a fragment thereof: IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSF YLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM (SEQ ID NO: 427).ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 22. The fusion polypeptide of claim 1 or claim 2, wherein the HLA-E polypeptide lacks a transmembrane domain.

23. The fusion polypeptide of claim 1 or claim 2 further comprising a transmembrane domain N-terminal to the HLA-E polypeptide, or the fragment thereof.

24. The fusion polypeptide of claim 1 or claim 2 further comprising a transmembrane domain C-terminal to the HLA-E polypeptide, or the fragment thereof.

25. The fusion polypeptide of claim 24, wherein the transmembrane domain comprises a cluster of differentiation 4 (CD4) transmembrane (CD4TM) domain, an HLA-E*01:03 transmembrane domain, or a CD8a transmembrane domain.

26. The fusion polypeptide of claim 25, wherein the CD4TM domain comprises the following sequence with up to 4 total amino acid alterations: MALIVLGGVAGLLLFIGLGIFF (SEQ ID NO: 433).

27. The fusion polypeptide of claim 26, wherein the CD4TM is fused at the C-terminus to a peptide comprising the following amino acid sequence:CVRC (SEQ ID NO: 466).

28. The fusion polypeptide of claim 1 or claim 2, further comprising a polypeptide comprising an amino acid sequence with at least 85% identity to one of the following amino acid sequences, wherein the polypeptide is C-terminal to the HLA-E polypeptide: VGIIAGLVLLGSVVSGAVVAAVIWRKKSSGGKGGSYSKAEWSDSAQGSESHSL (SEQ ID NO: 619); IYIWAPLAGTCGVLLLSLVITLYC (SEQ ID NO: 620); and MALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 621).

29. A fusion polypeptide comprising an amino acid sequence with at least 85% sequence identity to a sequence selected from the group consisting of: BTx_CM525 MSRSVALAVLALLSLSGLEANMPARTVLFGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 490); BTx_CM499 MSRSVALAVLALLSLSGLEAVMAPRTLLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 469); BTx_CM500 MSRSVALAVLALLSLSGLEAVMAPRTLVLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 470); BTx_CM501 MSRSVALAVLALLSLSGLEAVMAPRTLILGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 471); BTx_CM502ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 MSRSVALAVLALLSLSGLEAVMAPRALLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 472); BTx_CM503 MSRSVALAVLALLSLSGLEAVTAPRTVLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 473); BTx_CM504 MSRSVALAVLALLSLSGLEAVMAPRTVLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 474); BTx_CM505 MSRSVALAVLALLSLSGLEAVTAPRTLLLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFYATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 475); BTx_CM507 MSRSVALAVLALLSLSGLEASAPLKTRFLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 476); BTx_CM508 MSRSVALAVLALLSLSGLEATGPWRSLWIGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 477); BTx_CM509 MSRSVALAVLALLSLSGLEATAPARTMFLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 478); BTx_CM510 MSRSVALAVLALLSLSGLEANMPARTVLFGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGYYATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 479); BTx_CM514 MSRSVALAVLALLSLSGLEAVMAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 480); BTx_CM515 MSRSVALAVLALLSLSGLEAVMAPRTLVLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 481); BTx_CM516 MSRSVALAVLALLSLSGLEAVMAPRTLILGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 482); BTx_CM517 MSRSVALAVLALLSLSGLEAVMAPRALLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 483); BTx_CM518 MSRSVALAVLALLSLSGLEAVTAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 484); BTx_CM519 MSRSVALAVLALLSLSGLEAVMAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 485); BTx_CM520 MSRSVALAVLALLSLSGLEAVTAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 486); BTx_CM522ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 MSRSVALAVLALLSLSGLEASAPLKTRFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 487); BTx_CM523 MSRSVALAVLALLSLSGLEATGPWRSLWIGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 488); BTx_CM524 MSRSVALAVLALLSLSGLEATAPARTMFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 489); MSRSVALAVLALLSLSGLEAVMAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 606);ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 MSRSVALAVLALLSLSGLEAVMAPRTLVLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 607); MSRSVALAVLALLSLSGLEAVMAPRTLILGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 608); MSRSVALAVLALLSLSGLEAVMAPRALLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 609); MSRSVALAVLALLSLSGLEAVTAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 610); MSRSVALAVLALLSLSGLEAVMAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 611); MSRSVALAVLALLSLSGLEAVTAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 612); MSRSVALAVLALLSLSGLEASAPLKTRFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 613); MSRSVALAVLALLSLSGLEATGPWRSLWIGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 614); MSRSVALAVLALLSLSGLEATAPARTMFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCYATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 615); MSRSVALAVLALLSLSGLEANMPARTVLFGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 616); and MSRSVALAVLALLSLSGLEAVMAPRTLFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 617).

30. The fusion polypeptide of claim 29, wherein the amino acid sequence has at least 95% sequence identity to the sequence.

31. The fusion polypeptide of claim 29, wherein the amino acid sequence comprises or consists of the sequence.

32. The fusion polypeptide of claim 29, wherein the amino acid sequence has at least 95% sequence identity to one or more of the following sequences: BTx_CM525 MSRSVALAVLALLSLSGLEANMPARTVLFGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCYATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 490); MSRSVALAVLALLSLSGLEAVMAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 606); MSRSVALAVLALLSLSGLEAVMAPRTLVLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 607); MSRSVALAVLALLSLSGLEAVMAPRTLILGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 608); MSRSVALAVLALLSLSGLEAVMAPRALLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFYATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 609); MSRSVALAVLALLSLSGLEAVTAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 610); MSRSVALAVLALLSLSGLEAVMAPRTVLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 611); MSRSVALAVLALLSLSGLEAVTAPRTLLLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 612); and MSRSVALAVLALLSLSGLEAVMAPRTLFLGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENG KSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDMGGGGSGGGGSGGGGSGGGGSGSHSLKYFHTSVSRPGRGEPRFI SVGYVDDTQFVRFDNDAASPRMVPRAPWMEQEGSEYWDRETRSARDTAQIFRVNLRTLRGCY NQSEAGSHTLQWMHGCELGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISEQKS NDASEAEHQRAYLEDTCVEWLHKYLEKGKETLLHLEPPKTHVTHHPISDHEATLRCWALGFY PAEITLTWQQDGEGHTQKAELVETRPAGDGTFQKWVAVVVPSGEEQRYTCHVQHEGLPEPVT LRWKPASQPTIPIMALIVLGGVAGLLLFIGLGIFFCVRC (SEQ ID NO: 617).ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 33. A polynucleotide encoding the fusion polypeptide of any one of claims 1-32.

34. A polynucleotide encoding the fusion polypeptide of claim 1 and comprising a nucleotide sequence having at least 85% sequence identity to a sequence selected from the group consisting of: BTx_CM525 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAA TATGCCCGCTCGGACAGTATTGTTTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 512); BTx_CM499 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCCCCCAGGACTTTGCTTCTCGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCGATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 491); BTx_CM500 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT AATGGCCCCTCGAACCCTGGTACTCGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAAATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 492); BTx_CM501 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCTCCGCGAACTCTGATCCTCGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCATATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 493); BTx_CM502 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCGCCTCGAGCCCTGCTCCTTGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 494); BTx_CM503 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT TACCGCTCCTAGAACAGTCCTGCTGGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCTATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 495); BTx_CM504 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCACCGAGGACCGTACTCCTCGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGAATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 496); BTx_CM505 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT TACCGCGCCCCGGACTCTCCTTTTGGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGGATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 497); BTx_CM507 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCTC CGCCCCTCTGAAGACCCGATTTTTGGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 498); BTx_CM508 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAC CGGGCCTTGGCGGTCCCTCTGGATTGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGCATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 499); BTx_CM509 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAC TGCTCCGGCCAGGACCATGTTCCTTGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGCATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 500); BTx_CM510 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAA TATGCCCGCTCGGACAGTATTGTTTGGCGGCGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTACTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 501);ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 BTx_CM514 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCCCCCAGGACTTTGCTTCTCGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 502); BTx_CM515 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT AATGGCCCCTCGAACCCTGGTACTCGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCCATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 503); BTx_CM516 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCTCCGCGAACTCTGATCCTCGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACGATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 504); BTx_CM517 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCGCCTCGAGCCCTGCTCCTTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 505); BTx_CM518ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT TACCGCTCCTAGAACAGTCCTGCTGGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 506); BTx_CM519 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT GATGGCACCGAGGACCGTACTCCTCGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATCATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 507); BTx_CM520 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCGT TACCGCGCCCCGGACTCTCCTTTTGGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTACATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 508); BTx_CM522 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCTC CGCCCCTCTGAAGACCCGATTTTTGGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 509); BTx_CM523 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAC CGGGCCTTGGCGGTCCCTCTGGATTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCGATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAA GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGCTGATAGT AA (SEQ ID NO: 510); BTx_CM524 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAC TGCTCCGGCCAGGACCATGTTCCTTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAAATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 511).

35. The polynucleotide of claim 34, wherein the nucleotide sequence has at least 95% sequence identity to the sequence.

36. The polynucleotide of claim 34, wherein the nucleotide sequence comprises or consists of the sequence.

37. The polynucleotide of claim 34, wherein the nucleotide sequence has at least 95% sequence identity to the following sequence: BTx_CM525 ATGAGCCGGAGCGTGGCTCTGGCCGTGCTGGCCCTATTGTCTCTGAGCGGACTGGAAGCCAA TATGCCCGCTCGGACAGTATTGTTTGGCTGTGGCGGCTCCGGCGGTGGAGGCAGCGGAGGCG GCGGCAGCATCCAGAGAACCCCAAAGATCCAAGTGTACAGCAGACACCCTGCCGAGAACGGC AAGAGCAATTTCCTGAACTGCTACGTGTCCGGCTTTCACCCCAGCGACATCGAGGTGGATCT GCTGAAGAACGGCGAGAGAATCGAGAAGGTCGAACACAGCGATCTGAGCTTCAGCAAGGATT GGTCCTTCTACCTGCTGTACTACACCGAGTTCACCCCTACAGAGAAGGACGAGTACGCCTGC AGAGTGAACCACGTGACCCTGAGCCAGCCTAAGATCGTGAAGTGGGATAGAGATATGGGCGG CGGAGGCTCTGGAGGCGGAGGCTCTGGAGGAGGCGGCTCCGGCGGAGGCGGCTCCGGAAGCC ATTCTCTGAAGTACTTCCACACCAGCGTGTCCCGGCCTGGCAGAGGCGAACCCAGATTCATC AGCGTGGGCTATGTGGACGACACTCAGTTCGTGCGGTTCGACAATGACGCCGCCAGCCCTAG AATGGTGCCTAGGGCCCCTTGGATGGAACAGGAGGGCTCTGAATACTGGGACAGAGAGACAAATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 GAAGCGCCAGAGACACCGCCCAAATCTTCAGAGTGAACCTGCGCACCCTGCGGGGCTGTTAC AACCAGAGCGAGGCTGGCTCTCACACACTGCAGTGGATGCACGGCTGTGAACTGGGACCTGA CGGCAGATTTCTGAGAGGCTACGAGCAGTTCGCCTACGACGGCAAAGACTACCTGACCCTTA ATGAGGACCTCCGGAGCTGGACCGCCGTGGACACAGCCGCCCAGATCAGCGAGCAGAAAAGC AACGACGCCTCAGAAGCTGAGCACCAGCGGGCCTATCTGGAGGATACATGCGTGGAATGGCT GCATAAGTACCTGGAAAAAGGCAAGGAAACCCTGCTGCACCTGGAGCCTCCAAAAACCCACG TTACACACCACCCCATTAGCGACCACGAGGCAACCCTGAGATGTTGGGCCCTAGGCTTCTAC CCCGCTGAGATCACCCTGACATGGCAGCAGGATGGAGAGGGCCACACCCAGGACACCGAGCT GGTGGAAACCAGACCTGCTGGCGACGGAACATTCCAGAAGTGGGCCGCCGTGGTCGTGCCAT CTGGAGAAGAGCAGCGGTACACCTGCCACGTGCAGCACGAGGGCCTGCCTGAGCCTGTGACC CTGCGCTGGAAGCCCGCCAGCCAACCTACCATCCCCATCATGGCCCTGATCGTGCTGGGCGG CGTGGCCGGCCTGCTGCTGTTCATCGGCCTGGGCATTTTTTTCTGCGTGCGGTGC (SEQ ID NO: 512).

38. A vector comprising the polynucleotide of any one of claims 33-37.

39. The vector of claim 38, wherein the vector is a viral vector or a transposon.

40. The vector of claim 39, wherein the viral vector is a lentiviral vector.

41. The vector of claim 39, wherein the vector comprises a promoter.

42. An allogeneic modified immune cell comprising the fusion polypeptide of any one of claims 1-32, the polynucleotide of any one of claims 33-37, or the vector of any one of claims 38-41.

43. The allogeneic modified immune cell of claim 42, wherein the cell comprises nucleobase alterations resulting in reduced expression of a functional B2M polypeptide and / or a functional cluster of differentiation 58 (CD58) polypeptide relative to an unmodified immune cell.

44. The allogeneic modified immune cell of claim 43, wherein the cell comprises reduced expression levels of both the B2M and CD58 polypeptides relative to the unmodified immune cell and / or comprises undetectable levels of functional B2M or CD58 polypeptides.ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 45. The allogeneic modified immune cell of any one of claims 42-44, wherein the allogeneic modified immune cell is a T cell or a macrophage cell.

46. The allogeneic modified immune cell of any one of claims 42-45, wherein the allogeneic modified immune cell expresses a chimeric antigen receptor (CAR).

47. The allogeneic modified immune cell of any one of claims 42-46, wherein the modified immune cell shows reduced lysis by a natural killer cell relative to an allogeneic immune cell that does not express the fusion polypeptide and / or that express a CD58 polypeptide.

48. The allogeneic modified immune cell of claim 47, wherein lysis by the natural killer cell is reduced by at least 15%, 25%, 50%, or 75%.

49. A pharmaceutical composition comprising the fusion polypeptide of any one of claims 1-32, the polynucleotide of any one of claims 33-37, the vector of any one of claims 38-41, or the cell of any one of claims 42-48, and a pharmaceutically acceptable excipient.

50. A method for preparing a modified immune cell, the method comprising: a) modifying an immune cell to knock-out expression of an endogenous beta-2- microglobulin (B2M) polypeptide in the cell; and b) contacting the cell with a polynucleotide encoding the fusion polypeptide of any one of claims 1-32.

51. The method of claim 50 further comprising modifying the immune cell to knock-out expression of an endogenous cluster of differentiation 58 (CD58) polypeptide.

52. The method of claim 50 or claim 51, wherein modifying the cell to knock-out expression of the B2M polypeptide and / or CD58 polypeptide is carried out using base editing.

53. The method of claim 52, wherein the base editing comprises contacting the cell with a base editor and:ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 i) a guide polynucleotide targeting the base editor to effect an alteration of a nucleobase of an endogenous B2M gene in the cell, thereby knocking out expression of the endogenous B2M polypeptide in the cell; and / or ii) a guide polynucleotide targeting the base editor to effect an alteration of a nucleobase of an endogenous CD58 gene in the cell, thereby knocking out expression of the endogenous CD58 polypeptide in the cell.

54. The method of claim 53, wherein the guide polynucleotide of i) comprises a spacer having the nucleotide sequence CUUACCCCACUUAACUAUCU (SEQ ID NO: 467), and wherein the guide polynucleotide of ii) comprises a spacer having the nucleotide sequence ACUCACCAAAGCAGUGCAGC (SEQ ID NO: 468).

55. The method of claim 54, wherein the guide polynucleotides of i) and ii) each comprise a scaffold having the nucleotide sequence GUUUUAGAGCUAGAAAUAGCAAGUUAAAAUAAGGCUAGUCCGUUAUCAACUUGAAAAAGUGG CACCGAGUCGGUGCUUUU (SEQ ID NO: 317).

56. The method of any one of claims 53-55, wherein the base editor comprises a nucleic acid programmable DNA binding protein (napDNAbp) domain and an adenosine deaminase domain comprising an amino acid sequence with a least 90% sequence identity to the following amino acid sequence and further comprising the amino acid alterations I76Y, V82S, Y123H, Y147R, and Q145R: MSEVEFSHEYWMRHALTLAKRARDEREVPVGAVLVLNNRVIGEGWNRAIGLHDPTAHAEIMA LRQGGLVMQNYRLIDATLYVTFEPCVMCAGAMIHSRIGRVVFGVRNAKTGAAGSLMDVLHYP GMNHRVEITEGILADECAALLCYFFRMPRQVFNAQKKAQSSTD (SEQ ID NO: 1).

57. The method of claim 56, wherein the base editor comprises a single adenosine deaminase domain.

58. The method of claims 56 or claim 57, wherein the napDNAbp is a Cas9 nickase.

59. The method of any one of claims 50-58, further comprising expressing a chimeric antigen receptor in the cell.ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 60. The method of claim 59, wherein the chimeric antigen receptor targets an antigen expressed on the surface of a neoplastic cell.

61. The method of any one of claims 50-60, wherein the cell is a T cell or a macrophage cell.

62. The method of claim 61, wherein the T cell is a CD4+ or CD8+ T cell.

63. The method of any one of claims 50-60, wherein the modified immune cell shows reduced lysis by a natural killer cell relative to an allogeneic immune cell that does not express the fusion polypeptide and / or that express a CD58 polypeptide.

64. The method of claim 63, wherein lysis by the natural killer cell is reduced by at least 15%, 25%, 50%, or 75%.

65. A cell produced by the method of any one of claims 50-64.

66. A method for treating a subject having a neoplasia or an autoimmune disease, the method comprising administering to the subject the polynucleotide, vector, pharmaceutical composition, and / or cell of any of the above claims.

67. The method of claim 66, wherein NKG2A expression in natural killer cells (NK cells) from the subject is assessed prior to administering to the subject the polynucleotide, vector, pharmaceutical composition, and / or cell.

68. The method of claim 67, wherein the polynucleotide, vector, pharmaceutical composition, and / or cell is administered to the subject if at least 70% of the NK cells from the subject are determined to be NKG2A+.

69. The method of any one of claims 66-68, wherein the subject has been administered a lymphodepleting chemotherapy prior to being administered the polynucleotide, vector, pharmaceutical composition, and / or cell.ATTORNEY DOCKET NO.180802-056504 / PCT ELECTRONIC DEPOSIT DATE: January 7, 2025 70. A kit for use in the method of any one of claims 50-69, wherein the kit comprises the fusion polypeptide, polynucleotide, vector, pharmaceutical composition, and / or cell of any of the above claims and a container.

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