Methods comprising oncolytic viruses expressing bcmat and BCMA-targeted therapies

Abstract

Described herein, inter alia, are oncolytic viruses expressing a truncated human BCMA (BCMAt) and methods for treating a patient suffering from a solid tumor by administering an oncolytic virus expressing a truncated human BCMA and a BCMA-targeting therapy (e.g., a protein that binds a BCMA antigen, T cell engager targeted to BCMA, BCMA CAR immune cells, anti-BCMA antibody or antibody fragment).

Description

[0001] Attorney Docket No.40056-0104WO1 Methods Comprising Oncolytic Viruses Expressing BCMAt and BCMA-Targeted Therapies CLAIM OF PRIORITY This application claims the benefit of U.S. Provisional Application Serial No. 63 / 698,346, filed on September 24, 2024. The entire contents of the foregoing are incorporated herein by reference. TECHNICAL FIELD This disclosure relates to methods of treating a subject having a solid tumor comprising administering an oncolytic virus (OV) expressing a truncated B cell maturation antigen BCMA (BCMAt), and a BCMA-targeted therapy that binds to BCMAt (e.g., a protein, a bispecific T cell engager (TCE), immune cell expressing a CAR that binds to BCMA, a BCMA antibody or antibody drug conjugate). BACKGROUND A universal tumor-agnostic cancer therapy remains elusive in the field of immunotherapy. There have been impressive patient specific immunotherapies with recent FDA approvals including CAR T cell therapies. Limitations include the autologous nature of these cells and the length of time required for manufacturing. In contrast to autologous CAR T cells, the benefits of bispecific T cell engagers (called TCEs interchangeably herein) are their off-the-shelf availability and the ability to acutely tune targeting with dosing regimens [1, 2]. TCEs have emerged as a promising immunotherapy strategy for the treatment of B-cell hematological malignancies. Blinatumomab, an FDA approved TCE carrying CD19 and CD3 single chain variable fragments (scFvs) that drives endogenous T-cell mediated immune responses against malignant cells, has shown durable clinical responses for the treatment of B-cell acute lymphoblastic leukemia (B-ALL) and non-Hodgkin's lymphoma [3, 4]. Challenges facing solid tumor therapies using CAR T cells and TCE therapies are driven by a lack amenable and targetable tumor antigens [5, 6]. The shared expression of solid tumor antigens on normal tissue and their heterogeneous, and nonuniform, Attorney Docket No.40056-0104WO1 expression patterns on tumors limits the potential for effective and durable anti-tumor responses [7, 8]. Many solid tumors are also immunologically “cold” and limit T cell trafficking and anti-tumor functionality, a phenomenon uncommonly observed in hematological malignancies [9-11]. Further, the majority of solid tumors have a more complex microenvironment that represents a greater challenge for cancer therapies

[0024] . Thus, improved and more accessible immunotherapies remain to be explored. OV have recently emerged as a promising off-the-shelf treatment modality for various tumor types. OV are tumor-specific viruses that have desirable immunogenic properties with the capacity for transgene delivery to tumors

[0012] . In previous studies, an OV (OVCD19t) expressing a truncated non-signaling variant of CD19 (CD19t) has been shown to redirect of CD19-CAR T cells to solid tumors by exploiting the transgene delivery potential of OVCD19t to selectively infect and drive tumor-specific expression of the truncated nonsignaling variant of CD19

[0013] . The parent version of the chimeric poxvirus-based OV used herein has shown safety and antitumor activity in several preclinical models [14,15]. SUMMARY The present disclosure is based, at least in part, on the discovery that an oncolytic virus (OV) expressing a BCMA antigen can redirect BCMA-targeted therapies, such as proteins, BCMA-targeted bispecific T cell engagers (BCMA TCEs) and chimeric antigen receptor (CAR)-engineered T cell therapies targeting BCMA (e.g., BCMA CAR), to drive anti-tumor responses of endogenous T cells against multiple solid tumor types. BCMA, also known as CD269 and tumor necrosis factor (TNF) receptor superfamily member 17, is a receptor that plays a critical role in B lymphocytes (B cell) maturation and subsequent differentiation into plasma cells. Human BCMA (e.g., Genbank Accession No: BAB60895.1, UniProt ID No: Q02223-1, and UniProt ID No: Q02223-2) is a 184 amino acid receptor that has neither a secretory signal sequence nor any specific protease cleavage site in the N-terminal 54 amino acid extracellular domain. Amongst other things, the data in this application demonstrate robust cell surface BCMAt expression on multiple tumor types infected with an OV carrying the BCMAt- encoding gene (OVBCMAt) as described herein. This expression is shown to promote Attorney Docket No.40056-0104WO1 activation and tumor killing by T cells when treated with a BCMA-targeted therapy, such as a BCMA-TCE (e.g., Teclistamab). Described herein, inter alia, are methods of administering an oncolytic virus (OV) expressing a truncated variant of BCMA (BCMAt) and a therapeutic agent targeted to BCMAt, for example: a bispecific T cell engager, a chimeric antigen receptor, an antibody or an antibody-drug conjugate. The BCMAt includes at least the extracellular domain of BCMA and a transmembrane domain, e.g., the transmembrane domain of BCMA. A BCMAt lacks signaling activity because some or all of the cytoplasmic domain is deleted. Alternatively, the cytoplasmic domain can include one or more mutations that severely reduce or essentially eliminate signaling activity. Described herein are methods of killing solid tumor cancer cells comprising: administering to the subject an effective amount of an oncolytic virus expressing BCMAt (OVBCMAt); and administering to the subject an therapy, such as a bispecific T cell engager (TCE), that binds to the BCMAt encoded by the OVBCMAt. Also described herein are methods of treating a subject having a solid tumor comprising: administering to the subject an effective amount of an oncolytic virus expressing BCMAt (OVBCMAt); and administering to the subject a therapy, such as a protein, antibody, an immune cell, or a bispecific T cell engager (TCE), that binds to the BCMAt encoded by the OVBCMAt. In some embodiments, the therapy that binds BCMAt is any one or more of a population of immune cells expressing a BCMA-targeted scFv (e.g., BCMA CAR T cells), a BCMA- targeted TCE (e.g., Teclistamab), a BCMA antibody or antibody fragment, a BCMA antibody-drug conjugate, a protein that binds a BCMA antigen. Also described herein, inter alia, are methods of treating a subject having a solid tumor and / or methods of killing solid tumor cancer cells in a subject comprising: administering to the subject an effective amount of an oncolytic virus expressing a truncated BCMA (OVBCMAt), wherein the nucleotide sequence of OVBCMAt comprises: (a) a nucleotide sequence comprising at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NOs: X1, X17, X26, X27, X28, X32, X34, X36, X41, X52, X53, X55, X63, X65, X66, X76, X77, X79, X81, X82, X87, X90, X91, X92, X93, X104, X108, X110, X111, X116, X118, Attorney Docket No.40056-0104WO1 X120, X123, X128, X129, X130, X138, X140, X142, X143, X145, X146, X147, X149, X150, X151, X152, X153, X154, X155, X156, X157, X158, X160, X161, X165, X168, X169, X170, X172, X173, X174, X175, X176, X177, X178, X181, X182, X186, X192, X193, X194, X195, X197, X198, X199, X203, X206, X211, X212, X216, X219, X220, X222, X223, X224, X225, X226, X227, X228, X229, X231, X232, X233, X234, X236, X238, X240, X241, X243, X244, X252, X253, X254, X257, X258, X259, X260, X261, X263, X264, X265, X266, X267, X268, X269, X270, X271, X272, X274, and X275, or a variant of one or more thereof having 1, 2, 3, 4, or 5 single nucleotide substitutions, wherein the nucleotide substitutions do not alter the amino acid sequence of the encoded protein and / or do not alter the function of the encoded protein; or a nucleotide sequence encoding at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 proteins having the amino acid sequences of SEQ ID NOs: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275, or a variant of one or more thereof having 1, 2, 3, 4, or 5 single amino acid substitutions, wherein the amino acid substitutions are conservative and / or do not alter the function of the protein; and (b) a nucleotide sequence encoding a truncated human BCMA (e.g., SEQ ID NO: A3 or A4); and Attorney Docket No.40056-0104WO1 administering to the subject an effective amount of therapy that binds to BCMA (e.g., a BCMA TCE, a population of BCMA-targeted T cells, a population of BCMA- targeted NK cells, a BCMA-targeted antibody or antibody fragment). For example, an OVBCMAt can comprise a nucleotide sequence encoding 50 of SEQ ID NOs: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275 and of those 50, one or more and up to all fifty can comprises 1, 2, 3, 4, or 5 single amino acid substitution that are conservative and / or do not alter the function of the protein. Another example of an OVBCMAt is an OVBCMAt comprising a nucleotide sequence encoding 50 of SEQ ID NOs: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275. In another example, the OVBCMAt comprises a nucleotide sequence comprising all 121 of SEQ ID NOs: X1, X17, X26, X27, X28, X32, X34, X36, X41, X52, X53, X55, X63, X65, X66, X76, X77, X79, X81, X82, X87, X90, X91, X92, X93, X104, X108, X110, X111, X116, X118, X120, X123, X128, X129, X130, X138, X140, X142, X143, X145, X146, X147, X149, X150, X151, X152, X153, Attorney Docket No.40056-0104WO1 X154, X155, X156, X157, X158, X160, X161, X165, X168, X169, X170, X172, X173, X174, X175, X176, X177, X178, X181, X182, X186, X192, X193, X194, X195, X197, X198, X199, X203, X206, X211, X212, X216, X219, X220, X222, X223, X224, X225, X226, X227, X228, X229, X231, X232, X233, X234, X236, X238, X240, X241, X243, X244, X252, X253, X254, X257, X258, X259, X260, X261, X263, X264, X265, X266, X267, X268, X269, X270, X271, X272, X274, and X275, and of those 121, one or more (and up to all 121 sequences) have 1, 2, 3, 4, or 5 single nucleotide substitutions, wherein the nucleotide substitutions do not alter the amino acid sequence of the encoded protein and / or do not alter the function of the encoded protein Described herein, inter alia, are methods of treating a subject having a solid tumor comprising: administering to the subject an effective amount of an oncolytic virus expressing a truncated BCMA (OVBCMAt), the nucleotide sequence of OVBCMAt comprising: (a) an oncolytic virus nucleotide sequence; and (b) a nucleotide sequence encoding a truncated human BCMA; and administering to the subject an effective amount of a therapy, such as a bispecific T cell engager (TCE), that binds to BCMA. In various embodiments of any of the methods or compositions described herein: OVBCMAt does not encode functional thymidine kinase; the OVBCMAt comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to SEQ ID NO: A1 over the entire length of SEQ ID NO: A1; the OVBCMAt comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to SEQ ID NO: A1, but lacks the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO: A1 (i.e., lacks nucleotides 1 - 6,816 and 188,074 - 194,902 of SEQ ID NO: A1; i.e., nucleotides 6,817-188,073 of SEQ ID NO: A1); the oncolytic virus nucleotide sequence comprises a nucleotide sequence that is at 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% or 100% identical to: a) SEQ ID NO: A2 over the entire length of SEQ ID NO: A2 without the JR2 sequence of SEQ ID NO: A2 (i.e., as identified in FIGS.7A-7AU); or b) SEQ ID NO: A2 over the entire length of SEQ ID NO: A2 but not including the JR2 gene sequence, the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO: A2 (i.e., not including nucleotides 77682-78084, nucleotides 1- 4054, and nucleotides 185351-189404 of SEQ ID NO: A2); the oncolytic virus nucleotide Attorney Docket No.40056-0104WO1 sequence comprises at least 25, 50, 60, 70, 80, 90, 100, 110, 120, 130, 140 or 150 of the ORF in Table 4 and encodes at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NOs: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275; the oncolytic virus nucleotide sequence has no modifications in the regions encoding at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NOs: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275, or all of the open reading frame (ORF) in Table 4; the oncolytic virus nucleotide sequence comprises modifications within the regions encoding at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Attorney Docket No.40056-0104WO1 Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275, or any ORF identified in Table 4, that do not change the amino acid sequence of the encoded protein; the oncolytic virus nucleotide sequence comprises the regions encoding SEQ ID NOs: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275 and at least 130, 140, 150, 106, 170, 180, 190, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250, 255, 260, 265, 270, or 275 of the ORF in Table 4; the oncolytic virus nucleotide sequence comprises at least 25, 50, 60, 70, 80, 90, 100, 110, 120, 130, 140 or 150 of the ORF in Table 4 or all of the ORF in Table 4; the oncolytic virus nucleotide sequence comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, 99.99%, or 100% identical to: SEQ ID NO: A2 over the entire length of SEQ ID NO: A2, excluding all or a portion of the JR2 gene sequence (nt 77,603-78-137 of SEQ ID NO:A2) and excluding the ITR sequences, and comprises nucleotide sequences that encode at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NOs: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275, or a variant of one or more Attorney Docket No.40056-0104WO1 thereof having 1, 2, 3, 4, or 5 single amino acid substitutions. In some embodiments, the single amino acid substitutions are conservative and / or do not alter the function of the protein. In various embodiments of any of the methods or compositions described herein: the OVBCMAt comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, 99.99% or 100% identical to: SEQ ID NO: A1 over the entire length of SEQ ID NO: A1, and encodes at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 proteins having the amino acid sequences of SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275, or a variant of one or more thereof having 1, 2, 3, 4, or 5 single amino acid substitutions; the single amino acid substitutions are conservative and / or do not alter the function of the protein; the OVBCMAt comprises a nucleotide sequence: a) that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% or 100% identical to: SEQ ID NO: A1 over the entire length of SEQ ID NO: A1, but lacks the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO: A1; and b) encodes at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 proteins having the amino acid sequences of SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Attorney Docket No.40056-0104WO1 Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275, or a variant of one or more thereof having 1, 2, 3, 4, or 5 single amino acid substitutions; the amino acid substitutions are conservative and / or do not alter the function of the protein; the oncolytic virus sequence is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to nucleotides 6,817-188,073 of SEQ ID NO:A1 over the entire length of nucleotides 6,817- 188,073 SEQ ID NO: A1; the oncolytic virus sequence is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to nucleotides 7,000-188,000 of SEQ ID NO:A1 over the entire length of nucleotides 7,000- 188,000 SEQ ID NO: A1; the oncolytic virus sequence is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to nucleotides 8,000-187,000 of SEQ ID NO:A1 over the entire length of nucleotides 8,000- 187,000 SEQ ID NO: A1; the oncolytic virus sequence is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to nucleotides 10,000-185,000 of SEQ ID NO:A1 over the entire length of nucleotides 10,000-185,000 SEQ ID NO: A1; the oncolytic virus sequence is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to nucleotides 10,001-184,901 of SEQ ID NO: A1 over the entire length of the oncolytic virus sequence is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to nucleotides 10,001-184,901 of SEQ ID NO: A1; the OVBCMAt is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% or 100% identical to: SEQ ID NO: A2 over the entire length of SEQ ID NO: A2 except that the nucleotide sequence encoding BCMAt and a promoter sequence for expressing BCMAt replaces at least 10 contiguous nucleotides of the JR2 gene sequence; and at least about 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 125, 150, 175, 200, 225, 250, 275, 300, 325, 250, 275, 400, 425, 450, 475, or 500 nucleotides (nts) of the J2R gene sequence have been deleted. In various embodiments of any of the methods or compositions described herein: the nucleotide sequence encoding BCMAt is inserted into a noncoding region of SEQ ID NO: A1 or A2; the nucleotide sequence encoding BCMAt encodes the extracellular domain and the transmembrane domain of BCMA (e.g., SEQ ID NO: A3 or A4); the Attorney Docket No.40056-0104WO1 nucleotide sequence encoding BCMAt does not encode the entirety of the cytoplasmic domain of BCMA (e.g., a BCMA cytoplasmic domain: amino acids 78-184 of Genbank Accession No: BAB60895.1 and / or UniProt ID Nos: Q02223-1 or Q02223-2); the BCMAt comprises or consists of an amino acid sequence identical to SEQ ID NO: A3 (or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative amino acid substitutions)); the BCMAt comprises or consists of an amino acid sequence identical to SEQ ID NO: A3 or A4, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative amino acid substitutions); the nucleotide sequence encoding BCMAt is operably linked to a synthetic early promoter. In various embodiments of any of the methods described herein: the therapy binds the BCMAt encoded by the OVBCMAt; the therapy comprises a domain that binds BCMA (e.g., an scFv targeted to BCMA); the therapy comprises a protein comprising a domain that binds BCMA; the therapy comprises a TCE comprising a domain that binds BCMA and a domain that binds CD3; the domain that binds BCMA is a BCMA-targeted scFv; the domain that binds CD3 is a CD3-targeted scFv; the TCE is teclistamab or elranatamab; the therapy comprises a population of BCMA-targeted CAR immune cells; the BCMA CAR immune cells are BCMA CAR T cells; the BCMA CAR immune cells (e.g., BCMA CAR T cells) comprise a domain that binds BCMA; the domain that binds BCMA is a BCMA-targeted scFv; the therapy comprises an antibody or an antibody drug conjugate comprising a domain that binds BCMA. In various embodiments, the BCMA-targeted domain (e.g., the BCMA scFv) comprises any one of the following: a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B1-B3 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B5-B7; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B9-B11 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B13-B15; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B17-B19 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B21-B23; Attorney Docket No.40056-0104WO1 a variable light chain region comprising SEQ ID NO: B4 and a variable heavy region comprising SEQ ID NO: B8; a variable light chain region comprising SEQ ID NO: B12 and a variable heavy region comprising SEQ ID NO: B16; and a variable light chain region comprising SEQ ID NO: B20 and a variable heavy region comprising SEQ ID NO: B24. In various embodiments: the CD3 targeted scFv comprises any one of the following: a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C1-C3 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C5-C7; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C9-C11 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C13-C15; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C17-C19 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C21-C23; a variable light chain region comprising SEQ ID NO: C4 and a variable heavy region comprising SEQ ID NO: C8; a variable light chain region comprising SEQ ID NO: C12 and a variable heavy region comprising SEQ ID NO: C16; and a variable light chain region comprising SEQ ID NO: C20 and a variable heavy region comprising SEQ ID NO: C24. In some embodiments, the nucleotide sequence encoding BCMAt encodes an amino acid sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to: MLQMAGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKGTNAI LWTCLGLSLIISLAVFVLMFLLRKIS (SEQ ID NO: A3). In some embodiments, the methods comprise administering to the subject, any of the oncolytic viruses described herein; and, simultaneously or subsequently, administering to the subject an therapy, such as a protein, CAR, or TCE described herein (e.g., a BCMA TCE). In some embodiments, the therapy (e.g., TCE) is administered at least or about 1, Attorney Docket No.40056-0104WO1 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 26, 17, 18, 19, or 20 days after administration of the oncolytic virus. In some embodiments, the therapy (e.g., TCE) is administered at least or about 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 weeks after administration of the oncolytic virus. In some embodiments, the therapy (e.g., TCE) is administered at least or about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, or 13 months after administration of the oncolytic virus. In some embodiments, the solid tumor includes any one or more of: a sarcoma (e.g., tumors in a blood vessel, bone, fat tissue, ligament, lymph vessel, muscle or tendon), a carcinoma (e.g., tumors that form in epithelial cells), adrenocortical carcinoma, non-small cell lung carcinoma, gall bladder cancer, pancreatic cancer, prostate cancer, and urinary bladder cancer, gastric cancer, bone cancer, breast cancer, cervical cancer, colon cancer, rectal cancer, endometrial cancer, esophageal cancer, skin cancer, lung cancer, ovarian cancer, testicular cancer, thyroid cancer, etc., a metastases of one or more of these cancers, or a subpopulation of one or more of these or other cancers. In some embodiments, the solid tumor includes any cancer cell expressing BCMA, a BCMA antigen, or BCMAt. In some embodiments, the 5’ ITR comprises or consists of nucleotides (nt) 1 - 6,816 of SEQ ID NO:A1, and the 3’ ITR comprises or consists of nucleotides (nt) 188,074 - 194,902 of SEQ ID NO:A1. In some embodiments, the 5’ ITR comprises or consists of nucleotides (nt) 1- 4,054 of SEQ ID NO:A2, and the 3’ ITR comprises or consists of nucleotides (nt) 185,351-189,404 of SEQ ID NO:A2. The chimeric oncolytic poxviruses as described herein include a transgene (e.g., encoding human a truncated human BCMA (BCMAt)). In some embodiments, the BCMAt lacks a functional signaling domain, but includes the extracellular domain and transmembrane domain. In some embodiments, the truncated human BCMA (BCMAt) comprises the amino acid sequence (or a sequence at least 90%, 95%, 97%, 98% or 99% identical to): MLQMAGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKGTNAI LWTCLGLSLIISLAVFVLMFLLRKIS (SEQ ID NO: A3). In some embodiments, the truncated human BCMA (BCMAt) comprises the amino acid sequence (or a sequence at least 90%, 95%, 97%, 98% or 99% identical to: Attorney Docket No.40056-0104WO1 MLQMAGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKGTNAI LWTCLGLSLIISLAVFVLMFLL (SEQ ID NO: A4) In some embodiments, a useful BCMAt can be proceeded by a signaling domain and / or a promoter. For example, a useful signaling domain can comprise the amino acid sequence MLLLVTSLLLCELPHPAFLLIP (SEQ ID NO: A5), a variant thereof, or a different signaling domain known in the art. Thus, in some embodiments, an oncolytic virus described herein comprises a sequence comprising a nucleotide sequence encoding a truncated human BCMA operably linked to an expression control sequence (e.g., an early promoter). In some embodiments, the BCMAt comprises an amino acid sequence that comprises or consists of SEQ ID NOs: A3 or A4. In some embodiments, the BCMAt comprises or consists of an amino acid sequence that comprises or consists of SEQ ID NOs: A3 or A4, or a variant thereof with 1, 2, 3, 4, or 5 single amino acid modifications. In some embodiments, the amino acid modifications are amino acid substitutions (e.g., 1, 2, 3, 4, or 5 conservative amino acid substitutions). In some embodiments, the BCMAt is operably linked to a promoter, optionally wherein the promoter is a synthetic early promoter. Sequence identity for nucleotide and amino acid sequences are calculated using BLAST 2.0 with the default parameters. The percent sequence identity refers to a global alignment between the sequences. In some embodiments, the recombinant oncolytic viruses described herein comprises a transgene, e.g., a transgene in an expression cassette, wherein the transgene encodes all or a portion of a human BCMA (e.g., Genbank Accession No: BAB60895.1, UniProt ID Nos: Q02223-1 and Q02223-2, the extracellular portion of BCMA, a truncated BCMA, BCMAt (e.g., SEQ ID NOs: A3 or A4), or a variant of one or more thereof that can be recognized by an antibody that binds BCMA). In some embodiments, the expressed portion of BCMA encoded by a useful transgene is a portion that can be expressed on the cell surface and can be recognized by an anti-BCMA antibody. In some embodiments, the recombinant oncolytic viruses described herein comprise a transgene that encodes a single protein (e.g., BCMA or BCMAt). Attorney Docket No.40056-0104WO1 In some embodiments, the recombinant oncolytic viruses described herein do not include a transgene, e.g., a transgene in an expression cassette, wherein the transgene encodes all or a portion of a human CD19 (e.g., UniProt ID: P15391, the extracellular portion of CD19, or a truncated CD19, CD19t). In some embodiments, the recombinant oncolytic virus does not encode a CD19, a portion of CD19, or any portion of CD19 that comprises or consists of a CD19 portion that can be expressed on the cell surface and can be recognized by an anti-CD19 antibody. For example, in some embodiments, a recombinant oncolytic virus does not comprise a transgene encoding an amino acid sequence comprising or consisting of: EPLVVKVEEGDNAVLQCLKGTSDGPTQQLTWSRESPLKPFLKLSLGLPGL GIHMRPLAIWLFIFNVSQQMGGFYLCQPGPPSEKAWQPGWTVNVEGSGELFRW NVSDLGGLGCGLKNRSSEGPSSPSGKLMSPKLYVWAKDRPEIWEGEPPCVPPRD SLNQSLSQDLTMAPGSTLWLSCGVPPDSVSRGPLSWTHVHPKGPKSLLSLELKD DRPARDMWVMETGLLLPRATAQDAGKYYCHRGNLTMSFHLEITARPVLWHWL LRTGGWKVSAVTLAYLIFCLCSLVGILHLQRALVLRRKR (SEQ ID NO: A6) In some embodiments, the recombinant oncolytic viruses described herein do not comprise a sequence that encodes or expresses any one or more of an AFP, a CA125, a CD19 (e.g., a CD19t), a CD20, a CD33, a CD22, a CD123, a CD30, a CD38, a GPC-3, a CEA, a HER2, a GD2, a PSMA, CCL5, IL-12, anti-PD-1 antibody, a Claudin 18.2, a EpCAM, a GD2, a MSLN, an EGFR, an EGFRVIII, a Trop-2, a c-MET, a Nectin-4, a CD79b, a CCK4, a GPA33, a HLA-A2, a CLEC12A, a p-cadherin, a TDO2, a MART-I, a MUCI, a Pmel 17, a MAGE-I, a TRP-1, a TRP-2, a NY-ESQ, a PSA, a CDK4, a BCA225, a CA 125, a MG7-Ag, a NY-CO-I, a RCAS 1, a SDCCAG16, a TAAL6, a TAG72, and any combination thereof. Also described herein, inter alia, are oncolytic viruses expressing a truncated BCMA (OVBCMAt), the nucleotide sequence of OVBCMAt comprising: (a) an oncolytic virus nucleotide sequence; and (b) a nucleotide sequence encoding a truncated human BCMA (BCMAt); wherein the oncolytic virus nucleotide sequence encodes at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Attorney Docket No.40056-0104WO1 Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275, or a variant of one or more thereof having 1, 2, 3, 4, or 5 single aminoacid substitutions (optionally wherein the amino acid substitutions are conservative and / or do not alter the function of the protein); and / or wherein the OVBCMAt nucleotide sequence is at least 90% identical to: i) nucleotides 6,817-188,073 of SEQ ID NO:A1 over the entire length of nucleotides 6,817-188,073 SEQ ID NO: A1; ii) nucleotides 7,000-188,000 of SEQ ID NO:A1 over the entire length of nucleotides 7,000-188,000 SEQ ID NO: A1; iii) nucleotides 8,000-187,000 of SEQ ID NO:A1 over the entire length of nucleotides 8,000-187,000 SEQ ID NO: A1; or iv) nucleotides 10,000-185,000 of SEQ ID NO:A1 over the entire length of nucleotides 10,000-185,000 SEQ ID NO: A1. In some embodiments of any of the compositions or methods described herein, the OVBCMAt nucleotide sequence is at least 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to: i) SEQ ID NO: A1 over the entire length of SEQ ID NO: A1; ii) SEQ ID NO: A1 over the entire length of SEQ ID NO: A1, but lacks the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO: A1; iii) nucleotides 6,817-188,073 of SEQ ID NO:A1 over the entire length of nucleotides 6,817-188,073 SEQ ID NO: A1; iv) nucleotides 7,000-188,000 of SEQ ID NO:A1 over the entire length of nucleotides 7,000-188,000 SEQ ID NO: A1; v) nucleotides 8,000-187,000 of SEQ ID NO:A1 over the entire length of nucleotides 8,000-187,000 SEQ ID NO: A1; or Attorney Docket No.40056-0104WO1 vi) nucleotides 10,000-185,000 of SEQ ID NO:A1 over the entire length of nucleotides 10,000-185,000 SEQ ID NO: A1. In some embodiments of any of the compositions or methods described herein, an OVBCMAt comprises a nucleotide sequence comprising: (a) an oncolytic virus nucleotide sequence; and (b) a nucleotide sequence encoding a truncated human BCMA (BCMAt); wherein the oncolytic virus nucleotide sequence encodes at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275; and / or wherein the OVBCMAt nucleotide sequence comprises nucleotides 6,817- 188,073 of SEQ ID NO:A1 or a variant thereof with up to 100, 200, or 300 nucleotide substitutions. In some embodiments of any of the compositions or methods described herein, the OVBCMAt nucleotide sequence comprises nucleotides 6,817-188,073 of SEQ ID NO:A1 or a variant thereof with up to 100 nucleotide substitutions (e.g., 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, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100 nucleotide substitutions). In some embodiments of any of the compositions or methods described herein, any nucleotide modifications (e.g., nucleotide substitutions, nucleotide insertions) in the oncolytic virus nucleotide sequence do not change the amino acid sequence of encoded Attorney Docket No.40056-0104WO1 proteins having an amino acid sequences SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275. In some embodiments of any of the compositions or methods described herein, any nucleotide modifications (e.g., nucleotide substitutions, nucleotide insertions) in the oncolytic virus nucleotide sequence do not change the function of the encoded proteins having an amino acid sequences SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275. In some embodiments of any of the compositions or methods described herein, the OVBCMAt does not encode any of an AFP, a CA125, a CD19 (e.g., a CD19t), a CD20, a CD33, a CD22, a CD123, a CD30, a CD38, a GPC-3, a CEA, a HER2, a GD2, a PSMA, a Claudin 18.2, a EpCAM, a GD2, a MSLN, an EGFR, an EGFRVIII, a Trop-2, a c-MET, a Nectin-4, a CD79b, a CCK4, a GPA33, a HLA-A2, a CLEC12A, a p-cadherin, a TDO2, a MART-I, a MUCI, a Pmel 17, a MAGE-I, a TRP-1, a TRP-2, a NY-ESQ, a PSA, a CDK4, a BCA225, a CA 125, a MG7-Ag, a NY-CO-I, a RCAS 1, a SDCCAG16, a TAAL6, and a TAG72, and optionally functional variants of one or more thereof (e.g., a Attorney Docket No.40056-0104WO1 functional variant that would be recognized and bound by an antibody that binds the nonvariant version). In some embodiments of any of the compositions or methods described herein, the nucleotide sequence encoding BCMAt encodes the extracellular domain and the transmembrane domain of BCMA; the nucleotide sequence encoding BCMAt does not encode the entirety of the cytoplasmic domain of BCMA; the BCMAt comprises an amino acid sequence that comprises or consists of SEQ ID NO: A3 or A4; the nucleotide sequence encoding BCMAt is operably linked to a synthetic early promoter. In some embodiments of any of the compositions or methods described herein, the OVBCMAt comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to nucleotides 6,817-188,073 of SEQ ID NO: A1 over the entire length of nucleotides 6,817-188,073 of SEQ ID NO: A1. In some embodiments of any of the compositions or methods described herein, an OVBCMAt comprises nucleotides 6,817-188,073 of SEQ ID NO: A1 or a variant thereof with up to 100 nucleotide modifications (e.g., 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, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100 nucleotide substitutions). Also disclosed herein, inter alia, are CF33 viruses expressing a truncated human BCMA (OVBCMAt), wherein the transgene encoding the truncated BCMA (BCMAt) does not include the entirety of the cytoplasmic domain of BCMA and is inserted into the J2R gene, wherein the OVBCMAt does not encode a functional thymidine kinase. In some embodiments, the OVBCMAt does not encode a second tumor antigen. In some embodiments, the transgene comprises a promoter that drives expression the nucleotide sequence encoding a BCMAt. In some embodiments, the BCMAt lacks signaling domain activity. In some embodiments, the BCMAt comprises the extracellular domain and the transmembrane domain of BCMA. In some embodiments, the BCMAt comprises or consist of the amino acid sequence of SEQ ID NO: A3, or a variant thereof having 1, 2, 3, 4, or 5 single amino Attorney Docket No.40056-0104WO1 acid modifications (e.g., conservative amino acid substitutions). In some embodiments, the BCMAt comprises or consist of the amino acid sequence of SEQ ID NO: A4, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative amino acid substitutions). In some embodiments, a nonlimiting list of tumor antigens not encoded by an OVBCMAt described herein includes: an AFP, a CA125, a CD19 (e.g., a CD19t), a CD20, a CD33, a CD22, a CD123, a CD30, a CD38, a GPC-3, a CEA, a HER2, a GD2, a PSMA, a Claudin 18.2, a EpCAM, a GD2, a MSLN, an EGFR, an EGFRVIII, a GM- CSF, a Trop-2, a c-MET, a Nectin-4, a CD79b, a CCK4, a GPA33, a HLA-A2, a CLEC12A, a p-cadherin, a TDO2, a MART-I, a MUCI, a Pmel 17, a MAGE-I, a TRP-1, a TRP-2, a NY-ESQ, a PSA, a CDK4, a BCA225, a CA 125, a MG7-Ag, a NY-CO-I, a RCAS 1, a SDCCAG16, a TAAL6, and a TAG72, and / or truncations and / or functional variants thereof. Any of the OVBCMAt described herein can further comprise a second transgene comprising a reporter gene, wherein the second transgene does not encode tumor antigen. In some embodiments, the reporter gene is a human sodium iodide symporter (hNIS) gene. In some embodiments, the second transgene encodes a hNIS (e.g., UniProt ID: Q92911, or a variant or truncation thereof). In some embodiments the reporter would allow tracking of the virus in vivo, for example, using positron emission tomographic (PET) imaging. In some embodiments, the hNIS is inserted into the F14.5L gene of CF33. In some embodiments, the second transgene comprises a promoter that drives expression the nucleotide sequence encoding a hNIS. More information on reporter genes and insertion thereof into CF33 is known in the art, e.g., Chaurasiya, et al. (2022) Molecular Therapy: Methods & Clinical Development.24:102. In some embodiments, all or a portion of the J2R gene in CF33 is replaced by a transgene (e.g., a transgene encoding a BCMAt). In some embodiments, all or a portion of the F14.5L gene in CF33 is replaced by a transgene (e.g., a transgene encoding a reporter (e.g., a hNIS)). Also described herein are methods of treating a subject having a solid tumor comprising: administering to the subject an effective amount of any of the OVBCMAt Attorney Docket No.40056-0104WO1 herein; and administering to the subject an effective amount of any of BCMA-targeting therapy that binds to the BCMAt herein. Also described herein are methods of treating a solid tumor in a subject, the method comprising administering to the subject: an effective amount any OVBCMAt described herein, and a means for targeting BCMA; thereby treating the solid tumor. As used in this context, to “treat” means to ameliorate at least one symptom associated with a solid tumor or the reduce the size (or slow the growth) of the tumor. Examples of solid tumors are sarcomas, carcinomas, and lymphomas. In various embodiments, a solid tumor may be a carcinoma, adenocarcinoma, sarcoma, melanoma, mesothelioma, blastoma; a carcinoma or adenocarcinoma may for example be a bladder, a colon, a kidney, an ovary, a prostate, a lung, an uterus, a breast, or a prostate carcinoma or adenocarcinoma; a blastoma may for example be a neuroblastoma, a glioblastoma, or a retinoblastoma; the solid tumor is selected from the group consisting of prostate cancer (e.g., prostate adenocarcinoma), lung cancer (e.g., squamous cellular carcinoma), breast cancer (e.g., infiltrated ductal carcinoma), ovary cancer (e.g., serous papillary carcinoma), uterus cancer (e.g., squamous cellular carcinoma), CNS cancer and brain cancer (e.g., glioma (such as brainstem glioma and mixed gliomas), glioblastoma (also known as glioblastoma multiforme), astrocytoma, CNS lymphoma, germinoma, medulloblastoma, Schwannoma craniopharyngioma, ependymoma, pinealoma, hemangioblastoma, acoustic neuroma, oligodendroglioma, meningioma, neuroblastoma, retinoblastoma, and brain metastases), colon cancer (e.g., colon adenocarcinoma or colon carcinoma), colorectal cancer, rectal cancer (e.g., rectal adenocarcinoma), cancer of the striated muscle (e.g., rhabdomyosarcoma), thyroid cancer, testicular cancer, bladder cancer (e.g., bladder carcinoma), liver cancer, kidney cancer, fibrosarcoma, myxosarcoma, liposarcoma, chondrosarcoma, osteosarcoma, synovioma, mesothelioma, Ewing's tumor, leiomyosarcoma, rhabdomyosarcoma, lymphoid malignancy, pancreatic cancer, hepatocellular carcinoma, squamous cell carcinoma, basal cell carcinoma, adenocarcinoma, sweat gland carcinoma, medullary thyroid carcinoma, papillary thyroid carcinoma, pheochromocytomas sebaceous gland carcinoma, papillary carcinoma, papillary adenocarcinomas, medullary carcinoma, bronchogenic carcinoma, renal cell carcinoma, hepatoma, bile duct carcinoma, Attorney Docket No.40056-0104WO1 choriocarcinoma, Wilms' tumor, cervical cancer, seminoma, melanoma, and metastases of one or more thereof. In some embodiments of any of the methods disclosed herein, the BCMA-targeted therapy and / or therapy that binds to BCMAt can comprise any one or more of: Teclistamab, Elranatamab / PF-06863135, AMG -701, AMG-420, BI-836909, EM- 901 / CC-93269, JNJ-64007957 / JNJ-7957, REGN-5458, TNB-383B, BlenRep / GSK2857916, GSK2857916, CC99712, SEA-BCMA, MEDI2228, AMG 224, REGN5459, HDP-101, FPA-151, HPN-217, TNB-381M, bb2121, bb2127, bb21217, LCAR-B38M, MCARH171 / ET140, DESCARTES-08, KITE-585, P-BCMA-10, JCARH125, any protein comprising any BCMA-targeting domain described herein (including any antibody, antibody fragment, antibody drug conjugate, including bi- and tri-specific antibodies, CAR (e.g., a BCMA CAR expressed on a population of immune cells, such as T cells, NK cells, NKT cells, and subpopulations thereof), TCE, etc.). Any oncolytic virus described herein (e.g., an OVBCMAt) can be administered in single or repeated doses. An OVBCMAt can be administered alone or as a component of a pharmaceutical formulation (composition). The compounds may be formulated for administration, in any convenient way for use in human or veterinary medicine. Wetting agents, emulsifiers and lubricants, such as sodium lauryl sulfate and magnesium stearate, as well as coloring agents, release agents, preservatives and antioxidants can also be present in the compositions. Pharmaceutical formulations can be prepared according to any method known to the art for the manufacture of pharmaceuticals. Formulations of the compositions of the invention include those suitable for intradermal, subcutaneous, intravenous, transdermal, intraperitoneal, intramuscular, pulmonary, and / or parenteral administration. The formulations may conveniently be presented in unit dosage form and may be prepared by any methods well known in the art of pharmacy. The amount of active ingredient (e.g., an OVBCMAt) which can be combined with a carrier to produce a single dosage form will vary depending upon the host being treated, the particular mode of administration, e.g., subcutaneous or intravenous. The amount of active ingredient which can be combined with a carrier to produce a single dosage form will generally be that amount of the compound which produces a therapeutic effect, e.g., expression of a BCMA or Attorney Docket No.40056-0104WO1 BCMAt molecule on the surface of an infected cell, e.g., an infected solid tumor cell. Useful carriers are well known in the art and can include phosphate buffered saline solutions, water, liposomes, various types of wetting agents, sterile solutions, etc. Preparations for parenteral administration include sterile aqueous or non-aqueous solutions, or suspensions. Examples of non-aqueous solvents are propylene glycol, polyethylene glycol, and injectable organic esters such as ethyl oleate. Aqueous carriers include water, aqueous solutions, or suspensions, including saline and buffered media. Parenteral vehicles include sodium chloride solution, Ringer's dextrose, dextrose and sodium chloride, or lactated Ringer's. Intravenous vehicles include fluid and nutrient replenishes, electrolyte replenishers (such as those based on Ringer's dextrose), and the like. Preservatives and other additives may also be present such as, for example, antimicrobials, anti-oxidants, chelating agents, and inert gases and the like. In addition, the composition might comprise proteinaceous carriers, like, e.g., serum albumin or immunoglobulin, preferably of human origin. BCMA-targeted Therapies In some embodiments, the methods described herein comprise therapeutic agent that binds to BCMAt expressed by the OVBCMAt. Useful BCMA-targeting therapies can comprise a domain or scFv that binds BCMAt. In some embodiments, a useful therapy can be any one or more of a protein, a TCE, a population of immune cells expressing a BCMA CAR (e.g., BCMA CAR T cells or BCMA CAR NK cells), an anti- BCMA antibody, an anti-BCMA antibody fragment, an anti-BCMA antibody-drug conjugate, an anti-BCMA antibody or antibody fragment linked to a chemotherapeutic agent, a functional variant of each, and combinations thereof. Proteins targeted to a BCMA useful in the methods described herein include, for example, BCMA CAR, BCMA TCEs, BCMA antibodies, and the like. In some embodiments, a protein targeted to BCMA comprises a domain that binds a BCMA, such as the BCMAt encoded by the OVBCMAt viruses described herein. Attorney Docket No.40056-0104WO1 1. Bispecific T cell Engagers (TCEs) and Antibodies In some embodiments, the methods described herein comprise the use of a BCMA-targeted therapy, such as a TCE (e.g., a therapeutic agent that binds to CD3 and to BCMA or BCMAt; e.g., teclistamab and elranatamab) or an antibody or antibody fragment (e.g., BlenRep / GSK2857916). There are a number of BCMA-targeted therapies (e.g., proteins, CAR, TCEs, and antibodies) known in the art that can be used in any of the methods described herein. For example, useful BCMA TCEs include teclistamab (also called Teclistamab-cqyv and Tecvayli; US 20220041742 A1; WO 2017 / 031104) and elranatamab (also called elranatamab-bcmm, Elrexfio, PF06863135; US Pat. No.9,969,809; US 2023 / 0340137 A1; WO 2022 / 053990). Teclistamab-cqyv is a humanized immunoglobulin G4 (IgG4) bispecific BCMA-directed cluster of differentiation (CD3) T-cell engager. Teclistamab- cqvv utilizes an IgG4 PAA scaffold containing Pro mutations (S229P in the anti-BCMA mAb and S233P in the anti-CD3 mAb, according to sequential numbering of amino acids) that stabilize the hinge region and Ala / Ala mutations (F235A, L236A in the anti- BCMA mAb and F239A, L240A in anti-CD3 mAb, according to sequential numbering of amino acids) that suppress FcγR binding. The resulting teclistamab-cqyv bispecific antibody comprises Fc substitutions, with the BMCA-binding arm and CD3-binding arm each comprising Pro / Ala / Ala substitutions at amino acid positions 228 / 234 / 235, respectively (according to EU index numbering); and the CD3-binding arm also comprising F405L and R409K substitutions (according to EU index numbering). Teclistamab yielded comparable overall response rate (ORR) to other published experimental BCMA-directed immunotherapies, including AMG-420, a BiTE, and idecabtagene vicleucel (also called Abecma and bb2121), a CAR-T therapy (Raje N, Berdeja J, Lin Y, et al. (2019) Anti-BCMA CAR T-Cell Therapy bb2121 in Relapsed or Refractory Multiple Myeloma. N Engl J Med 2019; 380:1726-37; Topp M S, Duell J, Zugmaier G, et al. Anti-B-Cell Maturation Antigen BiTE Molecule AMG 420 Induces Responses in Multiple Myeloma. J Clin Oncol 2020; 38:775-83). The safety profile of teclistamab at the RP2D was favorable compared with idecabtagene vicleucel, with no grade ≥3 CRS (versus 5%) and a low rate of neurotoxicity (2.5% versus 18%). There Attorney Docket No.40056-0104WO1 were no cases of peripheral polyneuropathy, a serious adverse events (AE) observed with AMG-420, following teclistamab treatment. Useful therapies described herein (e.g., a TCE, BCMA CAR immune cells, BCMA antibody drug conjugates) can be administered in single or repeated doses. Useful therapies described herein can be administered via intradermal, subcutaneous, intravenous, transdermal, intraperitoneal, intramuscular, pulmonary, and / or parenteral administration. Additional information on administering a TCE, e.g., teclistamab, is known in the art and can be found, for example, in US 2022 / 0041742 A1, WO 2024 / 044545, and WO 2024 / 044548. Therapies described herein (e.g., a TCE) can be administered alone or as a component of a pharmaceutical formulation (composition). The compounds may be formulated for administration, in any convenient way for use in human or veterinary medicine. Wetting agents, emulsifiers and lubricants, such as sodium lauryl sulfate and magnesium stearate, as well as coloring agents, release agents, preservatives and antioxidants can also be present in the compositions. Pharmaceutical formulations can be prepared according to any method known to the art for the manufacture of pharmaceuticals. Formulations of the compositions of the invention include those suitable for intradermal, subcutaneous, intravenous, transdermal, intraperitoneal, intramuscular, pulmonary, and / or parenteral administration. The formulations may conveniently be presented in unit dosage form and may be prepared by any methods well known in the art of pharmacy. The amount of active ingredient (e.g., a BCMA TCE) which can be combined with a carrier to produce a single dosage form will vary depending upon the host being treated, the particular mode of administration, e.g., subcutaneous or intravenous. More detail on formulating and administering teclistamab is known in the art and can be found, for example, in US 2022 / 0041742 A1, WO 2024 / 044545, and WO 2024 / 044548. The amount of active ingredient which can be combined with a carrier to produce a single dosage form will generally be that amount of the compound which produces a therapeutic effect, e.g., an antigen specific T cell response. Useful carriers are well known in the art and can include phosphate buffered saline solutions, water, liposomes, various types of wetting agents, sterile solutions, etc. Preparations for parenteral administration include sterile aqueous or non-aqueous Attorney Docket No.40056-0104WO1 solutions, or suspensions. Examples of non-aqueous solvents are propylene glycol, polyethylene glycol, and injectable organic esters such as ethyl oleate. Aqueous carriers include water, aqueous solutions, or suspensions, including saline and buffered media. Parenteral vehicles include sodium chloride solution, Ringer's dextrose, dextrose and sodium chloride, or lactated Ringer's. Intravenous vehicles include fluid and nutrient replenishes, electrolyte replenishers (such as those based on Ringer's dextrose), and the like. Preservatives and other additives may also be present such as, for example, antimicrobials, anti-oxidants, chelating agents, and inert gases and the like. In addition, the composition might comprise proteinaceous carriers, like, e.g., serum albumin or immunoglobulin, preferably of human origin. More information on formulations, dosage, and administration of therapies such as TCEs is known in the art, for example, in US 20210403587 A1, US 2022 / 0041742 A1, US 2023 / 0235053 A1, US 2023 / 0340137 A1, WO 2016 / 166629, WO 2018 / 204907, WO 2022 / 053990, WO 2023 / 199235, WO 2023 / 062188, WO 2024 / 044545, and WO 2024 / 044548. Examples of additional BCMA TCE and antibody constructs can include any one or more of the therapeutic agents listed in Table A1. Table A1: Bispecific BCMA-targeting Therapies Attorney Docket No.40056-0104WO1 Adapted from Table 4 of Nie, S., et al. (2020) “Biology drives the discovery of bispecific antibodies as innovative therapeutics” Antibody Therapeutics, 3(1):18-62. Additional therapies are also known in the art (e.g., GSK2857916, CC99712, SEA-BCMA, MEDI2228, AMG 224, REGN5459, and HDP-101). A TCE as described herein includes bispecific antibody constructs, which are recombinant protein constructs made from two flexibly linked antibody-derived binding domains. One binding domain of a BCMA-TCE is specific for BCMA, BCMAt, or a variant thereof; the second binding domain is specific for CD3 or a variant thereof (e.g., a functional variant). The TCEs and antibody constructs disclosed herein can be prepared by methods known in the art, for example, by methods disclosed in WO 2008 / 119657 and WO 2017 / 134140. TCE constructs are uniquely suited to transiently connect T cells with target cells and, at the same time, potently activate the inherent cytolytic potential of T cells against target cells. An increased half-life is generally useful in in vivo applications of TCEs and immunoglobulins in general, especially antibodies and antibody fragments of small size. Some approaches described in the art to achieve such effect comprise the fusion of the TCE or bispecific antibody construct to larger proteins, which preferably do not interfere with the therapeutic effect of the TCE or bispecific antibody construct. Examples for such further developments of bispecific T cell engagers comprise bispecific Fc-molecules e.g., described in US 2014 / 0302037, US 2014 / 0308285, WO 2014 / 144722, WO 2014 / 151910, WO 2015 / 048272, WO 2017 / 031104, WO 2018 / 052503, WO 2018 / 204907, WO 2020 / 072306, WO 2021 / 222578, US 2021 / 0403587 A1, and US 2023 / 0272102 A1. Antibody constructs as described in WO 2008 / 119567 are likely to Attorney Docket No.40056-0104WO1 suffer from rapid clearance from the body; thus, whilst they are able to reach most parts of the body rapidly, and are quick to produce and easier to handle, their in vivo applications may be limited by their brief persistence in vivo. Prolonged administration by continuous intravenous infusion is used to achieve therapeutic effects because of the short in vivo half-life of this small, single chain molecule. In some embodiments, a useful TCE can be a bispecific antibody construct that further comprises a half-life extending (HLE) moiety (e.g., a scFc domain, a heteroFc domain, or an albumin binding domain). In some embodiments, the N-terminus or the C- terminus of the HLE domain is connected to the TCE (e.g., the portion that binds CD3, e.g., the VH or VL of a CD3-targeted scFv). In some embodiments, the HLE domain is connected to the bispecific antibody construct via a linker. In some embodiments, the TCE is a BiTE; in some embodiments, the BiTE further comprises a third domain comprising two polypeptide monomers, each comprises a hinge, a CH2 and a CH3 domain, wherein the two polypeptide monomers are linked to each other via a peptide linker. In some embodiments, the third domain comprises in an amino to carboxyl order hinge-CH2-CH3- linker-hinge-CH2-CH3. In some embodiments, the third domain is a half-life extended (HLE) domain. Useful proteins, CAR, TCEs and antibodies (including antibody fragments and antibody-drug conjugates) comprise a domain that targets BCMA (e.g., an scFv or domain comprising sequences in Table A2). In some embodiments, the domain that targets BCMA is a BCMA-targeted scFv. For example, a useful TCE comprises a domain that binds BCMA and a domain that binds CD3. In some embodiments, the domain that binds BCMA is a BCMA-targeted scFv and the domain that binds CD3 is a CD3-targeted scFv. For example, a useful TCE (e.g., Teclistamab) comprises a first heavy chain (HC) (SEQ ID NO: B26) and a first light chain (LC) (SEQ ID NO: B25), and a second heavy chain (HC) (SEQ ID NO: C51) and a second light chain (LC) (SEQ ID NO: C50). Another useful TCE (e.g., Elranatamab) comprises a first heavy chain (HC) (SEQ ID NO: B30) and a first light chain (LC) (SEQ ID NO: B29), and a second heavy chain (HC) (SEQ ID NO: C61) and a second light chain (LC) (SEQ ID NO: C60). Attorney Docket No.40056-0104WO1 a. BCMA-targeting Domains In some embodiments, a BCMA-targeted protein comprises: (a) a heavy chain variable region (VH) comprising a VH complementarity determining region (CDR)1 comprising or consisting of a sequence that is identical to a VH CDR1 amino acid sequence set forth in Table A2; a VH CDR2 comprising or consisting of a sequence that is identical to a VH CDR2 amino acid sequence set forth in Table A2; and a VH CDR3 comprising or consisting of a sequence that is identical to a VH CDR3 amino acid sequence set forth in Table A2; and (b) a light chain variable region (VL) comprising a VL CDR1 comprising or consisting of a sequence that is identical to a VL CDR1 amino acid sequence set forth in Table A2; a VL CDR2 comprising or consisting of a sequence that is identical to a VL CDR2 amino acid sequence set forth in Table A2; and a VL CDR3 comprising or consisting of a sequence that is identical to a VL CDR3 amino acid sequence set forth in Table A2. In some embodiments, a BCMA-targeted protein comprises a VH comprising or consisting of an amino acid sequence that is identical to a VH amino acid sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2); and a VL comprising or consisting of an amino acid sequence that is identical to a VL amino acid sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2). A useful BCMA-targeted protein comprises any one of the following: a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B1-B3 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B5-B7; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B9-B11 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B13-B15; Attorney Docket No.40056-0104WO1 a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B17-B19 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B21-B23; a variable light chain region comprising SEQ ID NO: B4 and a variable heavy region comprising SEQ ID NO: B8; a variable light chain region comprising SEQ ID NO: B12 and a variable heavy region comprising SEQ ID NO: B16; and a variable light chain region comprising SEQ ID NO: B20 and a variable heavy region comprising SEQ ID NO: B24. In some embodiments, a BCMA-targeted scFv comprises: (a) a heavy chain variable region (VH) comprising a VH complementarity determining region (CDR)1 comprising or consisting of a sequence that is identical to a VH CDR1 amino acid sequence set forth in Table A2; a VH CDR2 comprising or consisting of a sequence that is identical to a VH CDR2 amino acid sequence set forth in Table A2; and a VH CDR3 comprising or consisting of a sequence that is identical to a VH CDR3 amino acid sequence set forth in Table A2; and (b) a light chain variable region (VL) comprising a VL CDR1 comprising or consisting of a sequence that is identical to a VL CDR1 amino acid sequence set forth in Table A2; a VL CDR2 comprising or consisting of a sequence that is identical to a VL CDR2 amino acid sequence set forth in Table A2; and a VL CDR3 comprising or consisting of a sequence that is identical to a VL CDR3 amino acid sequence set forth in Table A2. In some embodiments, a BCMA-targeted scFv comprises a VH comprising or consisting of an amino acid sequence that is identical to a VH amino acid sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2); and a VL comprising or consisting of an amino acid sequence that is identical to a VL amino acid sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2). A useful BCMA-targeted scFv comprises any one of the following: Attorney Docket No.40056-0104WO1 a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B1-B3 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B5-B7; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B9-B11 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B13-B15; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B17-B19 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B21-B23; a variable light chain region comprising SEQ ID NO: B4 and a variable heavy region comprising SEQ ID NO: B8; a variable light chain region comprising SEQ ID NO: B12 and a variable heavy region comprising SEQ ID NO: B16; and a variable light chain region comprising SEQ ID NO: B20 and a variable heavy region comprising SEQ ID NO: B24. Useful BCMA-targeted antibodies (including monoclonal antibodies, antibody fragments, antibody-drug conjugates, and the like) can comprise the following: (a) a heavy chain variable region (VH) comprising a VH complementarity determining region (CDR)1 comprising or consisting of a sequence that is identical to a VH CDR1 amino acid sequence set forth in Table A2; a VH CDR2 comprising or consisting of a sequence that is identical to a VH CDR2 amino acid sequence set forth in Table A2; and a VH CDR3 comprising or consisting of a sequence that is identical to a VH CDR3 amino acid sequence set forth in Table A2; and (b) a light chain variable region (VL) comprising a VL CDR1 comprising or consisting of a sequence that is identical to a VL CDR1 amino acid sequence set forth in Table A2; a VL CDR2 comprising or consisting of a sequence that is identical to a VL CDR2 amino acid sequence set forth in Table A2; and a VL CDR3 comprising or consisting of a sequence that is identical to a VL CDR3 amino acid sequence set forth in Table A2. In some embodiments, a BCMA-targeted antibody (and the like) comprises a VH comprising or consisting of an amino acid sequence that is identical to a VH amino acid Attorney Docket No.40056-0104WO1 sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2); and a VL comprising or consisting of an amino acid sequence that is identical to a VL amino acid sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2). A useful BCMA-targeted antibody (and the like) comprises any one of the following: a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B1-B3 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B5-B7; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B9-B11 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B13-B15; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B17-B19 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B21-B23; a variable light chain region comprising SEQ ID NO: B4 and a variable heavy region comprising SEQ ID NO: B8; a variable light chain region comprising SEQ ID NO: B12 and a variable heavy region comprising SEQ ID NO: B16; and a variable light chain region comprising SEQ ID NO: B20 and a variable heavy region comprising SEQ ID NO: B24. TABLE A2: BCMA-Binding Sequences Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Additional BCMA binding sequences are known in the art, e.g., in WO 2013 / 072415, US 2015 / 0376287 A1, WO 2017 / 031104, WO 2017 / 134134, WO 2018 / 119215, WO 2019 / 075378, WO 2019 / 164891, WO 2020 / 018820, US 2022 / 0041742 A1, WO2022 / 006316, US 2023 / 0272102 A1, US 2023 / 0257473 A1, US 20230398147 A1, and as described throughout the present application. b. CD3-targeting Domains In some embodiments, a CD3-targeted domain and / or scFv comprises (a) a heavy chain variable region (VH) comprising a VH complementarity determining region (CDR)1 comprising or consisting of a sequence that is identical to a VH CDR1 amino acid sequence set forth in Table A3; a VH CDR2 comprising or consisting of a sequence that is identical to a VH CDR2 amino acid sequence set forth in Table A3; and a VH CDR3 comprising or consisting of a sequence that is identical to a VH CDR3 amino acid sequence set forth in Table A3; and (b) a light chain variable region (VL) comprising a VL CDR1 comprising or consisting of a sequence that is identical to a VL CDR1 amino acid sequence set forth in Table A3; a VL CDR2 comprising or consisting of a sequence that is identical to a VL CDR2 amino acid sequence set forth in Table A3; and a VL CDR3 comprising or consisting of a sequence that is identical to a VL CDR3 amino acid sequence set forth in Table A3. In some embodiments, a CD3-targeted domain and / or scFv comprises a VH comprising or consisting of a sequence that is identical to a VH amino acid sequence set forth in Table A3, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid Attorney Docket No.40056-0104WO1 modifications (e.g., substitutions), wherein the amino acid modifications are not in a CDR (also as set forth in Table A3); and a VL comprising or consisting of a sequence that is identical to a VL amino acid sequence set forth in Table A3, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in a CDR (also as set forth in Table A3). In some embodiments, the CD3-targeted domain and / or scFv comprises any one of the following: a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C1-C3 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C5-C7; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C9-C11 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C13-C15; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C17-C19 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C21-C23; a variable light chain region comprising SEQ ID NO: C4 and a variable heavy region comprising SEQ ID NO: C8; a variable light chain region comprising SEQ ID NO: C12 and a variable heavy region comprising SEQ ID NO: C16; and a variable light chain region comprising SEQ ID NO: C20 and a variable heavy region comprising SEQ ID NO: C24. TABLE A3: CD3-Binding Sequences Attorney Docket No.40056-0104WO1

[0002] Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Additional CD3 binding sequences are known in the art, e.g., in WO 2013 / 072415, US 2015 / 0376287 A1, WO 2017 / 031104, WO 2017 / 134134, WO 2018 / 052503, WO 2018 / 119215, WO 2019 / 075378, WO 2019 / 164891, WO 2020 / 018820, US 2021 / 0403587 A1, US 2022 / 0041742 A1, US 20220041742 A1, WO 2022 / 006316, WO 2023 / 056391, US 2023 / 0272102 A1, US 2023 / 0257473 A1, US 20230398147 A1, US 2024 / 0018235 A1, and as described throughout. 2. BCMA Cell-Based Therapies In some embodiments, a useful therapy in any of the methods described herein is a population of autologous or allogeneic BCMA-targeted human immune cells (e.g., macrophages, NK cells, NKT cells, T cells, subpopulations of one or more thereof, and combinations thereof). In some embodiments, any of the methods described herein comprise administering to the subject an effective amount of a population of immune cells (e.g., human T cells or human NK cells) expressing a CAR or harboring a nucleic acid encoding a CAR, wherein the CAR binds to BCMA. In some embodiments, the methods described herein comprise the use of a population of immune cells expressing a BCMA-targeted receptor, such as a CAR comprising a BCMA-targeted domain. In some embodiments, the methods described herein comprise administering a population of autologous or allogeneic human immune cells (e.g., macrophages, NK cells, NKT cells, T cells, subpopulations of one or more thereof, and combinations thereof) targeted to BCMA. In some embodiments, useful autologous or allogenic T cells comprise central memory T cells (TCM cells) or a combination of central memory T cells, naive T cells, and stem central memory cells (i.e., the T cells are TCM / SCM / Ncells). In some embodiments, the population of T cells includes both CD4+ cells and CD8+ cells. Attorney Docket No.40056-0104WO1 In some embodiments, the immune cells express a CAR or are transduced by a nucleic acid encoding a CAR (e.g., a BCMA CAR). In general, a BCMA CAR includes a BCMA-targeted domain (e.g., a BCMA scFv), a spacer domain, a transmembrane domain, one or more co-stimulatory domains, and a CD3zeta cytoplasmic domain. For example, in some embodiments, a useful CAR can comprise the following domains: BCMAscFv-IgG4(HL-CH3)-CD4tm-41BB-Zeta. In some embodiments, a BCMA CAR can comprise or consist of the amino acid sequence: MLLLVTSLLLCELPHPAFLLIPDIVLTQSPASLAMSLGKRATISCRASESVSV IGAHLIHWYQQKPGQPPKLLIYLASNLETGVPARFSGSGSGTDFTLTIDPVEEDDV AIYSCLQSRIFPRTFGGGTKLEIKGSTSGSGKPGSGEGSTKGQIQLVQSGPELKKPG ETVKISCKASGYTFTDYSINWVKRAPGKGLKWMGWINTETREPAYAYDFRGRFA FSLETSASTAYLQINNLKYEDTATYFCALDYSYAMDYWGQGTSVTVSSESKYGPP CPPCPGGGSSGGGSGGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVE WESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHN HYTQKSLSLSLGKMALIVLGGVAGLLLFIGLGIFFKRGRKKLLYIFKQPFMRPVQT TQEEDGCSCRFPEEEEGGCELGGGRVKFSRSADAPAYQQGQNQLYNELNLGRRE EYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEIGMKGERRRG KGHDGLYQGLSTATKDTYDALHMQALPPR (SEQ ID NO:D1), or a variant thereof have 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in the BCMA targeting domain (e.g., the BCMA scFv or the CDRs of the BCMA scFv). The amino acids in SEQ ID NO: D1 are underlined above to indicate the domain as in Signal sequence-BCMAscFv-IgG4 CH3)-CD4tm-41BB-L-Zeta. For example, in some embodiments, a useful CAR can comprise the following domains: BCMAscFv-IgG4(HL-CH3)-CD28tm-CD28gg-Zeta. In some embodiments, a BCMA CAR can comprise or consist of the amino acid sequence: MLLLVTSLLLCELPHPAFLLIPDIVLTQSPASLAMSLGKRATISCRASESVSV IGAHLIHWYQQKPGQPPKLLIYLASNLETGVPARFSGSGSGTDFTLTIDPVEEDDV AIYSCLQSRIFPRTFGGGTKLEIKGSTSGSGKPGSGEGSTKGQIQLVQSGPELKKPG ETVKISCKASGYTFTDYSINWVKRAPGKGLKWMGWINTETREPAYAYDFRGRFA Attorney Docket No.40056-0104WO1 FSLETSASTAYLQINNLKYEDTATYFCALDYSYAMDYWGQGTSVTVSSESKYGPP CPPCPGGGSSGGGSGGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVE WESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHN HYTQKSLSLSLGKMFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRGGHSDYM NMTPRRPGPTRKHYQPYAPPRDFAAYRSGGGRVKFSRSADAPAYQQGQNQLYNE LNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEIGM KGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR (SEQ ID NO:D2), or a variant thereof have 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in the BCMA targeting domain (e.g., the BCMA scFv or the CDRs of the BCMA scFv). The amino acids in SEQ ID NO:D2 above are underlined to indicate the domain as in Signal sequence- BCMAscFv-IgG4(HL-CH3)-CD28tm-CD28gg-L-Zeta. A CAR can comprise any BCMA targeting domain described herein (e.g., a BCMA targeted scFv or functional variant thereof) or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions); a transmembrane domain selected from: a CD4 transmembrane domain or variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions), a CD8 transmembrane domain or variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions), a CD28 transmembrane domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions), and a CD3ξ transmembrane domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions); a costimulatory domain (e.g., a CD28 co-stimulatory domain or a variant thereof having 1- 5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions); or a 4-l BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions); or both a CD28 co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions) and a 4-l BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions); and a CD3ξ signaling domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications. In some embodiments, a BCMA CAR comprises any BCMA-targeting domain described herein; a spacer comprising or consisting of an amino acid sequence of any one Attorney Docket No.40056-0104WO1 of SEQ ID NOs: 24-34 or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., conservative substitutions); a transmembrane domain comprising or consisting of an amino acid sequence of any one of SEQ ID NOs: 15-23 or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., conservative substitutions); a co-stimulatory domain comprising or consisting of an amino acid sequence of any one of SEQ ID NOs: 36-40 or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., conservative substitutions); and a CD3zeta domain comprising or consisting of the amino acid sequence of any one of SEQ ID NOs: 35 and 50-56 or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., conservative substitutions). (a) BCMA targeting domain In some embodiments, useful CAR comprise a BCMA scFv. In some embodiments, a BCMA scFv can comprise or consist of the amino acid sequence: MLLLVTSLLLCELPHPAFLLIPDIVLTQSPASLAMSLGKRATISCRASESVS VIGAHLIHWYQQKPGQPPKLLIYLASNLETGVPARFSGSGSGTDFTLTIDPVE EDDVAIYSCLQSRIFPRTFGGGTKLEIKGSTSGSGKPGSGEGSTKGQIQLVQSGP ELKKPGETVKISCKASGYTFTDYSINWVKRAPGKGLKWMGWINTETREPAYAYDFRGR FAFSLETSASTAYLQINNLKYEDTATYFCALDYSYAMDYWGQGTSVTVSS (SEQ ID NO:D3), or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in a CDR (underlined). In some embodiments, a BCMA scFv can comprise or consist of the amino acid sequence amino acids 23-268 of SEQ ID NO:D3, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in a CDR (underlined). In some embodiments, a BCMA scFv can comprise or consist of the amino acid sequence: DIVLTQSPASLAMSLGKRATISCRASESVSVIGAHLIHWYQQKPGQPPKLLIYLAS NLETGVPARFSGSGSGTDFTLTIDPVEEDDVAIYSCLQSRIFPRTFGGGTKLEIKGST SGSGKPGSGEGSTKGQIQLVQSGPELKKPGETVKISCKASGYTFTDYSINWVKRA PGKGLKWMGWINTETREPAYAYDFRGRFAFSLETSASTAYLQINNLKYEDTATYF Attorney Docket No.40056-0104WO1 CALDYSYAMDYWGQGTSVTVSS (SEQ ID NO:D4), or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in a CDR (underlined). In some embodiments, a BCMA scFv can comprise: a light chain variable domain that is at least 90%, 95%, 98%, 99% or 100% identical to: DIVLTQSPASLAMSLGKRATISCRASESVSVIGAHLIHWYQQKPGQPPKLLI YLASNLETGVPARFSGSGSGTDFTLTIDPVEEDDVAIYSCLQSRIFPRTFGGGTKLEI KGST (SEQ ID NO: D5), and comprises light chain CDRs 1-3 (underlined); and a heavy chain variable domain that is at least 90%, 95%, 98%, 99% or 100% identical to: QIQLVQSGPELKKPGETVKISCKASGYTFTDYSINWVKRAPGKGLKWMG WINTETREPAYAYDFRGRFAFSLETSASTAYLQINNLKYEDTATYFCALDYSYAMD YWGQGTSVTVSS (SEQ ID NO: D6) and comprises heavy chain CDRs 1-3 (underlined). In some embodiments, a BCMA scFv can comprise: a light chain variable domain comprising SEQ ID NO:D5, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in a CDR (underlined); and a light chain variable domain comprising SEQ ID NO:D6, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in a CDR (underlined). In some embodiments, a BCMA-targeted scFv comprises: (a) a heavy chain variable region (VH) comprising a VH complementarity determining region (CDR)1 comprising or consisting of a sequence that is identical to a VH CDR1 amino acid sequence set forth in Table A2; a VH CDR2 comprising or consisting of a sequence that is identical to a VH CDR2 amino acid sequence set forth in Table A2; and a VH CDR3 comprising or consisting of a sequence that is identical to a VH CDR3 amino acid sequence set forth in Table A2; and (b) a light chain variable region (VL) comprising a VL CDR1 comprising or consisting of a sequence that is identical to a VL CDR1 amino acid sequence set forth in Attorney Docket No.40056-0104WO1 Table A2; a VL CDR2 comprising or consisting of a sequence that is identical to a VL CDR2 amino acid sequence set forth in Table A2; and a VL CDR3 comprising or consisting of a sequence that is identical to a VL CDR3 amino acid sequence set forth in Table A2. In some embodiments, a BCMA-targeted scFv comprises a VH comprising or consisting of an amino acid sequence that is identical to a VH amino acid sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2); and a VL comprising or consisting of an amino acid sequence that is identical to a VL amino acid sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2). A useful BCMA-targeted scFv comprises any one of the following: a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B1-B3 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B5-B7; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B9-B11 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B13-B15; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B17-B19 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B21-B23; a variable light chain region comprising SEQ ID NO: B4 and a variable heavy region comprising SEQ ID NO: B8; a variable light chain region comprising SEQ ID NO: B12 and a variable heavy region comprising SEQ ID NO: B16; and a variable light chain region comprising SEQ ID NO: B20 and a variable heavy region comprising SEQ ID NO: B24. In some embodiments, the light chain variable domain can precede the heavy chain variable domain and they can be joined by a linker that includes 5-20 amino acids, preferably G and S. In some embodiments, the heavy chain variable domain can precede Attorney Docket No.40056-0104WO1 the light chain variable domain and they can be joined by a linker that includes 4-20 amino acids, preferably G and S. In some embodiments, such linkers can comprise GGGS (SEQ ID NO: D7) or repeats thereof, including the sequence: GGGGSGGGGSGGGGS (SEQ ID NO: D8) or GGGGSGGGGS (SEQ ID NO: D9), and can be located between the VH and VL domains. Other examples and BCMA-targeted moieties and BCMA scFvs are known in the art; for example, bb2121 (also called idecabtagene vicleucel, ide-cel, Abecma, bb2127, bb21217, LCAR-B38M (also called JNJ-4528), MCARH171 / ET140, DESCARTES-08, KITE-585, P-BCMA-10, and JCARH125 ( also called CARVYKTI®, ciltacabtagene autoleucel, orvacabtagene autoleucel); See also WO 2016 / 090320, WO 2016 / 014565, WO 2018 / 085690, WO 2019 / 149249, WO 2019 / 161035, WO 2021 / 127007, WO 2020 / 150339, WO 2021 / 091945, WO 2021 / 133712, US 2021 / 0128619 A1, US 2021 / 0330788 A1, US 2022 / 0003772 A1, WO 2022 / 040050, WO 2022 / 228429, WO / 2023 / 068382, WO 2023 / 220641, WO 2023 / 081752, WO 2023 / 230581, WO 2023 / 077343, WO 2023 / 109257, WO 2023 / 288185, US 20230270786 A1, and US 2024 / 0091264 A1; See also Table A1, Table A2, WO 2013 / 072415, US 2015 / 0376287 A1, WO 2017 / 031104, WO 2017 / 134134, WO 2018 / 119215, WO 2019 / 075378, WO 2019 / 164891, WO 2020 / 018820, US 2022 / 0041742 A1, WO2022 / 006316, US 2023 / 0272102 A1, US 2023 / 0257473 A1, US 20230398147 A1, and as described throughout). (b) Transmembrane Domain A CAR disclosed herein can contain a transmembrane domain, which can be a hydrophobic alpha helix that spans the membrane. As used herein, a transmembrane domain refers to any protein structure that is thermodynamically stable in a cell membrane, preferably a eukaryotic cell membrane. Transmembrane domains that can be used include those shown below in Table 1. Attorney Docket No.40056-0104WO1 Table 1: Examples of Transmembrane Domains (c) Spacer Domain A BCMA CAR described herein can include a spacer located between the BCMA targeting domain (i.e., a BCMA targeted scFv or functional variant thereof) and the transmembrane domain. Without being bound by theory, the spacer can function to provide flexibility to the CAR, or domains thereof, or to prevent steric hindrance of the CAR, or domains thereof. A variety of different spacers can be used. Some of them include at least portion of a human Fc region, for example a hinge portion of a human Fc region or a CH3 domain, or variants thereof. Table 2 below provides various spacers that can be used in the CARs or polypeptides described herein. Table 2: Examples of Spacer Domains Attorney Docket No.40056-0104WO1 Some spacer regions include all or part of an immunoglobulin (e.g., IgG1, IgG2, IgG3, IgG4) hinge region, i.e., the sequence that falls between the CH1 and CH2 domains of an immunoglobulin, e.g., an IgG4 Fc hinge or a CD8 hinge. Some spacer regions Attorney Docket No.40056-0104WO1 include an immunoglobulin CH3 domain (called CH3 or ΔCH2) or both a CH3 domain and a CH2 domain. The immunoglobulin derived sequences can include one or more amino acid modifications, for example, 1, 2, 3, 4 or 5 substitutions, e.g., substitutions that reduce off-target binding. The hinge / linker region can also comprise an IgG4 hinge region having the sequence ESKYGPPCPSCP (SEQ ID NO: 26) or ESKYGPPCPPCP (SEQ ID NO: 25). The hinge / linger region can also comprise the sequence ESKYGPPCPPCP (SEQ ID NO: 25) followed by the linker sequence GGGSSGGGSG (SEQ ID NO: 24) followed by IgG4 CH3 (HL-CH3) sequence GQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTT PPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK (SEQ ID NO: 34). Thus, the entire linker / spacer region can comprise the sequence: ESKYGPPCPPCPGGGSSGGGSGGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFY PSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSV MHEALHNHYTQKSLSLSLGK (SEQ ID NO: 31). In some cases, the spacer has 1, 2, 3, 4, or 5 single amino acid changes (e.g., conservative changes) compared to SEQ ID NO: 31. In some cases, the IgG4 Fc hinge / linker region that is mutated at two positions (L235E; N297Q) in a manner that reduces binding by Fc receptors (FcRs). (d) Intracellular Signaling Domains A CAR construct described herein contains one or more intracellular signaling domains (e.g., CD3ζ, and optionally one or more co-stimulatory domains), which are the functional end of the receptor. Following antigen recognition, receptors cluster and a signal is transmitted to the cell. CD3ζ is the cytoplasmic signaling domain of the T cell receptor complex. CD3ζ contains three immunoreceptor tyrosine-based activation motifs (ITAMs), which transmit an activation signal to the T cell after the T cell is engaged with a cognate antigen. In some cases, CD3ζ provides a primary T cell activation signal but not a fully competent activation signal, which requires a co-stimulatory signal. Accordingly, in some examples, the CAR constructs disclosed herein may further comprise one or more co-stimulatory signaling domains in addition to CD3ζ. For Attorney Docket No.40056-0104WO1 example, the co-stimulatory domain CD28 and / or 4-1BB can be used to transmit a proliferative / survival signal together with the primary signaling mediated by CD3ζ. The co-stimulatory domain(s) are located between the transmembrane domain and the CD3ζ signaling domain. Table 3 includes examples of suitable co-stimulatory domains together with the sequence of the CD3ζ signaling domain. Table 3: CD3ζ Domain and Examples of Co-stimulatory Domains Attorney Docket No.40056-0104WO1 In some examples, the CD3ζ signaling domain comprises an amino acid sequence that is at least 90%, at least 95%, at least 98% identical to SEQ ID NO: 35. In such instances, the CD3ζ signaling domain has 1, 2, 3, 4, or 5 single amino acid changes (preferably conservative substitutions) compared to SEQ ID NO: 35. In other examples, the CD3ζ signaling domain is SEQ ID NO: 35. In various embodiments: the co-stimulatory domain is selected from the group consisting of: a co-stimulatory domain depicted in Table 3 or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications, a CD28 co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications, a 4-1BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications and an Attorney Docket No.40056-0104WO1 OX40 co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications. In certain embodiments, a 4-1BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications is present in the CAR polypeptides described herein. In some embodiments, there are two co-stimulatory domains, for example, a CD28 co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions) and a 4-1BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions). In various embodiments the 1-5 (e.g., 1 or 2) amino acid modification are substitutions. In various embodiments, the co-stimulatory domain is amino terminal to the CD3ζ signaling domain and a short linker consisting of 2 – 10, e.g., 3 amino acids (e.g., GGG) can be positioned between the co-stimulatory domain and the CD3ζ signaling domain. In various embodiments: the costimulatory domain is selected from the group consisting of: a CD28 costimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2 acid modifications, a 4-l BB costimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications and an OX40 costimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications. In certain embodiments, a 4-1BB costimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications in present. In some embodiments there are two costimulatory domains, for example a CD28 co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions) and a 4-l BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions). In various embodiments the 1-5 (e.g., 1 or 2) amino acid modification are substitutions. In some embodiments, there is a short sequence of 1-6 amino acids (e.g. GGG) between the co-stimulatory domains and the CD3ξ signaling domain and / or between the two co- stimulatory domains. Also disclosed are populations of human immune cells (e.g., human T cells or human NK cells) transduced by a nucleic acid molecule encoding a chimeric antigen receptor, wherein chimeric antigen receptor comprises: a BCMA targeting domain (e.g., an scFv targeted to BCMA or functional variant thereof); Attorney Docket No.40056-0104WO1 a transmembrane domain selected from: a CD4 transmembrane domain or variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2) amino acid modifications (e.g., substitutions), a CD8 transmembrane domain or variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2) amino acid modifications (e.g., substitutions), a CD28 transmembrane domain or a variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2) amino acid modifications (e.g., substitutions), and a CD3ξ transmembrane domain or a variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2) amino acid modifications (e.g., substitutions); a costimulatory domain (e.g., a CD28 co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions); or a 4-l BB co- stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions); or both a CD28 co-stimulatory domain or a variant thereof having 1- 5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions) and a 4-lBB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) amino acid modifications (e.g., substitutions); and a CD3ξ signaling domain or a variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2) amino acid modifications (e.g., substitutions). The CAR can include a spacer region located between the BCMA targeting domain (e.g., a BCMA scFv) and the transmembrane domain. A variety of different spacers can be used. Some of them include at least portion of a human Fc region, for example a hinge portion of a human Fc region or a CH3 domain or variants thereof. In various embodiments: the population of human T cells comprises central memory T cells (TCM cells) e.g., at least 20%, 30%, 40%, 50% 60%, 70%, 80% of the cells are TCMcells, or the population of T cells comprises a combination of central memory T cells, naive T cells and stem central memory cells (TCM / SCM / Ncells) e.g., at least 20%, 30%, 40%, 50% 60%, 70%, 80% of the cells are TCM / SCM / N cells. In either case, the population of T cells includes both CD4+ cells and CD8+ cells (e.g., at least 20% of the CD3+ T cells are CD4+ and at least 3% of the CD3+ T cells are CD8+ and at least 70, 80 or 90% are either CD4+ or CD8+; at least 15%, 20%, 25%, 30%, 35%, 40%, 50%, 60% of the cells CD3+ cells are CD4+ and at least 4%, 5%, 8%, 10%, 20 of the CD3+ cells are CD8+ cells). Attorney Docket No.40056-0104WO1 Other examples of BCMA-targeted CAR and BCMA scFv are known in the art; for example, bb2121 (also called idecabtagene vicleucel, ide-cel, Abecma, bb2127, bb21217, LCAR-B38M (also called JNJ-4528), MCARH171 / ET140, DESCARTES-08, KITE-585, P-BCMA-10, and JCARH125 (also called CARVYKTI®, ciltacabtagene autoleucel, orvacabtagene autoleucel); See also WO 2016 / 090320, WO 2016 / 014565, WO 2018 / 085690, WO 2019 / 149249, WO 2019 / 161035, WO 2021 / 127007, WO 2020 / 150339, WO 2021 / 091945, WO 2021 / 133712, US 2021 / 0128619 A1, US 2021 / 0330788 A1, US 2022 / 0003772 A1, WO 2022 / 040050, WO 2022 / 228429, WO / 2023 / 068382, WO 2023 / 220641, WO 2023 / 081752, WO 2023 / 230581, WO 2023 / 077343, WO 2023 / 109257, WO 2023 / 288185, US 20230270786 A1, and US 2024 / 0091264 A1; See also Table A1, Table A2, WO 2013 / 072415, US 2015 / 0376287 A1, WO 2017 / 031104, WO 2017 / 134134, WO 2018 / 119215, WO 2019 / 075378, WO 2019 / 164891, WO 2020 / 018820, US 2022 / 0041742 A1, WO2022 / 006316, US 2023 / 0272102 A1, US 2023 / 0257473 A1, US 20230398147 A1, and as described throughout). Any of the methods described herein can comprise administering a population of autologous or allogeneic BCMA-targeted human immune cells (e.g., macrophages, NK cells, NKT cells, T cells, subpopulations of one or more thereof, and combinations thereof). Combination Therapies In some embodiments, any of the methods described herein further comprise administering to the subject an effective amount of a population of immune cells expressing a CAR or harboring a nucleic acid encoding a CAR targeted to cancer cells (e.g., solid tumor cells; e.g., HER2-expressing cells). In some embodiments, the CAR is targeted to HER2. In some embodiments, a HER2 CAR comprises a scFv targeted to HER2. In some embodiments, the solid tumor is a HER2-expressing cancer. In some embodiment, the population of immune cells expressing a CAR or harboring a nucleic acid encoding a CAR is a population of HER2 CAR T cells. In some embodiments, the population of immune cells expressing a CAR or harboring a nucleic acid encoding a CAR (e.g., HER2 CAR T cells) are autologous or allogeneic. In some embodiments, the Attorney Docket No.40056-0104WO1 population of immune cells expressing a CAR or harboring a nucleic acid encoding a CAR (e.g., HER2 CAR T cells) are administered simultaneously or subsequently to administering to the subject a BCMA-targeted therapy described herein (e.g., TCE- BCMA or BCMA CAR T cells). In some embodiments, the HER2 CAR T cells are administered at least or about 0.1, 0.25, 0.5, 0.75, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 26, 17, 18, 19, or 20 days after administration of the TCE. In some embodiments, the HER2 CAR T cells are administered at least or about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 26, 17, 18, 19, or 20 weeks after administration of the TCE. Useful HER2 CAR constructs are described in WO 2017 / 079694. In general, HER2 CAR include a HER2 scFv, a spacer domain, a transmembrane domain, one or more co-stimulatory domains, and a CD3zeta cytoplasmic domain. For example, a HER2 CAR can comprise or consist of the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSA SFLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGQGTKVEIKG STSGGGSGGGSGGGGSSEVQLVESGGGLVQPGGSLRLSCAASGFNIKDTYIHWVR QAPGKGLEWVARIYPTNGYTRYADSVKGRFTISADTSKNTAYLQMNSLRAEDTA VYYCSRWGGDGFYAMDYWGQGTLVTVSSESKYGPPCPPCPAPEFEGGPSVFLFPP KPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFQST YRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPS QEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSR LTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKMFWVLVVVGGVLAC YSLLVTVAFIIFWVRSKRSRGGHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS GGGRVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPR RKNPQEGLYNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDA LHMQALPPR (SEQ ID NO:ZZ1), or a variant thereof have 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in the HER2 targeting domain (e.g., the CDRs of the HER2 scFv). A useful HER2 CAR can comprise or consist of the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSA SFLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGQGTKVEIKG STSGGGSGGGSGGGGSSEVQLVESGGGLVQPGGSLRLSCAASGFNIKDTYIHWVR Attorney Docket No.40056-0104WO1 QAPGKGLEWVARIYPTNGYTRYADSVKGRFTISADTSKNTAYLQMNSLRAEDTA VYYCSRWGGDGFYAMDYWGQGTLVTVSSESKYGPPCPPCPAPEFEGGPSVFLFPP KPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFQST YRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPS QEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSR LTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKIYIWAPLAGTCGVLLL SLVITKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCELGGGRVKFSR SADAPAYQQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLY NELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR (SEQ ID NO:ZZ2), or a variant thereof have 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in the HER2 targeting domain (e.g., the CDRs of the HER2 scFv). A useful HER2 scFv can comprise or consist of the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSASFLYS GVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGQGTKVEIKGGGGS GGGGSGGGGSEVQLVESGGGLVQPGGSLRLSCAASGFNIKDTYIHWVRQAPGKG LEWVARIYPTNGYTRYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCSR WGGDGFYAMDYWGQGTLVTVSS (SEQ ID NO:ZZ3) or is least 90%, 95%.98%, 99% identical to SEQ ID NO:ZZ3. A HER2 scFv can comprise: a light chain variable domain that is at least 90%, 95%, 98%, 99% or 100% identical to: DIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSASFLYS GVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGQGTKVEIK (SEQ ID NO: ZZ4) and comprises light chain CDRs 1-3 (underlined) and a heavy chain variable domain that is at least 90%, 95%, 98%, 99% or 100% identical to: EVQLVESGGGLVQPGGSLRLSCAASGFNIKDTYIHWVRQAPGKGLEWVARIYPT NGYTRYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCSRWGGDGFYAM DYWGQGTLVTVSS (SEQ ID NO: ZZ5) and comprises heavy chain CDRs 1-3 (underlined). In some embodiments, the light chain variable domain can precede the heavy chain variable domain and they can be joined by a linker that includes 5-20 amino acids, preferably G and S; as described above. Attorney Docket No.40056-0104WO1 A useful scFv can target HER2. A useful HER2 scFv can comprise or consist of the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCKASQDVSIGVAWYQQKPGKAPKLLIYSASYRYT GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGQGTKVEIKGGGGS GGGGSGGGGSEVQLVESGGGLVQPGGSLRLSCAASGFTFTDYTMDWVRQAPGK GLEWVADVNPNSGGSIYNQRFKGRFTLSVDRSKNTLYLQMNSLRAEDTAVYYCA RNLGPSFYFDYWGQGTLVTVSS (SEQ ID NO:ZZ6) or is least 90%, 95%, 98%, 99% identical to SEQ ID NO:ZZ6. A HER2 scFv can comprise: a light chain variable domain that is at least 90%, 95%, 98%, 99% or 100% identical to: DIQMTQSPSSLSASVGDRVTITCKASQDVSIGVAWYQQKPGKAPKLLIYSASYRYT GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGQGTKVEIK (SEQ ID NO: ZZ7) and comprises light chain CDRs 1-3 (underlined) and a heavy chain variable domain that is at least 90%, 95%, 98%, 99% or 100% identical to: EVQLVESGGGLVQPGGSLRLSCAASGFTFTDYTMDWVRQAPGKGLEWVADVNP NSGGSIYNQRFKGRFTLSVDRSKNTLYLQMNSLRAEDTAVYYCARNLGPSFYFD YWGQGTLVTVSS (SEQ ID NO: ZZ8) and comprises heavy chain CDRs 1-3 (underlined). In some embodiments, the light chain variable domain can precede the heavy chain variable domain and they can be joined by a linker that includes 5-20 amino acids, preferably G and S, as described above. Generally, a useful HER2 CAR can comprise: any HER2 scFv described herein or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions), wherein the modifications are not in a CDR region; a transmembrane domain selected from: a CD4 transmembrane domain or variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions), a CD8 transmembrane domain or variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions), a CD28 transmembrane domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions), and a CD3ξ transmembrane domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions); Attorney Docket No.40056-0104WO1 a costimulatory domain (e.g., a CD28 co-stimulatory domain or a variant thereof having 1- 5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions); or a 4-l BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions); or both a CD28 co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions) and a 4-l BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions); and a CD3ξ signaling domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications. Also disclosed are populations of human immune cells (e.g., human T cells or human NK cells) transduced by a nucleic acid molecule encoding a chimeric antigen receptor, wherein chimeric antigen receptor comprises: an domain targeted to HER2 (e.g., a HER2 scFv); a transmembrane domain selected from: a CD4 transmembrane domain or variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2 amino acid modifications) (e.g., substitutions), a CD8 transmembrane domain or variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2 amino acid modifications) (e.g., substitutions), a CD28 transmembrane domain or a variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2 amino acid modifications) (e.g., substitutions), and a CD3ξ transmembrane domain or a variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2 amino acid modifications) (e.g., substitutions); a costimulatory domain (e.g., a CD28 co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions); or a 4-l BB co-stimulatory domain or a variant thereof having 1-5 single (e.g., 1 or 2) amino acid modifications (e.g., substitutions); or both a CD28 co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions) and a 4-1BB co- stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions); and CD3ξ signaling domain of a variant thereof having 1-5 single amino acid modifications (e.g., 1 or 2 amino acid modifications) (e.g., substitutions). The CAR can include a spacer region located between the tumor targeting domain (e.g., a scFv; e.g., a HER2 scFv) and the transmembrane domain. A variety of different Attorney Docket No.40056-0104WO1 spacers can be used as described above (e.g., in Table 2). Some of them include at least portion of a human Fc region, for example a hinge portion of a human Fc region or a CH3 domain or variants thereof. In various embodiments: the population of human T cells comprises central memory T cells (TCM cells) e.g., at least 20%, 30%, 40%, 50% 60%, 70%, 80% of the cells are TCM cells, or the population of T cells comprises a combination of central memory T cells, naive T cells and stem central memory cells (TCM / SCM / Ncells) e.g., at least 20%, 30%, 40%, 50% 60%, 70%, 80% of the cells are TCM / SCM / Ncells. In either case, the population of T cells includes both CD4+ cells and CD8+ cells (e.g., at least 20% of the CD3+ T cells are CD4+ and at least 3% of the CD3+ T cells are CD8+ and at least 70, 80 or 90% are either CD4+ or CD8+; at least 15%, 20%, 25%, 30%, 35%, 40%, 50%, 60% of the cells CD3+ cells are CD4+ and at least 4%, 5%, 8%, 10%, 20 of the CD3+ cells are CD8+ cells). Any of the methods described herein can further comprise administering a population of autologous or allogeneic HER2-targeted human immune cells (e.g., macrophages, NK cells, NKT cells, T cells, subpopulations of one or more thereof, and combinations thereof). In some embodiments, useful autologous or allogenic T cells comprise central memory T cells (TCMcells) or a combination of central memory T cells, naive T cells, and stem central memory cells (i.e., the T cells are TCM / SCM / N cells). In some embodiments, the population of T cells includes both CD4+ cells and CD8+ cells. In some embodiments, the immune cells express a CAR or are transduced by a nucleic acid encoding a CAR (e.g., a HER2 CAR). An “amino acid modification” refers to an amino acid substitution, insertion, and / or deletion in a protein or peptide sequence. An “amino acid substitution” or “substitution” refers to replacement of an amino acid at a particular position in a parent peptide or protein sequence with another amino acid. A substitution can be made to change an amino acid in the resulting protein in a non-conservative manner (i.e., by changing the codon from an amino acid belonging to a grouping of amino acids having a particular size or characteristic to an amino acid belonging to another grouping) or in a conservative manner (i.e., by changing the codon from an amino acid belonging to a Attorney Docket No.40056-0104WO1 grouping of amino acids having a particular size or characteristic to an amino acid belonging to the same grouping). Such a conservative change generally leads to less change in the structure and function of the resulting protein. The following are examples of various groupings of amino acids: 1) Amino acids with nonpolar R groups: Alanine, Valine, Leucine, Isoleucine, Proline, Phenylalanine, Tryptophan, Methionine; 2) Amino acids with uncharged polar R groups: Glycine, Serine, Threonine, Cysteine, Tyrosine, Asparagine, Glutamine; 3) Amino acids with charged polar R groups (negatively charged at pH 6.0): Aspartic acid, Glutamic acid; 4) Basic amino acids (positively charged at pH 6.0): Lysine, Arginine, Histidine (at pH 6.0). Another grouping may be those amino acids with phenyl groups: Phenylalanine, Tryptophan, and Tyrosine. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Methods and materials are described herein for use in the present invention; other, suitable methods and materials known in the art can also be used. The materials, methods, and examples are illustrative only and not intended to be limiting. All publications, patent applications, patents, sequences, database entries, and other references mentioned herein are incorporated by reference in their entirety. In case of conflict, the present specification, including definitions, will control. Other features and advantages of the invention will be apparent from the following detailed description and figures, and from the claims. DESCRIPTION OF DRAWINGS FIGS.1A-1E. OV effectively delivers BCMAt to solid tumors and redirects activation and cytotoxicity of BCMA-CAR T cells or human T cells in the presence of BCMA-TCE in vitro. FIG.1A) Illustration of vaccinia OV with BCMAt incorporated under the control of the synthetic early promoter inserted into the J2R locus and replacing a portion of the gene. FIG.1B) Quantification of BCMAt expression on various solid tumor cell lines after 24 hours (left) and 48 hours (right) exposure to indicated MOI of OVBCMAt. FIGS.1C-1E) Quantification of CD137 expression (left), tumor cell killing (middle), and BCMAt expression (right) assessed by flow cytometry. Attorney Docket No.40056-0104WO1 FIG.1C) MDA-MB-468, FIG.1D) SNU-16, and FIG.1E) OV90 tumor cells were co- cultured with or without BCMA-TCE in the presence of human T cells or BCMA-CAR T cells and indicated MOI of OVBCMAt. FIGS.2A-2B. Anti-tumor efficacy of combination therapy using OVBCMAt and BCMA-CAR T cells in human xenograft MDA-MB-468 tumor model. FIG.2A) Percent of BCMAt expression on tumor cells. NSG mice were engrafted with subcutaneous MDA-MB-468 tumors (5x106cells), and at day 38, mice were intratumorally (i.t.) injected with 0 (n=4) or 106 (n=7) plaque-forming units (pfu) of OVBCMAt per mouse, which were harvested at day 7 after treatment. FIG.2B) NSG mice were engrafted with subcutaneous MDA-MB-468 tumors (5x106cells), and at day 38 mice were i.t. injected with 106pfu of OVBCMAt. On day 45, tumors were injected with either TAG72-CAR T cells or BCMA-CAR T cells (5x106cells). Tumor volumes are shown as means ± SEM (n≥8 per group). FIGS.3A-3C. In vivo efficacy of combination therapy of BMCA-TCE and OVBCMAt in a human xenograft MDA-MB-468 tumor model. FIG.3A) Schematic of subcutaneous MDA-MB-468 tumor-bearing NSG mice (5x106cells on day 0) treated with intratumoral (IT) OVBCMAt (1x106pfu) on day 38, engrafted with intravenous (IV) PBMC (1x107cells) on day 40, and treated with IV BCMA-TCE (25 ug / dose, 8 times) on days 41-43 and 46-50. FIG.3B) Tumor volumes are shown as mean ± SEM (n ³ 5 per group). FIG.3C) Tumor measurements of each replicated from the average volumes shown in FIG.3B. FIGS.4A-4B. BCMAt expression by OVBCMAt induces cytokine secretion of human T cells in the presence of BCMA-TCE. (FIG.4A) IFN-g and (FIG.4B) IL-2 production measured by enzyme-linked immunosorbent assay (ELISA) in supernatants collected from co-cultures with or without BCMA-TCE and human T cells or BCMA- CAR T cells with addition of indicated MOIs of OV19t after 24 hours. quantified at 24 and 48 hours using flow cytometry. FIG.5 is a schematic of a map of an OVBCMAt. FIGS.6A-6AF provide the nucleotide sequence of an OVBCMAt (SEQ ID NO: A1). The sequences for the synthetic early promoter (pSE, “promotor”) and the sequence Attorney Docket No.40056-0104WO1 encoding human truncated BCMA (“BCMAt”) are underlined and identified on part 14 (FIG.6N). The remnants of the J2R gene are also underlined and identified. FIGS.7A-7AU provides the nucleotide sequence for the parent strain OV (CF33; SEQ ID NO: A2). The J2R gene encoding thymidine kinase (tk) is identified on part 20 (FIG.7T). Deletions of the J2R gene for transgene insertion can comprise all of or a portion of these nucleotides; e.g., the nucleotides deleted for transgene insertion in various constructs can comprise the nucleotides underlined and identified by [del1] designations (e.g., [del1 start] & [del1 end]) or are double underlined and identified by [del2] designations (e.g., [del2 start] & [del2 end]). DETAILED DESCRIPTION The present application is directed to, inter alia, the ability of OV to deliver truncated BCMA to solid tumors to be targeted with bispecific T cell engagers (TCE) to induce endogenous T cell activation and anti-tumor responses. The current findings support a fully off-the-shelf therapeutic combination with immediate clinical applications. Further, we demonstrate that this paradigm can be advanced with two clinically active TCEs, with the prospect of additional tumor antigens that may be exploited for this combinatorial immunotherapy strategy. Using a TCE rather than a CAR T cell carries several key advantages. Given the length of time required to generate patient-specific target-specific CAR T cells, we reasoned that the availability of off-the-shelf immunotherapies overcomes time restraints for patients undergoing treatment. With current manufacturing practices and capacities, the demand for CAR T cells exceeds supply and is still viewed as a niche technology that not all sites can perform

[0017] . Moreover, TCEs such as blinatumomab provide a safety advantage over CAR T cells due to the nature of their short in vivo half-life and dosing strategies [18, 19]. This treatment can then be suspended or delayed if needed, with the potential for reversing unfavorable immune-related adverse effects. Importantly, the proof-of-concept trial for the combination therapy using OVBCMAt and blinatumomab is underway with recent FDA clearance. Attorney Docket No.40056-0104WO1 EXAMPLES The invention is further described in the following examples, which do not limit the scope of the invention described in the claims. MATERIALS AND METHODS Study design All in vitro assays were performed with at least duplicate samples and were repeated in at least three independent experiments. All in vivo studies were performed using 6- to 8-week-old NSG, using at least three mice per group for all studies, and four to nine mice were included within each group for all therapeutic and survival studies to ensure statistical power and evenly distributed tumor sizes across groups at treatment initiation. The health condition of mice was monitored daily by the Department of Comparative Medicine at City of Hope with euthanasia applied according to the American Veterinary Medical Association Guidelines. Investigators were not blinded when monitoring mouse survival. All studies were performed under approved protocols of the Institutional Animal Care and Use Committee and the institutional review board. Cell lines and viruses Human triple-negative breast cancer cell line MDA-MB-468 [American Type Culture Collection (ATCC); HTB-132] was cultured in Dulbecco’s modified Eagle’s medium (DMEM) containing 10% fetal bovine serum (FBS; HyClone) and 1x antibiotic / antimycotic (AA; Gibco), supplemented with 25 mM Hepes (Irvine Scientific) and 2 mM L-glutamine (Thermo Fisher Scientific; complete DMEM). Both MDA-MB- 468-CD19t and MDA-MB-468-HER2 cell lines were cultured as mentioned above. Human pancreatic cancer cell line Capan-1 (ATCC, HTB-79) was cultured in Iscove’s modified Dulbecco’s medium containing 20% FBS and 1x AA. Human pancreatic cancer cell line Panc-1 (ATCC, CRL-1469) was cultured in RPMI containing 10% FBS and 1x AA. Human ovarian cancer cell line OV90 (ATCC CRL-11732) was cultured in 1:1 volume of MCDB 105 medium (Sigma-Aldrich) and medium 199 (Gibco) containing 20% FBS and 1x AA. Human head and neck carcinoma line UM-SCC-47 (EMD Millipore) was cultured in DMEM containing 10% FBS, 1x AA, and 1x non-essential Attorney Docket No.40056-0104WO1 amino acids (NEAA). Human prostate cancer cell line DU145 (ATCC, HTB-81) was cultured in RPMI containing 10% FBS and 1x AA. Human glioblastoma cell line U251T (gift from W. Debinski, Wake Forest School of Medicine) was cultured in complete DMEM. Human embryonic kidney cell line 293T (ATCC CRL-3216) and human fibrosarcoma cell line HT1080 (ATCC CCL-121) were cultured in complete DMEM. African green monkey kidney fibroblasts (CV-1; ATCC CCL-70) were cultured in DMEM containing 10% FBS and 1x AA. CV-1 cells were used for both amplification and titration of orthopoxviruses. PACBIO Single Molecule, Real-Time (SMRT) Sequencing To construct the SMRTbell libraries, a PacBio standard protocol (20-kb Template Preparation Using BluePippin Size-Selection System) was applied. Using Covaris g- TUBE devices (Woburn, MA), the DNA samples were sheared at 4800 rpm for 2 minutes in Eppendorf Mini Spin plus (Hauppauge, NY), and 0.45X volume of AMPure PB magnetic beads of PacBio (Menlo Park, CA) was applied to concentrate the DNA fragments. To remove single-stranded ends from the DNA fragments, 0.2 U / ul of ExoVII in SMRTbell Template Prep Kit 1.0 of PacBio (Menlo Park, CA) was treated at 37°C for 15 minutes. To repair the damages on the DNA templates, 1X DNA Damage Repair Mix in SMRTbell Template Prep Kit 1.0 of PacBio (Menlo Park, CA) was treated at 37°C for 20 minutes. To generate the blunt ends of the DNA, 1X End Repair Mix in SMRTbell Template Prep Kit 1.0 of PacBio (Menlo Park, CA) was treated at 25°C for 5 minutes. To ligate the SMRTbell adapters onto the blunt ended DNA, 5 uM of Annealed Blunt Adapters were applied with 0.75 U / ul of Ligase in SMRTbell Template Prep Kit 1.0 of PacBio (Menlo Park, CA). The ligation mixture was incubated at 25°C overnight and then incubated 65°C for 10 minutes. To degrade failed ligation products, ExoIII and ExoVII in SMRTbell Template Prep Kit 1.0 of PacBio (Menlo Park, CA) was treated at 37°C for 1 hour. After ExoIII and ExoVII Treatments of Library, the same amount (38.6 ng) of each sample was pooled. All reagents for this protocol were provided by PacBio (Menlo Park, CA) and the reagent concentrations in the protocol were calculated by the Sample Setup module in PacBio SMRT Link (v10.0.0.108728). The Sequencing Primer (1 ul) was diluted by 29 ul Attorney Docket No.40056-0104WO1 of Elution Buffer and the mixture was incubated at 80°C for 2 minutes. And, the conditioned sequencing primers were incubated with the library at 20°C for 1 hour.1 ul of Sequel Polymerase 3.0 was diluted by 9 ul of Sequel Binding Buffer.1.5 ul of the diluted polymerase was applied to the library with the sequencing primers, and 14.9 ul of the mixture was incubated at 30°C for 1 hour. The proper volume of all solutions in this step was calculated by SMRT Link’s Setup module. Complex Dilution Buffer was added into the polymerase complex, first, and Qubit checked the concentration. After adding AMPure PB beads into the diluted complex, it was incubated for 5 minutes on a rotator. The collected beads on a magnetic rack was resuspended by Complex Dilution buffer, directly, without any ethanol rinse and the polymerase complex was eluted for 15 minutes on a rotator. The concentration of the eluate was measured by Qubit again to calculate the final loading dilution. Each calculated volume of Complex Dilution Buffer, Polymerase-Complex, Diluted Control, DTT and Sequel Additive was mixed in 85 ul as the final loading dilution on the sample plate and it was loaded into Sequel UI v10.0.0.108728. The concentration of the sample on the plate was 8 pM and Movie Time was 20 hours and 2 hours of Pre-Extension Time was applied. The primary analyses, including real-time signal processing and base calling were processed by a built-in PacBio Blade Center through Sequel ICS, and result stream directly to SMRT Link (v10.0.0.108728). The demultiplexing process was carried out by the Demultiplex Barcode module which Infer Barcode Used option was set as false in SMRT Link (v10.0.0.108728). The high-fidelity (HiFi) CCS reads were generated by SMRT Link (v10.0.0.108728) Circular Consensus Sequences (CCS) module. CCS reads shorter than 5,000bp were removed before aligning to the reference. Mapping to the reference was performed using pbmm2v 1.0.0 with CCS preset parameters and “-N 1 -l 2500” option. Samtools v0.1.19 was used to pile up the reads and VarScan v2.3.9 was used to call variants and indels using the following option “--min-coverage 20 --min- reads210 --min-var-freq 0.9 --min-avg-qual 1 --strand-filter 0”. The CCS reads were also filtered using samclip (github.com / tseemann / samclip) for soft and hard clipped alignments, with 50 bp as maximum clip length. To perform the de novo assembly, the HiFi CCS reads were produced by the Circular Consensus Sequences (CCS) module in Attorney Docket No.40056-0104WO1 SMRT Link (v10.0.0.108728) using the default setting. The fasta file was subjected to the de novo assembly using Canu (v2.1) with the genome size (190 kb) and the batMemory=200 options. If a mis-assembly were suspected, another Canu assembly was carried out using the randomly selected reads by a QIIME Script (subsample_fasta.py). The structural feature of the contig sequence was investigated using dotted plot via Seqtools (v4.44.0) and the comparison of the sequences between the contig and its reference was performed by Blastn to discover any sequence variants. The global sequence alignment was done using Stretcher (ebi.ac.uk / jdispatcher / psa / emboss_stretcher) with default parameters. Blastn (blast.ncbi.nlm.nih.gov / Blast.cgi) was used for local sequence alignment. The genome was annotated the reference genome with ORFfinder (ncbi.nlm.nih.gov / orffinder / ) and the ORFs are searched against the nr database in NCBI. The annotations are visualized using SnapGene. Generation of recombinant chimeric orthopoxvirus expressing human BCMAt To generate a shuttle vector containing the human (hCD19t) CD19t expression cassette with the VACV PSE, the hCD19t complementary DNAs (cDNAs) were polymerase chain reaction (PCR) amplified from the plasmids hCD19t-2A-IL2-pHIV7 and mCD19t-epHIV7 using Q5 High-Fidelity 2X Master Mix (New England Biolabs Inc., Ipswich, MA) and the following primers: 5′-GCG GTC GAC CAC CAT GCC ACC TCC TCG CCT CCT CTT CTT CCT CCT CTT CCTC-3′ and 5′-GCG GGA TCC ATA AAA ATT AAT TAA TCA TCT TTT CCT CCT CAG GAC CAG GGC TCT TTG AAG ATG-3′. The PCR fragment was digested with Sal I and Bam HI and cloned into the same-cut p33NCTK-SE-hNIS replacing hNIS to yield p33NCTK-SE-hCD19t and p33NCTK-SE-mCD19t. The hCD19t and mCD19t cDNAs in p33NCTK-SE-hCD19t and p33NCTK-SE-mCD19t were confirmed by sequencing. CV-1 cells were infected with CF33 at an MOI of 0.1 for 1 hour and then transfected with p33NCTK- SE-hCD19t and p33NCTK-SE-mCD19t by using jetPRIME in vitro DNA and small interfering RNA transfection reagent (Polyplus-transfection Inc., New York, NY). Two days after infection, infected and transfected cells were harvested, and recombinant viruses (OV19t) were selected and plaque purified as described previously (13). Attorney Docket No.40056-0104WO1 This process was similarly carried out to develop a recombinant virus containing BCMAt (OVBCMAt), containing the BCMA sequence lacking the intracellular domain. DNA constructs MDA-MB-468 cells were engineered to express hCD19t by transduction with epHIV7 lentivirus carrying the human CD19t gene under the control of the EF1 promoter. This same process was used to engineer the expression of HER2 in MDA-MB- 468. The human CD19-28z CAR lentiviral construct with hEGFRt separated by a T2A ribosome skip sequence was used as previously described (21). The human HER2-41BBz CAR lentiviral construct previously described (22) was modified to remove the CD19t domain. For T cell trafficking studies, the firefly luciferase (ffluc) gene was cloned into an epHIV7 lentivirus construct and then used to transduce human T cells cultured as previously described (23). Human T cell enrichment, lentivirus production and transduction, and ex vivo expansion T cell isolation, lentivirus production and transduction, and ex vivo expansion of untransduced (mock) and CAR T cells were performed as previously described (23). Untransduced human T cells in all studies were processed in parallel with CAR T cells. Extracellular staining and flow cytometry Flow cytometric analysis was performed as previously described [13, 23]. Tumor cells and T cells were discriminated using CD45 (PerCP, BD Biosciences) for all in vitro studies. T cell activation was determined by using antibodies against CD69 and 4-1BB (CD137) (BD Biosciences). HER2 expression on tumor cells was determined using a HER2 antibody (PE, BD Biosciences). Tumor cells were identified using an antibody recognizing Ep-CAM (APC, BioLegend) for all in vivo studies. BCMAt expression following virus infection were determined using an antibody against BCMA (PE, BioLegend) for all in vitro and in vivo studies, respectively. For the detection of TCE on the surface of T cells, biotinylated Protein-L (brand) and a secondary streptavidin PE (BD Biosciences) antibody were used. Samples were then washed twice, stained with DAPI Attorney Docket No.40056-0104WO1 for viability, and processed on the MACSQuant Analyzer 10 or 16 (Miltenyi Biotec). Data were analyzed with FlowJo software (v10, TreeStar). OV transduction and T cell functional assays For OVBCMAt transduction and tumor killing assays, tumor targets plated with varying multiplicity of infections (MOIs) of OVBCMAt were co-cultured with untransduced T cells or PBMCs at varying effector T cell–to–tumor cell ratios along with TCE concentrations of either 0, 20, 100, or 500 ng / mL (Teclistamab; BCMA-TCE). Tecvalyi® (Teclistamab; BCMA-TCE) was used at a concentration of either 1, 10, or 100 ug / mL in culture. Cocultures were maintained in complete X-VIVO (Lonza) and in the absence of exogenous cytokines in round-bottom 96-well tissue culture–treated plates (Corning) for 1 to 3 days and analyzed by using flow cytometry as described above. Tumor cell killing by T cells with TCE was calculated by comparing CD45− cell counts relative to the killing observed by T cells without TCE from the same healthy donor in the absence of OV. For T cell activation assays, T cells and tumor targets were cocultured at an effector T cell–to–tumor cell ratio of 1:1 along with varying MOIs of OV in complete X-VIVO in the absence of exogenous cytokines in 96-well plates for 1 to 3 days and analyzed by using flow cytometry for specific markers of T cell activation. For the preloading of TCE onto T cells, T cells and PBMCs were thawed and rested overnight in X-VIVO containing 10% FBS and IL-2 (100 U / mL) and IL-15 (0.5 ng / mL) cytokines. T cells and PBMCs (3 x106cells / mL) were then incubated on ice for 30 minutes with 10 ug / mL, 25 ug / mL, 50 ug / mL or 100 ug / mL TCE. Following incubation, T cells were then washed with PBS and co-cultured with tumor cells targets with varying MOIs of OV. T cell activation and killing was determined as previously mentioned. Cytokine enzyme-linked immunosorbent assay Tumor cells and T cells were plated into 96-well round-bottom plates (Costar) along with varying MOIs of OVBCMAt in the presence or absence of BCMA-targeting TCE. After incubations at 37°C for 24, 48, or 72 hours, supernatants were collected and analyzed according to the human IFN- or IL-2 enzyme-linked immunosorbent assay Attorney Docket No.40056-0104WO1 (ELISA) Ready-SET-Go! (eBioscience) manufacturer’s protocol. Plates were read at 450 nm and 570 nm using the Cytation 3 Cell Imaging Multi-Mode Reader and Gen5 Microplate Reader and Imager Software (BioTek).. In vivo studies All animal experiments were performed under protocols approved by the City of Hope Institutional Animal Care and Use Committee. For human tumor xenograft studies, MDA-MB-468 cells (5 × 106cells per mouse) were prepared in PBS and injected subcutaneously into the flank of female NSG mice. Tumor growth was monitored 2-3 times per week by caliper measurement. Once tumor volumes reached about 100 to 300 mm3, OVBCMAt virus was prepared and diluted in PBS (pH 7.4) and intratumorally administered at 106pfu per MDA-MB-468 tumor-bearing mice.2 days post OVBCMAt treatment, PBMCs were isolated from leukapheresis products obtained from a consented research participant (healthy donor) under protocols approved by the City of Hope (COH) Internal Review Board (IRB using density gradient centrifugation over Ficoll-Paque (GE Healthcare) followed by multiple washes in PBS / EDTA (Milteny Biotec). PBMCs were then counted, washed, and prepared in PBS (pH 7.4) for intravenous tail vein injection (5 x 106cells per mouse). Four days post T cell engraftment, mice were treated with TCE (25 ug / ms in PBS) intravenously for five consecutive days (Monday - Friday) and then again for three consecutive days the following week (Monday - Wednesday) for a total of 8 treatments (64 ug total per mouse). Mice were euthanized two weeks post OVBCMAt treatment in accordance with our animal safety guidelines. For in vivo studies with mice bearing MDA-MB-468-BCMAt tumors as BCMAt+ controls, treatment with PBMCs and TCE coincided with the same schedule as mentioned above, without OV treatment. For in vivo T cell trafficking studies, mice were engrafted subcutaneously with either MDA-MB-468 and treated with OVBCMAt. Two days post OVBCMAt treatment, firefly luciferase (ffluc)-expressing T cells were thawed, washed, and prepared in PBS (pH 7.4) for intravenous tail vein injection (5 x 106cells per mouse). TCE treatment followed as previously described. ffluc-T cell trafficking was monitored 2-3 times a week by noninvasive optical imaging (LagoX). Mice were imaged after intraperitoneal Attorney Docket No.40056-0104WO1 injection of 150 to 250 uL of d-luciferin potassium salt (PerkinElmer) suspended in PBS (pH 7.4, 4.29 mg per mouse). Flux was then analyzed with Living Image software (Aura). Statistical analysis Data are presented as means ± SEM, unless otherwise stated. Statistical comparisons between groups were performed using the unpaired two-tailed Student’s t test to calculate P value, unless otherwise stated. Statistical comparison of Kaplan-Meier survival data was performed using the log-rank (Mantel-Cox) test. Example 1: Development of a novel target for delivery by OV to be combined with Teclistamab, an FDA approved BCMA-TCE To expand on potential targets that can be used within this combinatorial strategy, we developed a novel oncolytic chimeric orthopoxvirus expressing a truncated BCMA target (BCMAt) under the control of a synthetic early promoter that allowed for immediate surface target expression. This version was inserted into the J2R locus encoding thymidine kinase (tk) (FIG.1A). The novel oncolytic virus containing BCMAt (OVBCMAt; also called CF33-BCMAt) was sequenced as described above. The OVBCMAt sequence comprises 194,902 bp, including ITR regions (Inverted Terminal Repeat; 1 bp - 6,816 bp at 5’ end and 188,074 bp - 194,902 bp at 3’ end; FIGS. 5-6AF). In the de novo assembly using Canu, the CCS reads from the sample CF33- BCMAt were concatenated first, and the assembly was repeated by several times using different parameters to generate the best contig. The OVBCMAt generated high-quality reads, with over 29 billion bases and >300 long reads in the assembly. Genome annotation of OVBMCAt (called “CF33-BCMAt contig”) is shown in FIGS.5 & 6A-6AF). the variants, the JR2 remnants located at 80,396 bp - 80,475 bp (80 bp) and 80,807 bp - 80,860 bp (54 bp), the ITRs, and BCMAt located at 80,528 bp – 80,773 bp are also highlighted and identified in the annotated genome map (FIGS.5, 6A- 6AF). The genome annotation shows the 275 open reading frames (ORFs; see Table 4), which could be protein-coding genes; the ORFs in FIG.5 are highlighted in green (+ strand) and orange (- strand). Moreover, 121 of 275 ORFs got significant hits in NCBI nr Attorney Docket No.40056-0104WO1 database indicating that at least some of the ORFs, if not all, are protein-coding genes (Table 5). Experiments were conducted to determine the ability of OVBCMAt to infect tumor cells. We demonstrated the ability of OVBCMAt to effectively deliver and generate cell surface expression of BCMAt on multiple solid tumor cell lines (FIG.1B). To evaluate the anti-tumor activity of OVBCMAt in combination with BCMA-CAR T cells in vivo, we treated NSG mice bearing subcutaneous MDA-MB-468 tumors with a single intratumoral injection of 106plaque-forming units (pfu) OVBCMAt. Seven days after OVBCMAt treatment, tumors were harvested and demonstrated high expression of BCMAt (FIG.2A). Therefore, mice were systemically treated with BCMA-CAR T cells on day 7 following OVBCMAt treatment and tumor volumes were monitored. Mice treated with OVBCMAt alone delayed tumor growth was expected, but there was an observed marked tumor regression with the combination of OVBCMAt and BCMA-CAR T cells (FIG.2B). Using OVBCMAt, we next assessed whether BCMAt delivered to tumors activated BCMA-CAR T cells or non-targeting T cells in the presence of Teclistamab (BCMA-TCE). MDA-MB-468 triple negative breast cancer tumor cells were infected with varying MOIs of OVBCMAt, and BCMA-TCE was added at a concentration of 100 ug / mL. These tumor cells were then co-cultured with BCMA-CAR T cells or non- targeting T cells at an effector:target (E:T) ratio of 1:1 for 24h. Cell surface expression of 4-1BB (CD137) was used as markers of T cell activation and quantified via flow cytometry. At 24h, BCMA-CAR T cells and non-targeting T cells in combination with BCMA-TCE demonstrated activation against OVBCMAt infected tumor cells in an MOI- dependent manner compared with OVBCMAt and non-targeting T cells in the absence of BCMA-TCE (FIG.1C). To further quantify the T cell activation in the presence of BCMA-TCE, supernatants from co-cultures were collected to evaluate T cell dependent cytokine production. At 24h, IFNγ and IL-2 secretion were detected in an MOI- dependent manner (FIGS.4A-4B). We quantified killing of tumor cells when co-cultured with OVBCMAt and BMCA-CAR T cells or non-targeting T cells with BCMA-TCE using flow cytometry. At 24h, we observed enhanced killing of tumor cells infected with OVBCMAt and co-cultured with non-targeting T cells in the presence of BCMA-TCE Attorney Docket No.40056-0104WO1 (FIG.1C). In addition, we validated the ability of BCMA-TCE to specifically redirect non-targeting T cells to BCMAt expressing tumor cells following OVBCMAt expression and found that the percent BCMAt expression was significantly reduced in wells with Teclistamab (FIG.1C). Additionally, we tested this combination in vitro against two other solid tumor cell lines including SNU16 (gastric) and OV90 (ovarian). Following 24h co-culture, we demonstrated enhanced activation, tumor cell killing, and BCMAt targeting in the presence of BCMA-TCE similar to BCMA-CAR T cells (FIGS.1D-1E). Example 2: Anti-tumor efficacy with the combination of OV and TCE in human solid tumor xenograft models To evaluate the anti-tumor activity of OVBCMAt in combination with BCME- TCE in vivo, we treated NSG mice bearing subcutaneous MDA-MB-468 tumors with a single intratumoral injection of 106pfu OVBCMAt as previously described

[0013] . MDA- MB-468 tumor-bearing NSG mice (5x106cells on day 0) treated with intratumoral (IT) OVBCMAt (1x106pfu) on day 38, engrafted with intravenous (IV) PBMC (1x107cells) on day 40, and treated with IV BCMA-TCE (25 ug / dose, 8 times) on days 41-43 and 46- 50 (FIG.3A). The MDA-MB-468 tumor-bearing mice treated with PBMCs alone or PBMCs and BCME-TCE showed no tumor control. Notably, mice treated with OVBCMAt and PBMCs or OVBCMAt and BCMA-TCE slowed tumor growth as expected with OVBCMAt alone, but we observed marked tumor regression with the combination of OVBCMAt, PBMCs, and BCMA-TCE (FIGS.3A-3C). These studies highlight the therapeutic efficacy of combining OV and TCE in preclinical models. We previously developed a novel combination therapy for solid tumors by delivering a truncated CD19 antigen with an oncolytic virus (OV) followed by CD19- CAR T cells to mitigate antigen heterogeneity and elicit an immunologically warm TME

[0013] . In the present application, amongst other things, we now demonstrate the ability of OV to deliver truncated BCMA to solid tumors to be targeted with bispecific T cell engagers (TCE) to induce endogenous T cell activation and anti-tumor responses. The current findings support a fully off-the-shelf therapeutic combination with immediate clinical applications. Further, we demonstrated that this paradigm can be advanced with a Attorney Docket No.40056-0104WO1 clinically active TCE (Teclistamab), with the prospect of targeting additional tumor antigens that may be exploited for this combinatorial immunotherapy strategy. In some instances, using a TCE rather than a CAR T cell carries several key advantages. Given the length of time required to generate patient-specific BCMA-CAR T cells, we reasoned that the availability of off-the-shelf immunotherapies overcomes time restraints for patients undergoing treatment. With current manufacturing practices and capacities, the demand for CAR T cells exceeds supply and is still viewed as a niche technology that not all sites can perform

[0017] . Moreover, TCEs such as blinatumomab (a TCE targeting CD19) or Teclistamab provide a safety advantage over CAR T cells due to the nature of their short in vivo half-life and dosing strategies [18, 19]. This treatment can then be suspended or delayed if needed, with the potential for reversing unfavorable immune-related adverse effects. In summary, we have successfully developed a clinically viable, tumor-agnostic, combinatorial immunotherapy using an OV to deliver TCE targets for the off-the-shelf treatment of solid tumors. REFERENCES 1. Huehls, A.M., T.A. Coupet, and C.L. Sentman, Bispecific T-cell engagers for cancer immunotherapy. Immunol Cell Biol, 2015.93(3): p.290-6. 2. Goebeler, M.E. and R.C. Bargou, T cell-engaging therapies - BiTEs and beyond. Nat Rev Clin Oncol, 2020.17(7): p.418-434. 3. Kantarjian, H., et al., Blinatumomab versus Chemotherapy for Advanced Acute Lymphoblastic Leukemia. N Engl J Med, 2017.376(9): p.836-847. 4. 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Clin Cancer Res, 2018.24(1): p.95-105. 23. Priceman, S.J., et al., Co-stimulatory signaling determines tumor antigen sensitivity and persistence of CAR T cells targeting PSCA+ metastatic prostate cancer. Oncoimmunology, 2018.7(2): p. e1380764. 24. Voynov, V., et. al., Discovery Strategies to Maximize the Clinical Potential of T- Cell Engaging Antibodies for the Treatment of Solid Tumors. Antibodies (Basel), 2020 Dec.9(4): p.65. 25. Laurent et al., Nat Commun.2015; 6:7333. Table 4: OVBCMAt Open Read Frames (ORFs) and Corresponding Sequences (the nucleotide sequences for the identified coding regions of OVBCMAt, ORF1- ORF275, coincide with SEQ ID NOs: X1-X275, respectively; the amino acid sequences below coincide with SEQ ID NOs: Z1-Z275, respectively) >ORF1:4294:4422 MRDVRPEYWMGLDVAVFLFFATSDVDRHLTVFPSADSEMDLI >ORF2:5215:5298 MDSLRPVVVVRVHDVSLTGYRLISTSI >ORF3:7198:7296 MTTGDIILTLEGKSSSRIKAYLIQANNGSGYR >ORF4:7405:7500 MAVLIIERDVVTLAPYSNNRFANCILLTSTA >ORF5:8227:8319 MRRYIVMKRVLTHITVVHTGTKYVTGAVTF >ORF6:11722:11835 MVYVDLRTIYHRKVSHKYSCNGRCFCILLINIYKRRM Attorney Docket No.40056-0104WO1 >ORF7:12151:12321 MYILQVILGTHHHINTGNYILRNIKLVCICKMFRKWIFPHCFKMDGANNCHTSING >ORF8:13627:13716 MTRSLNRLCDARLLRLSSLRIIFMLVILL >ORF9:14368:14478 MYLSNSDFFSHVCVDTSLVIGDMCSASSTSDTLSIL >ORF10:15283:15378 MDFPIQSVHRQSIMTLTQQCMLYWQVLLSLR >ORF11:17194:17313 MIITYFEIRIKSQQHFSHMNIITHFNTKIQMEWCITTII >ORF12:17332:17439 MLYKQRNNSLGLFYRYRFSTLTWFINVCETQIIIM >ORF13:20443:20589 MISVQSLTSSHGIFFTSSRMSMNTDSASSLKERSVEYNCPAHCLLRYA >ORF14:21178:21291 MDSNPSILSGRMTIILVSPTYGSSMIEKLPNDSFTDA >ORF15:21763:21846 MNTFSPFIEDAISLKISIVIDIGRVAR >ORF16:23470:23589 MSSFSILLTTIVLLELFMNNPPVTKIVLLTETADTLLFL >ORF17:23659:23832 MNTAISSFGIEIFGNYTQPYFQSPCFLFSLLTSSNRHGVDDRGEQKDYNQGPHLENG >ORF18:23863:23985 MQFYFVFVSLIKISYEYLVKLSMLRKVVTSFDVLPRNLVK >ORF19:24364:24465 MYKLIWSSYSVNVTVGGPIFTSTHSPVQYSSTL >ORF20:25102:25227 MESNPTSHDSVIIEIVYSLKFNTNSLLSSVYEFSILSTPSI >ORF21:26653:26784 MAYHIIQRHNQKLCTFSCMDFRISIYLFRRQHLDPKNDIPDHM >ORF22:27178:27315 Attorney Docket No.40056-0104WO1 MILRTRLPYTSRLVHFTKEGCLPYLIKVLMSLIQKTNWNTVLFFI >ORF23:27325:27405 MISISSKHFKIYHLYCCSDCTSIRVS >ORF24:28375:28485 MDDDNLRLCINDPFLLIFNTLSRKKIIIFVLASSIE >ORF25:29101:29205 MNRHVYLMSSFFSQKCTTQSLLICFSISFSISLR >ORF26:29257:29391 MNKYPPFVLVKDESIKGSCCRIRVLSCLAETDVCLTINRITKFD >ORF27:29638:29925 MRMHITAFFTIHNIKMIIYNRPHMAYSFQTFHEYIIHAVFLRGGYLDGAADIVEERFSVSFSPSLTFTRF GICSTAPFLNLILIISFPCTSTAVT >ORF28:32092:32229 MAVFPEPDGPLNMIDFTIPDIYVSQKSRLCSLFCIYVNVYYIYNM >ORF29:33664:33795 MTYINPFNIATPISHFGSRILAYFCQYGFDGFHLSILDVNDES >ORF30:33820:33945 MYSSSASPPQLERGYFSSGISYIQEFVHVLYAITFELLYGD >ORF31:34060:34176 MEILSCELLIPIDINSMLWYLGNDSSKNAILFKNVIHS >ORF32:34297:34485 MRISGAKSSFFIFNISSLKIFIIDSSVKYLKFSSLMSLKIFRNIVLNDADSIFLLLYLSAYM >ORF33:34522:34626 MYFSHSVMADPICKKSAVERIYFTLSLVRLKGIP >ORF34:35407:35574 MTSIRIIGDCGICMRWAAFTFCVIVTITSNLGKFSRWTPITTLIMPLIKIFSLVT >ORF35:37261:37338 MNLTPRMHTICLMRLIVHRHLYPFL >ORF36:38398:38601 MSVISNPSKYKQSNTNKHMLEFLYSFFLCIPKLPNGSGTLCSSTRTISESNTIDVAFLNAFGMYSLR >ORF37:38767:38874 Attorney Docket No.40056-0104WO1 MGLIGVITEIDIESRFCLDAFSIISFKLLDFLNTS >ORF38:39073:39174 MLLSRGRISVFSLKKVLIVSPIYPYPKSCSISS >ORF39:39265:39342 MIKYLSSLSVIKSLINLDFSLYPDA >ORF40:39832:39924 MRVRYAYRTRIRVLIPSCQSNMLHPFITLY >ORF41:41569:41886 MLSVCPRRYLHRLYRSLDSSDIGILSDICSANAIHLYFLFVNSQCLDTRLDRATTILESQHIISFTKLTK SNSPESESTLSFSLNNRSMSPYCLIAKSSSVINAE >ORF42:42517:42594 MDWFKVNNSSDIIVVYYTNSHYLVK >ORF43:42613:42693 MSGSNGRVRGYWWCRISRQVYSKTVN >ORF44:44416:44514 MEYADYILYLLHYRSYQNTNAHNIIPHPLNEI >ORF45:44521:44631 MSCMPIPALLTSSIWILSISSSSFKIDTTYEYYFLF >ORF46:44875:44958 MRGIISPGLILANVLLGIAARTFFVVL >ORF47:44965:45075 MAASSNLLFFEISSIILCHSAIVIYYICFLIRHLLE >ORF48:46225:46308 MDTFIIIAYPVSRTIFSNICIFYRFIY >ORF49:47185:47274 MLLVNHLLELRYPPCINHNHMVRQIFSIV >ORF50:48172:48270 MRSIFVLSVNVYSPAYYWIVDDDVTIYISYNY >ORF51:48304:48393 MRCTPHYLLSIGRIHFNGFGFGIEFKGMC >ORF52:48499:48660 Attorney Docket No.40056-0104WO1 MCIIPRASRRGRGTRNYCYFIIILDLILILFIRFFASSFISRYTTEFHKKRRE >ORF53:48775:49026 MLIFILSILPYNICSLIGTELYDCIFLYTKSNGCSRLQTCIKVSCSMLEFMYLAEDIPIQFDGIGNCLLS MVIMEYHLLFANI >ORF54:49123:49245 MSFVNDVTNRLLGISALTTNMVVGPLLTTTHLLSGDMITA >ORF55:49249:49350 MGKVRIFLPLTSLSIEITHPPTELIQSIIVDNL >ORF56:49906:49998, partial MCSVLGAITLDSLSHIKLPAKLSSSNISFLE >ORF57:4121:4282 MSEVSSVAPSDADPSTYLTSSSDDSLHMSPIRTLNSRFLTHFVSTIVEPMISS >ORF58:4301:4417 MLDPSTGWVLMSLSFSSSLHLMSIDTSQSFHQRILRWI >ORF59:5012:5110 MIVSFFAFVNCLEEESLLLHLISKFRVHTFLL >ORF60:5537:5635 MTRPLIGSRLVSFLRSNRRRERHLVEQRFNHR >ORF61:5759:5854 MRQHCCYNFERRYYSIRLSECRTYLVDTVVY >ORF62:5969:6067 MMGVQSRLLRILVSAPRDKRAYTTRGLCLVYC >ORF63:6572:6784 MRRCIHIKERKIHMTNIVDRNVTFILTVVHKYVRYVPHTVANDAYNLVHLIMIYFFIIKDVKEKQNNIFF >ORF64:8132:8218 MGKDPPSSLPWMETLLLIKHLITSLDRD >ORF65:8876:9016 MMKAIIPHKMIKSVVREHEGDLVFSSADMIQEGEIVVLVQNLSQHK >ORF66:9263:9436 MGPSMRNPQDVFSQTMSDVGHGIQGVLSSVAMTGSELGTRRGHCKGRPVAVYANRGL >ORF67:12047:12223 Attorney Docket No.40056-0104WO1 MLYIPSMSSGSIITILEFPSYGISIIENPPNNSLICTYCKLFSVPTIISTLVTIFLEI >ORF68:12314:12424 MDSGLVNKELILPFVIVLTHSLISSFVWLALLKFTV >ORF69:12533:12631 MSLLSSFLSSGVFSFIFSIYFDSCSAVEPAAP >ORF70:13256:13435 MSHTTYISSLCETTPGFIVPVQKLGNVFHILLTVLYLITLFEIFVSSSISMLFTVCTDV >ORF71:13886:13963 MEFAFVYLHLVRLYHFRYTLITSCN >ORF72:15719:15820 MRSNYTLNTVTILCSYGTQIPTVTEFRCIVGYP >ORF73:16133:16216 MYHHFHRHLYYTALKYLYNISFFTHIA >ORF74:16280:16393 MYNISYIISEGSNVSRQFLSVKTGNSLSYTFDTYISL >ORF75:16817:16918 MVYGEFSLLSIMSCVACLLLSVNAFISPLIRIR >ORF76:18092:19114 MSRKFMQVYEYDREQYLDEFIEDRYNDSFITSPEYYSAEKYMCRYTTLNHNCINVRRCALDSKLLHDIIT NCKIYNNIELVRATKFVYYLDLIKCNWVSKVGDSVLYPVIFITHTSTRNLDKVSVKTYKGVKVKKLNRCA DHAIVINPFVKFKLTLPNKTSHAKVLVTFCKLRTDITQIEAPLSGNVLVYTFPDINKRIPGYIHVNIEGC IDGMIYINSSKFACVLKLHRSMYRIPPFPIDICSCCSQYTNDDIEIPIHDLIKDVAIFKNKETVYYLKLN NKTIARFTYFNNIDTAITQEHEYVKIALGIVCKLMINNMHSIVGVNHSNTFVNCLLEDNV >ORF77:19652:19777 MSAPYNICVYVTSNKCINIGTYHFASRSLIYYLWIRDKIYI >ORF78:22949:23080 MFLLFSISTFFSISSFSLSISFMISSTFVTSVSMLVVSNKTIG >ORF79:23777:23893 MIEGNRRTIIRDLILKMVRAYKGVNQCIICSFISFLYH >ORF80:24398:24484 MLQSVVQFLLRRIVPYNTLPLYNRLVQI Attorney Docket No.40056-0104WO1 >ORF81:25478:25567 MYIPSSLKALLYLSLARIIDTLLIISYIS >ORF82:25607:25822 MNSIPVPTLTETSRSFIIIPLSVSITHCLTRDSFGIVRTISSNGITAHLVNSLYILCNMALLLPYTINLL L >ORF83:28136:28255 MILILISYSDIYIYVIMYNRNCLLHLYKIHDLLKYIYRY >ORF84:28577:28690 MFERDYNPVLYGMWKNWNTRVLYNEEINIHSSQVFPF >ORF85:31724:31819 MNLIIRFSVSTTKLGLNHFKRGRSYIHRVRH >ORF86:32000:32131 MVIDTFSFHRTRKSSGMGHHKSKYIPIVFWLWLSFLNQMVRSI >ORF87:32576:32683 MIFYIISNWFRSRDFEYRRAIKIIYILWFLRTSFW >ORF88:33776:33853 MSTMNPDRVCRLYNKCIRHQPVPHN >ORF89:36644:36745 MFFISCLKKLSRGYTVNVVAIASSPGNVVSISY >ORF90:40496:40675 MMFIHCVVFPDLSNPSKTINAPRDIFVNLTYFLQFMRIIKLKINIWSSETIRSTFIDHG >ORF91:42626:43666 MAVYAVTGGAGFLGRYIVKLLISADDVQEIRVIDIVEDPQPITSKVKVINYIQCDINDFDKVREALDGVN LIIHTAALVDVFGKYTDNEIMKVNYYGTQTILAACVDLGIKYLIYTSSMEAIGPNKHGDPFIGHEHTLYD ISPGHVYAKSKRMAEQLVMKANNSVIMNGAKLYTCCLRPTGIYGEGDKLTKVFYEQCKQHGNIMYRTVDD DAVHSRVYVGNAAWMHVLAAKYIQYPGSKIKGNAYFCYDYSPSCSYDMFNLLLMKPLGIEQGSRIPRWML KMYACKNDMKRILFRKPSLLNNYTLKISNTTFEVRTNNAELDFNYSPIFNVDVAFERTRKWLEESE >ORF92:45194:45853 MYSLLFIILMCIPFSFQTVYDDKSVCDSDNKEYMGIEVYVEATLDEHLRQTTCESEIHKYGASVSNGGLN ISVDLLNCFLNFHTVGVYTNRDTVYAKFASLDPWTTEPINSMTHDDLVKLTEECIVDIYLKCEVDKTKDF MKTNGNRLKPRDFKTVPPSDVGSMIELQSDYCVNDVTAYVKIYDECGNIKQHSIPTLRDYFTTKNGQPRK Attorney Docket No.40056-0104WO1 ILKKKFDNC >ORF93:47663:48496 MSRVRISLIYLYTLVVITTTKTIEYTACNDTIIIPCTIDNPTKYIRWKLDNHDILTYNKTSKTTILSKWH TSARLHSLSDSDVSLIMEYKDILPGTYTCGDNTGIKSTVKLVQLHTNWFNDYQTMLMFIFTGITLFLLFL EITYTSISVVFSTNLGILQVFGCVIAMIELCGAFLFYPSMFTLRHIIGLLMMTLPSIFLIITKVFSFWLL CKLSCAVHLIIYYQLAGYILTVLGLGLSLKECVDGTLLLSGLGTIMVSEHFSLLFLVCFPSTQRDYY >ORF94:2094:2210 MTPLKRERENENENKNILVTPSERGLIFFMRPSKRERE >ORF95:5658:5762 MMSFTTSALYMMFLFSNTKSNTVFSRKVDVVSDV >ORF96:6948:7115 MGNFEIKLSSVLMLSTMESILSLFFTVSVMMDVSSFLYHLMSDSLRISICGVCFV >ORF97:8598:8678 MLLAELILRCFYKVSRLRERVTVEQS >ORF98:9081:9242 MIARSSSAVFMESFLMKHLMISTQLSILSHGSESFNSPPKSSVASVLKEMRSL >ORF99:9417:9506 MLIEGFNFHFFNGLWMRNESDIILRYVVM >ORF100:9591:9668 MTFSHKWTYRCRSNEEKYYLYHLHN >ORF101:9900:9992 MIQILHSLDNSVTESYLLLVCLYHSILQTV >ORF102:10554:10649 MLQLNVMIQRSFSYACFITPRTCRSKIYSQR >ORF103:11439:11540 MDEVTNIRHAINPYIIILILLIITICLIFSLYY >ORF104:12771:12884 MLNFSLCLYPVFILNKLVLRTQSIILHTINNASIKNR >ORF105:13503:13586 MLYSAMKWCTSFKVTIDIESIQRSNNI >ORF106:14493:14618 Attorney Docket No.40056-0104WO1 MVVFVYIIYALLSYTVYAIIMFLPYIPPSYVRLSSIYYFIN >ORF107:18117:18236 MNMTESNISMSSLKTDITIVLSLVQNTIVRKNTCVDILH >ORF108:19191:19298 MLGIVNAIHVNVVASSSLTGLMFNRDVITRLLSVI >ORF109:19452:19568 MPSGNCIVEGIILSRTSNFTILVTLYVLPLYIYSKTHV >ORF110:19599:19826 MVIIPGVRCLSLLFLRRRCPLHIISAFTLLAINALILGHTISPVDLSFTICGYEIRSIFDSETDTIVKFN DIMSQ >ORF111:20241:20516 MYNSSIHTPEYDVIIHVIEHLKHHKQCVQTVTSGMVFTSPVSSSICTKSDDGRNLSDGFLLIRYITTDDF CTIFDIIPRHIFYQLANVDEH >ORF112:22110:22217 MEVCHRTILSCNIPTFLNLLVLKLLLQDDCLHTYN >ORF113:24357:24437 MLDVQIDMVVVFSQCYSRWSNFYFDA >ORF114:26223:26375 MGFHLPSIHVDDGDPVSIKPLLQLRCITPPIENVDPEINPLDRDGISHFC >ORF115:26415:26501 MYEAPITSYPTSQLIVIYSPNEYFSLTG >ORF116:29145:29294 MHNTKSFDMLFYIILYQSEVVVTHRESKYFVCIIINSNEQISTLCVGKR >ORF117:29634:29717 MNAYAHNSILYHSQYQNDHIQQTTYGV >ORF118:30021:30101 MLNFSIYSVSCFKYVMMNPYSFQTQV >ORF119:30378:30521 MKILVVPTESVCVKHRHDFGCTHEINNKLSYFLIFIDKNFTSTKHHT >ORF120:30597:30920 MVIYCSNSLGAYCKLVINKVAVLLTYFCFVALTNAQFFVSDILVHGKIPPNHLIIQYPSVSRSPRLDTTY Attorney Docket No.40056-0104WO1 PLCESIGVNSRVPLSILFGFLINGTCSPLDMNLETNP >ORF121:31017:31205 MVFKISIPINITDLFGNLLLLALITASRSAPNLLITKNRYSTLMDLYRPNALHVIRPTCFIL >ORF122:34044:34130 MIVAVYGNLIMRITYTDRYQLDAMVSRK >ORF123:35571:35894 MTRWWRSRYICRSQCSNVKNSTCSQQILYIHLLILSYTTITKSFFKTLNHHQKSMFKVIRLKYIFEINSC ISYPSILDLYIFEINSCISHPSILDLYVLKNTILLIL >ORF124:35952:36092 MYFFNYYRKNNKYGIQPYIFLLSLTFYDISTYTSLFCSIDFILSSM >ORF125:36777:36923 MSGSYFPNILDPNSPTSGKFIIIQCLFISHDDPLSISSLSRILICGSK >ORF126:37290:37376 MSDEINSSQTSLSFPIDMITGITSLGLK >ORF127:37761:37871 MSRFFPRFILSYPSKSRKSNGYSICGMGLGRCKLCS >ORF128:38517:38717 MFVYKNNFRIQYDRRSFFKCFRYVFFEIIHFMREYWFHVSTKEGKLVIIFMNLYSFTIVFDFRKHS >ORF129:40668:41402 MGNKNIKPSKENRLSILSKDKMDSFKRGSWATSSFKEKSRATIQRFSSLRREHIKVDHPDKFLELKRGIY EIIQKSSSIDVDKRTKLMSNIKTMMINPFMIEGLMTSLENLDPDNKMSYSSVMILGEFDIINISDNEAAF EFINSLLKSLLLLNTRQLKLLEYSISNDLLYAHINALEYIIKNTFNVPERQLILRGQYLTPIFSDLLKYA GLTIKSNILMWNKQFIKPVSDLYTSIRLLYCVTV >ORF130:43026:43103 MSIPFMIYHQDMYTQKVNVWPSNWL >ORF131:43287:43415 MLHGCTCWLQNISSIRDLRLKEMLTFATITLHRVRTICLIFY >ORF132:44094:44183 MSLYLSFISLYHIIESYPIIVIHVDRCRE >ORF133:44235:44345 MRHDTFTEHCISLYFKFPDNETIKLGLSEPYLCFKK Attorney Docket No.40056-0104WO1 >ORF134:44730:44810 MSSRYNDRRYRGVPSKQLHSIRVLIH >ORF135:45015:45113 MPFSHCYLLYMFFNKTSIGINLTLAFYSYYKI >ORF136:45969:46073 MQFGSIRCTTNIFPFFSSILRGIFSYKIIWGCLV >ORF137:46281:46358 MHLLSFYLLMVYELIYVLQLLIVSL >ORF138:46623:46892 MKYILYSRCSFSFSFISNHLTPDGPSKIGWLDKGFIISSSTLYFSMTSNVVCGTTFPAGKHIPGAGDGNC FVYPSNFDVEKDCLMVFIE >ORF139:48726:48863 MINDPHTRNLLIHRNTNAHIYIINSTVQYLFLDRYRIVRLHFFVY >ORF140:49461:49598 MFCIYIISTVIISNKIANFRNAEYREYLHLYNVTAAIILNITSIL >ORF141:49641:49742 MILFLLIKIIIAMCSSKRIILTKFIVEFCNERI >ORF142:49928:49611 MAPSTEHIYDSVAGSTLLINNDRNEQTIYQNTTVVLNEDTKQNPNYSSNPFVNYNKTSICSKSNPFITEL NNKFSENNPFRRAHSDDYLNKQEQDHEHDDIESLV >ORF143:49547:48756 MEIFPVFGISKISNFIANNDCRYYIDTEHQKIISDEINRQMDETVLLTNILSVEVVNDNEMYHLIPHRLS TIILCISSVGGCVISIDNDVNGKNILTFPIDHAVIISPLSKCVVVSKGPTTILVVKADIPSKRLVTSFTN DILYVNNLSLINYLPLSVFIIRRVTDYLDRHICDQIFANNKWYSIITIDNKQFPIPSNCIGMSSAKYINS SIEQDTLIHVCNLEHPFDLVYKKMQSYNSVPIKEQILYGRIDNINMSISISVD >ORF144:45728:45651 MQSHRLRNSQTVVLSCFLHQKEEQF >ORF145:45029:44628 MAEWHKIIEDISKNNKFEDAAIVDYKTTKNVLAAIPNRTFAKINPGEIIPLITNRNILKPLIGQKYCIVY TNSLMDENTYAMELLTGYAPVSPIVIARTHTALIFLMGKPTTSRRDVYRTCRDHATRVRATGN >ORF146:42212:41490 Attorney Docket No.40056-0104WO1 MAFDISVNASKTINALVYFSTQQNKLVIRNEVNDTHYTVEFDRDKVVDTFISYNRHNDTIEIRGVLPEET NIGCAVNTPVSMTYLYNKYSFKLILAEYIRHRNTISGNIYSALMTLDDLAIKQYGDIDLLFNEKLKVDSD SGLFDFVNFVKDMICCDSRIVVALSSLVSKHWELTNKKYRCMALAEHISDSIPISELSRLRYNLCKYLRG HTESIEDEFDYFEDDDSSTCSAVTDRETDV >ORF147:39386:37728 MTSLREFRKLCCDIYHASGYKEKSKLIRDFITDRDDKYLIIKLLLPGLDDRIYNMNDKQIIKLYSIIFKQ SQEDMLQDLGYGYIGDTIRTFFKENTEIRPRDKSILTLEEVDSFLTTLSSVTKESHQIKLLTDVASVCTC NDLKCVVMLIDKDLKIKAGPRYVLNAISPHAYDVFRKSNNLKEIIENASKQNLDSISISVMTPINPMLAE SCDSVNKAFKKFPSGMFAEVKYDGERVQVHKNNNEFAFFSRNMKPVLSHKVDYLKEYIPKAFKKATSIVL DSEIVLVDEHNVPLPFGSLGIHKKKEYKNSNMCLFVFDCLYFDGFDMTDIPLYERRSFLKDVMVEIPNRI VFSELTNISNESQLTDVLDDALTRKLEGLVLKDINGVYEPGKRRWLKIKRDYLNEGSMADSADLVVLGAY YGKGAKGGIMAVFLMGCYDDESGKWKTVTKCSGHDDNTLRELQDQLKMIKINKDPKKIPEWLVVNKIYIP DFVVEDPKQSQIWEISGAEFTSSKSHTANGISIRFPRFTRIREDKTWKESTHLNDLVNLTKS >ORF148:37280:37185 MRGVKFISRSHSSHECFLFYQRKCLVDYSPV >ORF149:35663:35367 MDIKNLLTACTIFYITTLATADIPTPPPTGHVTRENILIRGIINVVIGVHLENLPRLDVMVTITQNVNAA HLIHIPQSPIILMDVINVENAQPDHLIR >ORF150:35231:35052 MNKEILFVNRAVLVNIATTYVIIDLIHFLHANYLNVINYDFDDNVTIHYIATWLVYYSV >ORF151:34862:33168 MNSSSKLIAVINGFRNSGRFCDINIVINDERINAHRLILSGASEYFSILFSNNFIDSNEYEVNLSHLDYQ SVNDLIDYIYGIPLSLTNDNVKYILSTADFLQIGSAITECEKYILKNLCSRNCIDFYIYADKYNNKKIES ASFNTILRNILRLINDENFKYLTEESMIKILSDDMLNIKNEDFAPLILIKWLESTQQSCTVELLRCLRIS LLSPQVIKSLYSHQLVSSIYECITFLNNIAFLDESFPRYHSIELISIGISNSHDKISINCYNHKKNTWEM ISSRRYRCSFAVAVLDNIIYMMGGYDQSPYRSSKVIAYNTCTNSWIYDIPELKYPRSNCGGLADDEYIYC IGGIRDQDSSLTSSIDRWKPSKPYWQKYAKMREPKCDMGVAMLNGLIYVMGGIVKGDTCTDALESLSEDG WMKHQRLPIKMSNMSTIVHDGKIYISGGYNNSSVVNVISNLVLSYNPIYDEWTKLSSLNIPRINPALWSA HNKLYVGGGISDDVRTNTSETYDKEKDCWTLDNGHVLPRNYIMYKCEPIKHKYPLEKTQYTNDFLKYLES FIGS >ORF152:32153:32040 Attorney Docket No.40056-0104WO1 MSGIVKSIILSGPSGSGKTAIAKRLWEYIWICGVPYH >ORF153:30428:29769 MAMFYAHALGGYDENLHAFPGISSTVANDVRKYSVVSVYNNKYDIVKDKYMWCYSQVNKRYIGALLPMFE CNEYLQIGDPIHDQEGNQISIITYRHKNYYALSGIGYESLDLCLEGVGIHHHVLETGNAVYGKVQHDYST IKEKAKEMNALSSGPIIDYHVWIGDCICQVTAVDVHGKEIMRMRFKKGAVLQIPNLVKVKLGENDTENLS STISAAPSR >ORF154:28700:27024 MDFFKKEILDWSVYLSLHYIARVCSNSSTSHIIQDYNLVRTYEKVDKTIVDFLSRLPNLFHILEYGENIL HIYSMDDANTNIIIFFLDRVLNINKNGSFIHNLRLSSSINIKEYVYQLVNNDHPDNRIRLMLENGRRTRH FLSYISDTVNIYICILINHGFYIDAEDSYGCTLLHRCIYHYKKSESESYNELIKILLNNGSDVDKKDTYG NTPFILLCKHDINNVELFEICLENANIDSVDFNRYTPLHYVSCRNKYDFVKLLISKGANVNARNKFGTTP FYCGIIHGISLIKLYLESDTELEIDNEHIVRHLIIFDAVESLDYLLSRGVIDINYRTIYNETSIYDAVSY NAYNTLVYLLNRNGDFETITTSGCTCISEAVANNNKIIMEVLLSKRPSLKIMIQSMIAITKNKQHNADLL KMCIKYTACMTDYDTLIDVQSLQQYKWYILKCFDEIDIMKRCYIKNKTVFQLVFCIKDINTLMRYGKHPS FVKCTSLDVYGSRVRNIIASIRYRQRLISLLSKKLDAGDKWSCFPNEIKYKILENFNDNELSTYLKIL >ORF155:25868:25722 MLISTMPLEHFYSGTIITRDLLCMEEVTPYYIIYTGYLQDAPLYRSMI >ORF156:25325:24777 MYKKLITFLFVIGALASYSNNEYTPFNKLSVKLYIDGVDNIENSYTDDNNELVLNFKEYTISIITESCDV GFDSIDIDVINDYKIIDMYTIDSSTIQRRGHTCRISTKLSCHYDKYPYIHKYDGDEQQYSITAEGKCYKG IKYEISMINDDTLLRKHTLKIGSTYIFDRHGHSNTYYSKYDF >ORF157:24722:23904 MRYIIILAVLFINSIHAKITSYKFESVNFDSKIEWTGDGLYNISLKNYGIKTWQTMYTNVPEGTYDISAF PKNDFVSFWVKFEQGDYKVEEYCTGLCVEVKIGPPTVTLTEYDDHINLYIEHPYATRGSKKIPIYKRGDM CDIYLLYTANFTFGDSKEPVPYDIDDYDCTSTGCSIDFVTTEKVCVTAQGATEGFLEKITPWSSKVCLTP KKSVYTCAIRSKEDVPNFKDKMARVIKRKFNKQSQSYLTKFLGSTSNDVTTFLSMLNLTKYS >ORF158:23621:23121 MDSGIYETPINYKKSNVSAVSVNNTIFVTGGLFINNSNSTIVVNNMEKLDIYKDKQWSIIEMPMARVYHG IDSTFGMLYFAGGLSVTEQYGNLEKNNEISCYNPRTNKWFDISYTIYKISISSLCKLNNVFYVFSKDIGY VEKYDGAWKLVHDRLPAIKALSTSPY >ORF159:22733:22635 Attorney Docket No.40056-0104WO1 MARNGLSEILYILVIQYYIRSEKISLVRSTIT >ORF160:21815:20778 MDIFREIASSMKGENVFISPASISSVLTILYYGANGSTAEQLSKYVETEENTDKVSAQNISFKSMNKVYG RYSAVFKDSFLRKIGDKFQTVDFTDCRTIDAINKCVDIFTEGKINPLLDEPLSPDTCLLAISAVYFKAKW LMPFEKEFTSDYPFYVSPTEMVDVSMMSMYGKAFNHASVKESFGNFSIIELPYVGDTSMMVILPDKIDGL ESIEQNLTDTNFKKWCNSLEATFIDVHIPKFKVTGSYNLVDTLVKSGLTEVFGSTGDYSNMCNSDVSVDA MIHKTYIDVNEEYTEAAAATCALVSDCASTITNEFCVDHPFIYVIRHVDGKILFVGRYCSPTTNC >ORF161:20702:20253 MTANFSTHVFSPQHCGCDRLTSIDDVRQCLTEYIYWSSYAYRNRQCAGQLYSTLLSFRDDAESVFIDIRE LVKNMPWDDVKDCTEIIRCYIPDEQKTIREISAIIGLCAYAATYWGGEDHPTSNSLNALFVMLEMLNYVD YNIIFRRMN >ORF162:20066:19965 MYRQRAIFCIIHGVRKRASNLTMSSNKYAIIRI >ORF163:16682:16584 MTHFTIGTLRIAILKRIDTHFQNTCRLINTMV >ORF164:16415:16320 MRDTLMYIIKICTCQRYMINYFLFSQIKIVY >ORF165:14369:13413 MEMYPRHRYSKHSVFKGFSDKVRKNDLDMNVVKELLSNGASLTIKDSSNKDPITVYFRRTIMNLEMIDII NKHTTIDERKYIVHSYLKNYKNFDYPFFRKLVLTNKHCLNNYYNISDSKYGTPLHILASNKKLITPNYMK LLVYNGNDINARGEDTQMRTPLHKYLCKFVYHNIEYGIRYYNEKIIDAFIELGADLTIPNNDGMIPVVYC IHSNAEYGYNNITNIKIIRKLLNLSRRASHNLFRDRVMHDYISNTYIDLECLDIIRSLDGFDINGYFEGR TPLHCAIQHNFTQIAKYLLDRGADIVVPNTLIIHQYIQ >ORF166:13280:13125 MIYMLYATSKMKKMLRLVYLDITRIRITDGNWLRRQKADYQLCILFFMTIP >ORF167:13109:12978 MNRICYKIHLMCTLANGIICVINIRIVISCTIYYPSTKYNRIK >ORF168:10664:10509 MNLQKLSLAIYLTATCSWCYETCIRKTALYHDIQLEHVEDNKDSVASLPYK >ORF169:9656:9546 MIEVILFFITSASICPLMRKRHLIRCIVKRNLLKSW Attorney Docket No.40056-0104WO1 >ORF170:9542:9420 MKPKVNNIGNTPLHNYVSQYDITLIPHPQPIKKMEIKALY >ORF171:8720:8613 MRYIVTSSINAIQTLRLFDCYSLAESRDFVETTKD >ORF172:7679:7188 MAVNHVSNNGRLCMYGLILSRFNNCGYHCYETILIDVFDILSKYMDNIDMIDNENKTLLYYAVDVNNIQF AKRLLEYGASVTTSRSIINTAIQKSSYRRENKTRIVDLLLSYHPTLETMIDAFNRDIRYLYPEPLFACIR YALILDDDFPSKVSMISPVVIRN >ORF173:6032:5703 MLFYLEEPIRGYVIILIVHPSWNDCATGHILIMLLNWHEQKEEGQHLLYLFIKHNQGYTLNILRYLLDRF DIQKDEYYNTAFQNCNNNVASYIGYDINLPTKDGIRLGV >ORF174:5339:5085 MYDDLKPVPRNTFNYIDVEINLYPVNDTSCTRTTTTGLSESISTSELTITMNHKDCNPVFRDGYFSVLNK VATSGFFTGERCAL >ORF175:4694:4284 MHVPASLQQSSSSCTEEENKHHMGIDVIIKVTKQDQTPTDDKICQSVTEITESESDPDPEVESVEDVDPP TTYYSIIGGGLRMNFGFTKCPQIKSISESADGKTVRCLSTSDVAKKRKTATSRPIQYSGLTSLIRK >ORF176:4169:4068 MSTDRHLKVQPMILHSSIQQNSKRVSESITLFI >ORF177:4061:3939 MSRVNRTIQAHHELKKCTGHYIPVCKTKSYLSRLLLFLSQ >ORF178:3128:2460 MVSLKYFYSHSLFNGVIKYFYSLSLFDGLTKILNLFLMVSLKYFYSHSLFNGVIKYFYSLSLFDGLIKKV LQKYFYSLSLFDGLIKKVLQKYFYSLSLFDGLIKKFYKNIFILFLSLMVSQKYFYSLSLFDGLIKKVLQK YFYSLSLFDGLIKNIKPLSDGVTKIFLFSFSLQWSHKIFLFSFSLRWSHKNIKPLSDGVTKIFLFSFSLQ WSHKIFLFSFSL >ORF179:49378:49289 MTMRCTILFLIDYRRLYSVLVLSEDVLSL >ORF180:47818:47666 MVIQFPSNILCRIIYSTRNNDGIITCCILYGLCSCYNNQRIEVYQRYSNS >ORF181:47089:46457 Attorney Docket No.40056-0104WO1 MCLNDEGGPSSLSSHRWSTFLKVELECDIDGRSYRQIIHSRTIKTDNDTILYVFFDSPYSKSALCTYSMN TIKQSFSTSKLEGYTKQLPSPAPGICLPAGKVVPHTTFEVIEKYNVLDDIIKPLSNQPIFEGPSGVKWFD IKEKENEHREYRIYFIKENSIYSFDTKSKQTRSSQVDARLFSVMVTSKPLFIADIGIGVGMPQMKKILKM >ORF182:46036:45926 MPRRMELKNGNIFVVQRILPNCIRVTLYNNYTTFLS >ORF183:45769:45692 MLFNVSALIVYFDVCSHIVYAIVRL >ORF184:45535:45419 MGHRIYRFRSPWIQTSKLRVYGIAISVYTNCMKIKKTV >ORF185:44683:44603 MCIERVEITLPVYAQLVIKIKSNIHM >ORF186:44590:44006 MMMMKWIISILTMSIMPVLAYSSSIFRFHSEDVELCYGHLYFDRIYNVVNIKYNPHIPYRYNFINRTLTV DELDDNVFFTHGYFLKHKYGSLNPSLIVSLSGNLKYNDIQCSVNVSCLIKNLATSTSTILTSKHKTYSLH RSTCITIIGYDSIIWYKDINDKYNDIYDFTAICMLIASTLIVTIYVFKKIKMNS >ORF187:43267:43154 MHRVIIDCTIHNVTVLLTLLVKDFRQFVSFSVNSSGS >ORF188:43033:42947 MLMADEWITVFIGSYCFHATSIDQILDS >ORF189:41497:41408 MYNFFYSVKDMIKNIIVVFIPFQSPYMIL >ORF190:41209:41021 MIYSNAFMWAYNKSLLMEYSKSFSCLVFNKRRDFNRLFMNSNAASLSLILMMSNSPNIITDE >ORF191:40966:40886 MNGFIIIVFMLDMSLVRLSTSIDDDF >ORF192:40795:40634 MVARDFSLKDDVAQDPLLNESILSLDKMDSLFSLDGLIFLLPMIYKGRPNRLG >ORF193:39907:39419 MDEAYYSGNLESVLGYVSDMHTELASISQLVIAKIETIDNDILNKDIVNFIMCRSNLDNPFISFLDTVYT IIDQEIYQTELINSLDDNEIIDCIVNKFMSFYKDNLENIVDAIITLKYIMNNPDFKTTYAEVLGSRIADI DIKQVIRKNILQLSNDIRERYL Attorney Docket No.40056-0104WO1 >ORF194:37675:36671 MDGVIVYCLNALVKHGEEINHIKNDFMIKPCCERVCEKVKNVHIGGQSKNNTVIADLPYMDNAVSDVCNS LYKKNVSRISRFANLIKIDDDDKTPTGVYNYFKPKDVIPVIISIGKDKDVCELLISSDISCACVELNSYH VAILPMNVSFFTKGNASLIILLFDFSIDAAPLLRSVTDNNVIISRHQRLHDELPSSNWFKFYISIKSDYC SILYMVVDGSVMHAIADNRTHAIISKNILDNTTINDECRCCYFEPQIRILDRDEMLNGSSCDMNRHCIMM NLPDVGEFGSSMLGKYEPDMIKIALSVAGNLIRNRDYIPGRRGYSYYVYGIASR >ORF195:36601:36029 MDIKIDISISGDKFTVTTRRENEERKKYLPLQKEKTTDVIKPDYLEYDDLLDRDEMFTILEEYFMYRGLL GLRIKYGRLFNEIKKFDNDAEEQFGTIEELKQKLRLNSEEGADNFIDYIKVQKQDIVKLTVYDCISMIGL CACVVDVWRNEKLFSRWKYCLRAIKLFINDHMLDKIKSILQNRLVYVEMS >ORF196:33358:33266 MMFELIHLKHTIKKKIVGHWIMVTCYHAII >ORF197:33118:32171 MTRLPILLLLISLVYATPFPQTSKKIGDDATLSCNRNNTNDYVVMSAWYKEPNSIILLAAKSDVLYFDNY TKDKISYDSPYDDLVTTITIKSLTARDAGTYVCAFFMTSTTNDTDKVDYEEYSTELIVNTDSESTIDIIL SGSTHSPETSSEKPEDIDNFNCSSVFEIATPEPITDNVEDHTDTVTYTSDSINTVSASSGESTTDETPEP ITDKEEDHTVTDTVSYTTVSTSSGIVTTKSTTDDADLYDTYNDNDTVPPTTVGGSTTSISNYKTKDFVEI FGITALIILSAVAIFCITYYIYNKRSRKYKTENKV >ORF198:32026:31571 MEREGVDYHYVNREAIWKGIAAGNFLEHTEFLGNIYGTSKTAVNTAAINNRICVMDLNIDGVRSLKNTYL MPYSVYIRPTSLKMVETKLRCRNTEADDEIHRRVMLAKTDMDEAGEAGLFDTIIIEDDVNLAYSKLIQIL QDRIRMYFNTN >ORF199:31420:30518 MNFQGLVLTDNCKNQWVVGPLIGKGGFGSIYTTNDNNYVVKIEPKANGSLFTEQAFYTRVLKPSVIEEWK KSHNIKHVGLITCKAFGLYKSINVEYRFLVINRLGADLDAVIRANNNRLPKRSVMLIGIEILNTIQFMHE QGYSHGDIKASNIVLDQIDKNKLYLVDYGLVSKFMSNGEHVPFIRNPNKMDNGTLEFTPIDSHKGYVVSR RGDLETLGYCMIRWLGGILPWTKISETKNCALVSATKQKYVNNTATLLMTSLQYAPRELLQYITMVNSLT YFEEPNYDEFRHILMQGVYY >ORF200:30379:30290 MPFLEYHRLLPMMSGNILLCQFIITSMTL >ORF201:30214:30122 Attorney Docket No.40056-0104WO1 MNIYKLEIRSMIKKEIKSLSSHIATKTTML >ORF202:29818:29741 MIQKIFLLLYRRHHRGNHLSRRPRE >ORF203:29080:28940 MRLPRHTCALSKWKDAVVLCLQIGQNHGIWILMVSRSILQMNGCHI >ORF204:28723:28640 MLQNINYIWIFLKRKYLTGVYIYLFII >ORF205:28210:28124 MQKTVTVVHYYIDVYITIRNQNQNHTMN >ORF206:26920:25967 MKTISVVTLLCVLPAVVYSTCTVPTMNNAKLTSTETSFNDKQKVTFTCDQGYHSLDPNAVCETDKWKYEN PCKKMCTVSDYVSELYDKPLYEVNSTMTLSCNGETKYFRCEEKNGNTSWNDTVTCPNAECQPLQLEHGSC QPVKEKYSFGEYMTINCDVGYEVIGASYISCTANSWNVIPSCQQKCDIPSLSNGLISGSTFSIGGVIHLS CKSGFILTGSPSSTCIDGKWNPILPTCVRSNEKFDPVDDGPDDETDLSKLSKDVVQYEQEIESLEATYHI IIVALTIMGVIFLISVIVLVCSCDKNNDQYKFHKLLP >ORF207:24988:24902 MISTLIFTNMMVMSNNILLLQRENAIKE >ORF208:24817:24734 MDIVIHIIQNMIFKNLKYIITSVTVVK >ORF209:24610:24422 MVYTIYPLKIMASRRGKQCIQMYQKEHTTYPHFQRMISYLSGLNLNKAIIKWKSIVRDYASK >ORF210:24352:24194 MLLEVAKRFLFTNAVTCVISTCCIRLTSHSEILKNQYHMISMTTIARLQVAA >ORF211:23890:23759 MIQKRNKTAYYTLVNALIGSNHFQDEVPDYSPSVPLYHLLHVY >ORF212:22408:22322 MRHYDKHVRVYTLSRIYPWKNRTEEYTD >ORF213:20953:20864 MSMKSIQKQLQQLVHWCQTVHQQLQMSSV >ORF214:20587:20486 MHTATGNALDSCIPHSSLLEMMRNQCSSTFASW Attorney Docket No.40056-0104WO1 >ORF215:20470:20324 MMSKIVQKSSVVIYRMSKKPSERFRPSSDFVHMLLLTGEVKTIPLVTV >ORF216:20140:19160 MSILPIIFLPIFFYSSFVQTFNAPECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDILWEKRGA DNDRIIPIDNGSNMLILNPTQSDSGIYICITTNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGE MVCPNINAFIASNVNADIIWSGHRRLRNKRLKQRTPGIITIEDVRKNDAGYYTCVLEYIYRGKTYNVTRI VKLEVRDKIIPSTMQLPDGIVTSIGSNLTIACRVSLRPPTTDADVFWISNGMYYEEDDGDGDGRISVANK IYMTDKRRVITSRLNINPVKEEDATTFTCMAFTIPSISKTVTVSIT >ORF217:17983:17900 MRTFTTKHHKNESSSDLCFKYQPQINS >ORF218:16576:16499 MSRRNNVTQTVHCSRHYTICSFKMP >ORF219:16156:15101 MTMKMMVHIYFVSLLLLLFHSYAIDIENEITEFFNKMRDTLPAKDSKWLNPACMFGGTMNDIAALGEPFS AKCPPIEDSLLSHRYKDYVVKWERLEKNRRRQVSNKRVKHGDLWIANYTSKFSNRRYLCTVTTKNGDCVQ GIVRSHIKKPPSCIPKTYELGTHDKYGIDLYCGILYAKHYNNITWYKDNKEINIDDIKYSQTGKKLIIHN PELEDSGRYNCYVHYDDVRIKNDIVVSRCKILTVIPSQDHRFKLILDPKINVTIGEPANITCTAVSTSLL IDDVLIEWENPSGWLIGFDFDVYSVLTSRGGITEATLYFENVTEEYIGNTYKCRGHNYYFEKTLTTTVVLE >ORF220:14785:14624 MNSESDNISIKTEYEFYDETQDQSTQLVGYDIKLKTNEDDFMAMIDQWVSMII >ORF221:13564:13472 MDSISMVTLKDVHHFIALYNITSLRLLSTY >ORF222:12871:12758 MLALLMVCNMIDCVRNTNLLSMNTGYKHKLKFNIIYL >ORF223:11488:10916 MMIYGLIACLIFVTSSIASPLYIPVIPPITEDKSFNSVEVLVSLFRDDQKDYTVTSQFNNYTIDTKDWTI GVLSTPDGLDIPLTNITYWSRFTIGRALFKSESEDIFQKKMSILGVSIECKKSSTLLTFLTVRKMTRVFN KFPDMAYYRGDCLKAVYVTMTYKNTKTGETDYTYLSNGGLPAYYRNGVDG >ORF224:10228:10118 MIHVLKYFPNKSFKYCINYEKLCYASMMQRCLMIRY >ORF225:9484:8939 Attorney Docket No.40056-0104WO1 MISLSFLIHNPLKKWKLKPSISINGYRSTFTMASPCAQFRPCHCHATKDSLNTVADVRHCLTEYILWVSH RWTHRESAGSLYRLLISFRTDATELFGGELKDSLPWDNIDNCVEIIKCFIRNDSMKTAEELRAIIGLCTQ SAIVSGRVFNDKYIDILLMLRKILNENDYLTLLDHIRTAKY >ORF226:7522:7418 MRIKLYYITRSMSIIYNLQSGYWNMERVLQHHAR >ORF227:6880:6791 MTYYKIDSVQDDKNIYRHHKHGVYFICLA >ORF228:6718:6047 MDEIVRIVRDSMWYIPNVFMDDGKNEGHVSVNNVCHMYFTFFDVDTSSHLFKLVIKHCDLNKRGNSPLHC YTMNTRFNPSVLKILLHHGMRNFDSKDEKGHIPLHHYLIHSLSIDNKIFDILTDTIDDFSKSSDLLLCYL RYKFNGSLNYYVLYKGSDPNCVDEDGLTSLHYYCKHISTFYKSNYYKLSHTKMRAEKRFIYAIIDYGANI NAVTHLPSTVYQT >ORF229:5770:5576 MLPHTSDTTSTFRLKTVFDLVFENRNIIYKADVVNDIIHHRLKVSLPMIKSLFYKMSLPTTITT >ORF230:5290:5198 MWKLICIPSTTHRVLGRPLPVSANPSQRRN >ORF231:4717:4553 MKQYIVLACMCLPVFSNHPHRVRKKKTNIIWESMLLSKSQSKTKHRPMIRFANP >ORF232:3661:3431 MVSLKYFYSLSLFNGVIKYFYSLSLFDGLTKILNLFLMVSLKYFYSLSLFNGVIKYFYSLSLFDGLTKIF LFSFSL >ORF233:2650:1694 MVSLKYFYSHSLFNGVIKYFYSLSLFDGLTKILNLFLMVSLKYFYSHSLFNGVIKYFYSLSLFDGLIKKV LQKYFYSLSLFDGLIKKVLQKYFYSLSLFDGLIKKVLQKYFYSLSLFDGLIKKVLQKYFYSLSLFDGLIK KVLQKYFYSLSLFDGLIKNIKPLSDGVTKIFLFSFSFSLSLFNGVIKYFYSLSLFDGLTKILNLFLMVSL KYFYSHSLFNGVIKYFYSLSLFDGLIKKVLQKYFYSLSLFDGLIKKVLQKYFYSLSLFDGLIKKVLQKYF YSLSLFDGLIKKVLQKYFYSLSLFDGLTKILNLFLMES >ORF234:48666:48493 MDSFSSLFMKLCCISTDKTGSKKSDKKNKNKIKDYYKITIVPGSSSTSTSSWYYTHA >ORF235:48321:48190 MRCTAHDNLHSNQNENTLVIIRNIDGNVIINNPIICRRVNIDG Attorney Docket No.40056-0104WO1 >ORF236:47646:47395 MIPLLFILFYFANGIEWHKFETSEEIISTYLLDDVLYTGVNGAVYTFSNNKLNKTGLTNNNYITTSIKVE DAEPITEIPNVGK >ORF237:47202:47095 MVYEEHSSIKMVLMTKFTFFSLILSAQRELSKFRI >ORF238:46431:46186 MNKHKTDYAGYACCVICGLIVGIIFTATLLKVVERKLVHTPSIDKTIKDAYIREDCPTDWISYNNKCIHL STDRKNLGGRT >ORF239:45684:45577 MLPTSEGGTVLKSLGFNLLPLVFMKSFVLSTSHFK >ORF240:45576:45439 MSTIHSSVNFTRSSWVIEFIGSVVHGSKLANFAYTVSRLVYTPTV >ORF241:43998:43762 MLLEMDKIKITVDSKIGNVVTISYNLEKITIDVTPKKKKEKDVLLAQSVAVEEAKDVKVEEKNIIDIEDD DDMDVESA >ORF242:43125:43039 MITELLAFITSCSAIRLLFAYTCPGDIS >ORF243:42579:42202 MAVCIIDHDNIRGVIYFEPVHGKDKVLGSVIGLKSGTYSLIIHRYGDISQGCDSIGSPEIFIGNIFVNRY GVAYVYLDTDVNIFTIIGKALSISKNDQRLACGVIGISYINEKIIHFLTINENGV >ORF244:40569:39955 MSRGALIVFEGLDKSGKTTQCMNIMESIPANTIKYLNFPQRSTVTGKMIDDYLTRKKTYNDHIVNLLFCA NRWEFASFIQEQLEQGITLIVDRYAFSGVAYAAAKGASMTLSKSYESGLPKPDLVIFLESGSKEINRNVG EEIYEDVTFQQKVLQEYKKMIEEGDIHWQIISSEFEEDVKKELIKNIVIEAIHTVTGPVGQLWM >ORF245:39927:39817 MLVQCYKWMKHITLATWNQYSDTCPICIPNSHQYLN >ORF246:38205:38119 MVKNKARLFERGFHGRFCRFSSTRCLLW >ORF247:37410:37333 MTMTRLLLVYIIILNLKMLFLLSYL >ORF248:36939:36856 Attorney Docket No.40056-0104WO1 MSVDAVILNHRLGFLIEMRCSMDHRVI >ORF249:36537:36448 MKKEKNIYLSKKKKLLMLSNLIILSTMTC >ORF250:36165:36073 MFGEMRNCFLDGNIVYERLNCLLMITCLIR >ORF251:36045:35962 MWKCHRKLMRAKIYKVVFHICYFFCNS >ORF252:35679:35281 MIILKDGYKEFADCMYYFLHYYIGYGRYTYSATNGSCDKGEYLDKRHNQCCNRCPPGEFAKVRCNGNDNT KCERCPPHTYTTIPNYSNGCHQCRKCPTGSFDKVKCTGTQNSKCSCLPGWYCATDSSQTEDC >ORF253:32079:31966 MGIYLDLWCPIPLDFLVLWNEKVSITITLTERPSGRE >ORF254:29733:29359 MKRLETIRHMWSVVYDHFDIVNGKECCYVHTHSSNQNPIPSTVKTNLYMKTMGSCIQMDSMEALEYLSEL KESGGWSPRPEMQEFEYPDGVEDTESIERLVEEFFNRSELQAGKLVKFGNSINC >ORF255:26805:26641 MINRKLHLHVIRDIILWIQMLSAKQINGNTKIHARKCAQFLIMSLNYMISHYTK >ORF256:26001:25900 MTNISSINCYRKYKSVKIINNLITNKYQKIKDL >ORF257:25884:25363 MSSSVDVDIYDAVRAFLLRHYYNKRFIVYGRSNAILHNIYRLFTRCAVIPFDDIVRTMPNESRVKQWVMD TLNGIMMNERDVSVSVGTGILFMEMFFDYNKNSINNQLMYDIINSVSIILANERYRSAFNDDGIYIRRNM INKLYGYASLTTIGTIAGGVCYYLLMHLVSLYK >ORF258:23817:23584 MRSLIIVLLFPSIIYSMSIRRCEKTEEETWGLKIGLCIIAKDFYPERTDCSVHLPTASEGLITEGNGFRD IRNTDKL >ORF259:23049:22831 MDTDVTNVEDIINEIDREKEEILKNVEIENNKNINKNHPSGYIREALVINTSSNSDSIDKEVIECISHDVGI >ORF260:22764:21913 MESFKYCFDNDGKKWIIGNTLYSGNSILYKVRKNFTSSFYNYVMKIDHKSHKPLLSEIRFYISVLDPLTI DNWTRERGIKYLAIPDLYGIGETDDYMFFVIKNSGRVFAPKDTESVFEACVTMINTLEFIHSRGFTHGKI Attorney Docket No.40056-0104WO1 EPRNILIRNKRLSLIDYSRTNKLYKSGNSHIDYNEDMITSGNINYMCVDNHLGATVSKRGDLEMLGYCMI EWFGGKLPWKNESSIKVIKQKKEYKKFIATFFEDCFPEGNEPLELVRYIELVYTLDYSQTPNYDRLRKLFIQD >ORF261:18864:18736 MGISMSSLVYCEQQEQISIGKGGMRYIDLCSFKTHANFEEFI >ORF262:18153:18070 MNSSRYCSLSYSYTCINFLDILQSVLF >ORF263:17952:16228 MSRRLIYVLNINRKSTHKIQENEIYTYFSHCNIDHTSTELDFVVKNYDLNRRQHVTGYTALHCYLYNNYF TNDVLKILLNHDVNVTMKTSSGRMPVYILLTRCCNISHDVVIDMIDKDKNHLLHRDYSNLLLEYIKSRYM LLKEEDIDENIVSTLLDKGIDPNFKQDGYTALHYYYLCLAHVYKPGECRKPITIKKAKRIISLFIQHGAN LNALDNCGNTPFHLYLSIEMCNNIHMTKMLLTFNPNFKICNNHGLTPILCYITSDYIQHDILVMLIHHYE TNVGEMPIDERRMIVFEFIKTYSTRPADSITYLMNRFKNINIYTRYEGKTLLHVACEYNNTHVIDYLIRI NGDINALTDNNKHATQLIIDNKENSPYTIDCLLYILRYIVDKNVIRSLVDQLPSLPIFDIKSFEKFISYC ILLDDTFYDRHVKNRDSKTYRYAFSKYMSFDKYDGIITKCHDETMLLKLSTVLDTTLYAVLRCHNSKKLR RYLNELKKYNNDKSFKIYSNIMNERYLNVYYKDMYVSKVYDKLFPVFTDKNCLLTLLPSEIIYEILYMLT INDLYNISYPPTKV >ORF264:14919:14782 MSTFIIIDQSTENTSIDTTVTINIIYLAIMKIIMNIIMMIMIELV >ORF265:13401:12997 MEEDTNISNKVIRYNTVNNIWKTLPNFWTGTINPGVVSHKDDIYVVCDIKDEKNVKTCIFRYNTNTYNGW ELVTTTESRLSALHTILHDNTIMMLHCYESYMLQDTFNVYTREWNHMCHQHSNSYIMYNILPIY >ORF266:12723:11650 MDIFKELILKHPDENVLISPVSILSTLSILNHGAAGSTAEQLSKYIENMNENTPDDKKDDNNDMDVDIPY CATLATANKIYGSDSIEFHASFLQKIKDDFQTVNFNNANQTKELINEWVKTMTNGKINSLLTSPLSINTR MTVVSAVHFKAMWKYPFSKHLTYTDKFYISKNIVTSVDMMVGTENNLQYVHINELFGGFSIIDIPYEGNS SMVIILPDDIEGIYNIEKNITDEKFKKWCGMLSTKSIDLYMPKFKVEMTEPYNLVPILENLGLTNIFGYY ADFSKMCNETITVEKFLHTTFIDVNEEYTEASAVTGVFMTNFSMVYRTKVYINHPFMYMIKDNTGRILFI GKYCYPQ >ORF267:10098:9823 MSLESFIITTFNNNSSTNIDNMCHLYVKVCPSSLLFRLFVECCDINKLVEGTTPLHCYLMNEGFESSVLK NLLKEYVMNTFNVHDIHYTNI Attorney Docket No.40056-0104WO1 >ORF268:9615:9523 MSTYEKTSFNKMHREKKFIKELVKYETESK >ORF269:8892:7735 MIAFIIFREIGIISTRIAMDCTCILCRLLDEDVTYKKIKLEIETCHNLSKHIDRRGNNALHCYVFNKCDT DIKIVRLLLSRGVERLCRNNEGLTPLGAYSKHRYVKSQIVHLLISSYSNSSNELKSNINDFDLYSYMSSD NIDLRLLKYLIVDKRIRPSKNTNYAINGLGLVDIYVTTPNPRPEVLLWLLKSECYSTGYVFRTCMYDSDM CKNSLHYYISSHRESQSLSKDVIKCLINNNVSIHGRDEGGSLPIQYYWSCSTIDIEIVKLLIKDVDTCRV YDVSPILEADYLNKRFRVTPYNVDMEIVNLLIERRHTLVDVMRSITSYDSRDYNHYIIDNILKRFRQQDE SIVQAMLINYLHYGDMVVRCMLDNGQQLSSARLLC >ORF270:7161:7045 MKNAYISGVSMFDILFKRSKRHRLRYAKNPTSNGTKKN >ORF271:6723:6559 MRWTRLYASFATVCGTYLTYLWTTVRMKVTFLSTMFVICILRSLMWIHRLICLS >ORF272:6102:5869 MEQTLTRLHTYLQQYTKHSPRVVYALLSRGADTRIRNNLDCTPIMERLCNRSYSHNVTQLARTKGRRTTS TLSIHKT >ORF273:5013:4903 MPHSETVTLASTSIYYIVIPILKTTKLIQSLIMWVM >ORF274:4203:4090 MCKESSELEVKYVDGSASEGATDDTSLIDSTKLKACV >ORF275:3471:2938 MVSQKYFYSLSLFDGLIKKVLQKYFYSLSLFDGLIKKVLQKYFYSLSLFDGLIKKVLQKYFYSLSLFDGL IKKVLQKYFYSLSLFDGLIKKVLQKYFYSLSLFDGLIKNIKPLSDGVTKIFLFSFSLQWSHKIFLFSFSL RWSHKNIKPLSDGVTKIFLFSFSLQWSHKIFLFSFSL

[0003] Attorney Docket No.40056-0104WO1 Table 5: OVBCMAt Open Read Frames (ORFs) and nr NCBI Database Entry from Blast Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Attorney Docket No.40056-0104WO1 Additional Sequences: >BCMAt coding sequence: ATGTTGCAGATGGCTGGGCAGTGCTCCCAAAATGAATATTTTGACAGTTTGTT GCATGCTTGCATACCTTGTCAACTTCGATGTTCTTCTAATACTCCTCCTCTAAC ATGTCAGCGTTATTGTAATGCAAGTGTGACCAATTCAGTGAAAGGAACGAAT GCGATTCTCTGGACCTGTTTGGGACTGAGCTTAATAATTTCTTTGGCAGTTTTC GTGCTAATGTTTTTGCTAAGGAAGATAAGCTGA >Promoter: AAAATTGAAAAACTAGCGTC, >J2R ATGAACGGCGGACATATTCAGTTGATAATCGGCCCCATGTTTTCAGGTAAAA GTACAGAATTAATTAGACGAGTTAAACGTTATCAAATAGCTCAATATAAATG CGTGACTATAAAATATTCTAACGATAATAGATACGGAACGGGACTATGGACG CATGATAAGAATAATTTTGAAGCATTGGAAGCAACTAAACTATGCGATGTTT TGGAATTAATTACAGATTTCTCCGTGATAGGTATCGATGAAGGACAGTTCTTT CCAGACATTGTTGAATTCTGTGAGCGTATGGCAAACGAAGGAAAAATAGTTA TAGTAGCCGCACTCGATGGGACATTTCAACGTAAACCGTTTAATAATATTTTG AATCTTATTCCATTATCTGAAATGGTGGTAAAACTAACTGCTGTGTGTATGAA ATGCTTTAAGGAGGCTTCCTTTTCTAAACGATTGGGTGAGGAAACCGAGATA AAAATAATAGGAGGTAATGATATGTATCAATCGGTGTGTAGAAAGTGTTACA TCGACTCATAA Attorney Docket No.40056-0104WO1 > J2R 5’ remnant in OVBCMAt | 80,396 bp - 80,475 bp (80 bp): ATGAACGGCGGACATATTCAGTTGATAATCGGCCCCATGTTTTCAGGTAAAA GTACAGAATTAATTAGACGAGTTAAACG >J2R 3’ remnant in OVBCMAt | 80,807 bp - 80,860 bp (54 bp): GGAGGTAATGATATGTATCAATCGGTGTGTAGAAAGTGTTACATCGACTCAT AA OTHER EMBODIMENTS It is to be understood that while the invention has been described in conjunction with the detailed description thereof, the foregoing description is intended to illustrate and not limit the scope of the invention, which is defined by the scope of the appended claims. Other aspects, advantages, and modifications are within the scope of the following claims.

Claims

Attorney Docket No.40056-0104WO1 1. A method of treating a subject having a solid tumor comprising: administering to the subject an effective amount of an oncolytic virus expressing a human truncated BCMA (BCMAt); and administering to the subject an effective amount of a BCMA-targeting therapy that binds to the BCMAt; wherein the nucleotide sequence of the oncolytic virus expressing BCMAt (OVBCMAt) comprises: (a) an oncolytic virus nucleotide sequence encoding at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NOs: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275; and (b) a transgene comprising a nucleotide sequence encoding the BCMAt.

2. The method of claim 2, wherein the BCMAt lacks signaling domain activity.

3. The method of claim 1 or claim 2, wherein the OVBCMAt does not encode a functional thymidine kinase.

4. The method of any one of claims 1-3, wherein the OVBCMAt does not encode any of an AFP, a CA125, a CD19 (e.g., a CD19t), a CD20, a CD33, a CD22, a CD123, a CD30, a CD38, a GPC-3, a CEA, a HER2, a GD2, a PSMA, a Claudin 18.2, a EpCAM, a GD2, a MSLN, an EGFR, an EGFRVIII, a Trop-2, a c-MET, a Nectin-4, a CD79b, a CCK4, a GPA33, a HLA-A2, a CLEC12A, a p-cadherin, a TDO2, a MART-I, a MUCI, a Pmel 17, a MAGE-I, a TRP-1, a TRP-2, a NY-ESQ, a PSA, aAttorney Docket No.40056-0104WO1 CDK4, a BCA225, a CA 125, a MG7-Ag, a NY-CO-I, a RCAS 1, a SDCCAG16, a TAAL6, and a TAG72, and optionally including truncations and / or functional variants of one or more thereof.

5. The method of any one of claims 1-4, wherein the transgene comprises a promoter that drives expression the nucleotide sequence encoding a truncated human BCMA.

6. The method of any one of the forgoing claims, wherein truncated human BCMA does not include the entirety of the cytoplasmic domain of BCMA.

7. The method of any one of the forgoing claims, wherein the truncated human BCMA comprises an amino acid sequence that comprises or consists of SEQ ID NOs: A3-A4, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative amino acid substitutions).

8. The method of any one of the forgoing claims, wherein the OVBCMAt comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% or 100% identical to or has no more than 100 single nucleotide changes compared to SEQ ID NO: A1 over the entire length of SEQ ID NO: A1 excluding the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO: A1, wherein the 5’ ITR consists of nucleotides (nt) 1 - 6,816 SEQ ID NO: A1 and the 3’ ITR consists of nt 188,074 - 194,902 SEQ ID NO: A1; or wherein the OVBCMAt comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% or 100% identical to nucleotides (nt) 10,001-184,901 of SEQ ID NO: A1 over the entire length of nt 10,001-184,901 of SEQ ID NO: A1.

9. The method of any one of claims 1-7, wherein oncolytic virus nucleotide sequence comprises a nucleotide sequence that is at 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to or has no more than 100 single nucleotide changes compared to SEQ ID NO: A2 over the entire length of SEQ ID NO: A2 excluding the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO:A2, but comprises a deletionAttorney Docket No.40056-0104WO1 of all or a portion of the JR2 gene sequence of SEQ ID NO: A2, wherein the 5’ ITR consists of nt 1- 4,054 SEQ ID NO:A2 and the 3’ ITR consists of nt 185,351-189,404 of SEQ ID NO:A2; or wherein the OVBCMAt comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% or 100% identical to or has no more than 100 single nucleotide changes compared to nucleotides (nt) 10,001- 179,403 of SEQ ID NO: A2 over the entire length of nt 10,001-179,403 of SEQ ID NO: A2.

10. The method of claim 9, wherein the deletion comprises at least about 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 125, 150, 175, 200, 225, 250, 275, 300, 325, 250, 275, 400, 425, 450, 475, or 500 contiguous nucleotides of nt 77,603-78,136 of SEQ ID NO:A2.

11. The method of any one of claims 1-6, wherein the oncolytic virus nucleotide sequence comprises: a nucleotide sequence that is at 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to nt 4,055-77,602 of SEQ ID NO:A2 and a nucleotide sequence that is at 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to nt 78,137-158,350 of SEQ ID NO:A2; a nucleotide sequence that is at 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to nt 4,055-77,681 of SEQ ID NO:A2 and a nucleotide sequence that is at 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to nt 78,085-158,350 of SEQ ID NO:A2; a nucleotide sequence comprising nt 4,055-77,602 of SEQ ID NO:A2 having no more than 100 single nucleotide changes and a nucleotide sequence comprising nt 78,137-158,350 of SEQ ID NO:A2 having no more than 100 single nucleotide changes; or a nucleotide sequence comprising nt 4,055-77681 of SEQ ID NO:A2 having no more than 100 single nucleotide changes and a nucleotide sequence comprising nt 78085-158,350 of SEQ ID NO:A2 having no more than 100 single nucleotide changes.Attorney Docket No.40056-0104WO1 12. The method of any one of the forgoing claims, wherein the BCMA-targeting therapy comprises a bispecific T cell engager comprising a scFv that binds BCMA and an scFv that binds CD3.

13. The method of any one of the forgoing claims, wherein the BCMA-targeting therapy is selected from Teclistamab, Elranatamab / PF-06863135, AMG -701, AMG- 420, BI-836909, EM-901 / CC-93269, JNJ-64007957 / JNJ-7957, REGN-5458, TNB- 383B, FPA-151, HPN-217, and TNB-381M.

14. The method of any one of claims 1-12, wherein the BCMA-targeting therapy comprises: (a) a BCMA target domain comprising: a variable heavy (VH) chain as set forth in table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region, and a variable light (VL) chain as set forth in table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region; and (b) a CD3 target domain comprising: a variable heavy (VH) chain as set forth in table A3, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region, and a variable light (VL) chain as set forth in table A3, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region.

15. The method of any one of claims 1-12, wherein the BCMA-targeting therapy comprises: a BCMA-targeting domain comprising: a heavy chain (HC) comprising or consisting of the amino acid sequence SEQ ID NO: B26 or a variant thereof having 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., conservativeAttorney Docket No.40056-0104WO1 substitutions), wherein the modifications are not in a CDR region, and a light chain (LC) comprising or consisting of the amino acid sequence SEQ ID NO: B25 or a variant thereof having 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region; and a CD3-targeting domain comprising: a HC comprising or consisting of the amino acid sequence SEQ ID NO: C51 or a variant thereof having 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region, and a LC comprising or consisting of the amino acid sequence SEQ ID NO: C50 or a variant thereof having 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region.

16. The method of any one of claims 1-11, wherein the BCMA-targeting therapy comprises a population of autologous or allogeneic human immune cells expressing a chimeric antigen receptor (CAR) or harboring a nucleic acid encoding a CAR, wherein the CAR comprises a BCMA-targeting domain, a transmembrane domain, a costimulatory domain, and a CD3z signaling domain.

17. The method of claim 16, wherein the CAR comprises: a BCMA-targeting domain comprising a BCMA scFv or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions), wherein the modifications are not in a CDR region; a transmembrane domain is selected from: a CD4 transmembrane domain or variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions), a CD8 transmembrane domain or variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions), a CD28 transmembrane domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions), and a CD3ξ transmembrane domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions);Attorney Docket No.40056-0104WO1 a costimulatory domain is selected from: a CD28 co-stimulatory domain or a variant thereof having 1- 5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions); or a 4-l BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions); or both a CD28 co- stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions) and a 4-l BB co-stimulatory domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications (e.g., substitutions); and a CD3ξ signaling domain or a variant thereof having 1-5 (e.g., 1 or 2) single amino acid modifications.

18. The method of claim 16 or 17, wherein the CAR further comprises a spacer domain located between the BCMA targeting domain and the transmembrane domain and comprising any one of SEQ ID NOs: 24-34, or a variant of one or more thereof having 1-5 (e.g., 1 or 2) single amino acid modifications.

19. The method of any one of claims 16-18, wherein the CAR comprises SEQ ID NO: D1 or D2, or a variant thereof having 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region or the BCMA scFv domain.

20. The method of any one of claims 16-19, wherein the immune cells are selected from: macrophages, NK cells, NKT cells, T cells, subpopulations of one or more thereof, and combinations thereof.

21. The method of claim 16, wherein the population of immune cells is selected from bb2121, bb2127, bb21217, LCAR-B38M, MCARH171 / ET140, DESCARTES-08, KITE-585, P-BCMA-10, and JCARH125.Attorney Docket No.40056-0104WO1 22. The method of any one of the forgoing claims, wherein the solid tumor is HER2 positive and the method further comprises administering an effective amount of a populations of HER2 CAR T cells.

23. A method of treating a subject having a solid tumor comprising: administering to the subject an effective amount of an oncolytic virus expressing a truncated BCMA (BCMAt), wherein the nucleotide sequence of oncolytic virus (OVBCMAt) comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to or has no more than 300 single nucleotide changes compared to: a) SEQ ID NO: A1 over the entire length of SEQ ID NO: A1; b) SEQ ID NO: A1 over the entire length of SEQ ID NO: A1, but lacks the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO: A1; or c) nucleotides 6,817-188,073 of SEQ ID NO:A1 over the entire length of nucleotides 6,817-188,073 SEQ ID NO: A1; and administering to the subject an effective amount of a therapy that binds to the BCMAt.

24. The method of claim 23, wherein the OVBCMAt does not encode functional thymidine kinase; and / or wherein the OVBCMAt does not encode CD19.

25. A method of treating a subject having a solid tumor comprising: administering to the subject an effective amount of an oncolytic virus expressing a truncated BCMA (BCMAt), wherein the nucleotide sequence of oncolytic virus (OVBCMAt) comprises: (a) an oncolytic virus nucleotide sequence; and (b) a nucleotide sequence encoding a truncated human BCMA (BCMAt); and administering to the subject an effective amount of a therapy that binds to the BCMAt;Attorney Docket No.40056-0104WO1 wherein the oncolytic virus nucleotide sequence comprises a nucleotide sequence that is at 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to or has no more than 300 single nucleotide changes compared to: a) SEQ ID NO: A2 over the entire length of SEQ ID NO: A2, but lacks a functional JR2 gene sequence of SEQ ID NO: A2; b) SEQ ID NO: A2 over the entire length of SEQ ID NO: A2, but lacks a functioning JR2 gene sequence, the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO: A2 (e.g., a nucleotide sequence that is at 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to nt 4,055-77,602 of SEQ ID NO:A2 and a nucleotide sequence that is at 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, or 100% identical to nt 78,137-158,350 of SEQ ID NO:A2); or c) nucleotides 4,055-185,350 of SEQ ID NO:A2 over the entire length of nucleotides 4,055-185,350 SEQ ID NO: A2, but all or a portion of the J2R sequence.

26. The method of claim 25, wherein the OVBCMAt does not encode functional thymidine kinase; and / or wherein the OVBCMAt does not encode CD19.

27. The method of any of claims 23-26, wherein the oncolytic virus nucleotide sequence has no modifications in the coding regions comprising SEQ ID NOs: X1-X275, or wherein any modifications within the coding regions (SEQ ID NOs: X1-X275) do not change the amino acid sequence of the encoded protein.

28. The method of any of claims 25-27, wherein the oncolytic virus nucleotide sequence comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, 99.99%, or 100% identical to or has no more than 100 single nucleotide changes compared to: SEQ ID NO: A2 over the entire length of SEQ ID NO: A2, but lacks all or a portion of the JR2 gene sequence and comprises nucleotide sequences that encode the proteins having SEQ ID NOs: Z1-Z275, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid substitutions.Attorney Docket No.40056-0104WO1 29. The method of claim 23 or 24, wherein the OVBCMAt comprises a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, 99.99% or 100% identical to or has no more than 100 single nucleotide changes compared to: SEQ ID NO: A1 over the entire length of SEQ ID NO: A1, and encodes proteins having the amino acid sequences of SEQ ID NOs: SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid substitutions.

30. The method of claim 23 or claim 24, the OVBCMAt comprises a nucleotide sequence: a) that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% or 100% identical to or has no more than 100 single nucleotide changes compared to: SEQ ID NO: A1 over the entire length of SEQ ID NO: A1, but lacks the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO: A1; and b) encodes proteins having the amino acid sequences of SEQ ID NOs: Z1-Z275, or a variant of thereof having 1, 2, 3, 4, or 5 single amino acid substitutions.

31. The method of claim 25 or claim 26, wherein: the oncolytic virus sequence is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% or 100% identical to or has no more than 300 single nucleotide changes compared to nt 4,055-77,602 of SEQ ID NO:A2 and nt 78,137-158,350 SEQ ID NO: A2 over the entire length of nt 4,055-77,602 of SEQ ID NO:A2 and nt 78,137-158,350 SEQ ID NO: A2.Attorney Docket No.40056-0104WO1 32. The method of claim 25 or claim 26, wherein OVBCMAt is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% or 100% identical to or has no more than 300 single nucleotide changes compared to: SEQ ID NO: A2 over the entire length of SEQ ID NO: A2 except that the nucleotide sequence encoding BCMAt and a promoter sequence for expressing BCMAt replaces at least 10 contiguous nucleotides of the JR2 gene sequence.

33. The method of any one of claims 25, 26, and 32, wherein at least about 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 125, 150, 175, 200, 225, 250, 275, 300, 325, 250, 275, 400, 425, 450, 475, or 500 contiguous nucleotides of the J2R gene sequence (nt 77,603-78,136 of SEQ ID NO:A2) have been deleted.

34. The method of claim 33, wherein the deletion comprises nucleotides 77,682- 78,084 of SEQ ID NO:A2.

35. The method of any one of claims 25, 26, and 32-34, wherein the nucleotide sequence encoding BCMAt is inserted into a noncoding region of SEQ ID NO:A2.

36. The method of any of claims 25, 26, and 32-35, wherein the nucleotide sequence encoding BCMAt encodes the extracellular domain and the transmembrane domain of BCMA.

37. The method of any of claims 25, 26, and 32-36, wherein the nucleotide sequence encoding BCMAt does not encode the entirety of the cytoplasmic domain of BCMA.

38. The method of any of claims 25, 26, and 32-37, wherein the BCMAt comprises an amino acid sequence that comprises or consists of SEQ ID NO: A3 or A4.

39. The method of any of claims 25, 26, and 32-38, wherein the nucleotide sequence encoding BCMAt is operably linked to a promoter.Attorney Docket No.40056-0104WO1 40. The method of any one of claims 23-39, wherein the therapy that binds to the BCMAt is a TCE comprising a domain that binds BCMA and a domain that binds CD3.

41. The method of claim 40, wherein the domain that binds BCMA is a BCMA- targeted scFv and the domain that binds CD3 is a CD3-targeted scFv.

42. The method of claim 41, wherein the BCMA targeted scFv comprises any one of the following: a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B1-B3 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B5-B7; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B9-B11 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B13-B15; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B17-B19 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: B21-B23; a variable light chain region comprising SEQ ID NO: B4 and a variable heavy region comprising SEQ ID NO: B8; a variable light chain region comprising SEQ ID NO: B12 and a variable heavy region comprising SEQ ID NO: B16; and a variable light chain region comprising SEQ ID NO: B20 and a variable heavy region comprising SEQ ID NO: B24.

43. The method of claim 41 or claim 42, wherein the CD3 targeted scFv comprises any one of the following: a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C1-C3 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C5-C7;Attorney Docket No.40056-0104WO1 a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C9-C11 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C13-C15; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C17-C19 and a variable light chain region having CDR1, CDR2, and CDR3 regions comprising SEQ ID NOs: C21-C23; a variable light chain region comprising SEQ ID NO: C4 and a variable heavy region comprising SEQ ID NO: C8; a variable light chain region comprising SEQ ID NO: C12 and a variable heavy region comprising SEQ ID NO: C16; and a variable light chain region comprising SEQ ID NO: C20 and a variable heavy region comprising SEQ ID NO: C24.

44. The method of any one claims 40-43, wherein the TCE comprises any one of the constructs in Table A1.

45. The method of any one of the preceding claims, wherein the solid tumor is HER2 positive and the method further comprises administering an effective amount of a populations of HER2 CAR T cells.

46. An oncolytic virus expressing a truncated BCMA (OVBCMAt), the nucleotide sequence of OVBCMAt comprising: (a) an oncolytic virus nucleotide sequence; and (b) a nucleotide sequence encoding a truncated human BCMA (BCMAt); wherein the oncolytic virus nucleotide sequence encodes at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186,Attorney Docket No.40056-0104WO1 Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275; and / or wherein the OVBCMAt nucleotide sequence is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9% identical to or has no more than 300 single nucleotide changes compared to: i) nucleotides 6,817-188,073 of SEQ ID NO:A1 over the entire length of nucleotides 6,817-188,073 SEQ ID NO: A1; ii) nucleotides 7,000-188,000 of SEQ ID NO:A1 over the entire length of nucleotides 7,000-188,000 SEQ ID NO: A1; iii) nucleotides 8,000-187,000 of SEQ ID NO:A1 over the entire length of nucleotides 8,000-187,000 SEQ ID NO: A1; or iv) nucleotides 10,000-185,000 of SEQ ID NO:A1 over the entire length of nucleotides 10,000-185,000 SEQ ID NO: A1.

47. The OVBCMAt of claim 46, wherein the OVBCMAt nucleotide sequence is at least 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to or has no more than 100 single nucleotide changes compared to: i) SEQ ID NO: A1 over the entire length of SEQ ID NO: A1; ii) SEQ ID NO: A1 over the entire length of SEQ ID NO: A1, but lacks the 5’ ITR sequence and the 3’ ITR sequence of SEQ ID NO: A1; iii) nucleotides 6,817-188,073 of SEQ ID NO:A1 over the entire length of nucleotides 6,817-188,073 SEQ ID NO: A1; iv) nucleotides 7,000-188,000 of SEQ ID NO:A1 over the entire length of nucleotides 7,000-188,000 SEQ ID NO: A1; v) nucleotides 8,000-187,000 of SEQ ID NO:A1 over the entire length of nucleotides 8,000-187,000 SEQ ID NO: A1; or vi) nucleotides 10,000-185,000 of SEQ ID NO:A1 over the entire length of nucleotides 10,000-185,000 SEQ ID NO: A1.Attorney Docket No.40056-0104WO1 48. The OVBCMAt of claim 46 or claim 47, wherein any nucleotide modifications in the oncolytic virus nucleotide sequence do not change the amino acid sequence of encoded proteins having an amino acid sequences SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275.

49. The OVBCMAt of any one of claims 46-48, wherein any nucleotide modifications in the oncolytic virus nucleotide sequence do not change the amino acid sequence of encoded proteins having an amino acid sequences SEQ ID NO: Z1-Z275.

50. The OVBCMAt of any one of claims 46-49, wherein the OVBCMAt does not encode any of an AFP, a CA125, a CD19 (e.g., a CD19t), a CD20, a CD33, a CD22, a CD123, a CD30, a CD38, a GPC-3, a CEA, a HER2, a GD2, a PSMA, a Claudin 18.2, a EpCAM, a GD2, a MSLN, an EGFR, an EGFRVIII, a Trop-2, a c-MET, a Nectin-4, a CD79b, a CCK4, a GPA33, a HLA-A2, a CLEC12A, a p-cadherin, a TDO2, a MART-I, a MUCI, a Pmel 17, a MAGE-I, a TRP-1, a TRP-2, a NY-ESQ, a PSA, a CDK4, a BCA225, a CA 125, a MG7-Ag, a NY-CO-I, a RCAS 1, a SDCCAG16, a TAAL6, and a TAG72, and optionally functional variants of one or more thereof.

51. The OVBCMAt of any one of claims 46-50, wherein the nucleotide sequence encoding BCMAt encodes the extracellular domain and the transmembrane domain of BCMA.Attorney Docket No.40056-0104WO1 52. The OVBCMAt of any one of claims 46-51, wherein the nucleotide sequence encoding BCMAt does not encode the entirety of the cytoplasmic domain of BCMA.

53. The OVBCMAt of any one of claims 46-52, wherein the BCMAt comprises an amino acid sequence that comprises or consists of SEQ ID NO: A3 or A4.

54. The OVBCMAt of any one of claims 46-53, wherein the nucleotide sequence encoding BCMAt is operably linked to a synthetic early promoter.

55. An oncolytic virus expressing a truncated BCMA (OVBCMAt) comprising a nucleotide sequence that is at least 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%, 99.99%, or 100% identical to or has no more than 100 single nucleotide changes compared to nucleotides 6,817-188,073 of SEQ ID NO: A1 over the entire length of nucleotides 6,817-188,073 of SEQ ID NO: A1.

56. An oncolytic virus expressing a truncated BCMA (OVBCMAt), the nucleotide sequence of OVBCMAt comprising: (a) an oncolytic virus nucleotide sequence; and (b) a nucleotide sequence encoding a truncated human BCMA (BCMAt); wherein the oncolytic virus nucleotide sequence encodes at least 25, 50, 60, 70, 80, 90, 100, 110, 120, or 121 of SEQ ID NO: Z1, Z17, Z26, Z27, Z28, Z32, Z34, Z36, Z41, Z52, Z53, Z55, Z63, Z65, Z66, Z76, Z77, Z79, Z81, Z82, Z87, Z90, Z91, Z92, Z93, Z104, Z108, Z110, Z111, Z116, Z118, Z120, Z123, Z128, Z129, Z130, Z138, Z140, Z142, Z143, Z145, Z146, Z147, Z149, Z150, Z151, Z152, Z153, Z154, Z155, Z156, Z157, Z158, Z160, Z161, Z165, Z168, Z169, Z170, Z172, Z173, Z174, Z175, Z176, Z177, Z178, Z181, Z182, Z186, Z192, Z193, Z194, Z195, Z197, Z198, Z199, Z203, Z206, Z211, Z212, Z216, Z219, Z220, Z222, Z223, Z224, Z225, Z226, Z227, Z228, Z229, Z231, Z232, Z233, Z234, Z236, Z238, Z240, Z241, Z243, Z244, Z252, Z253, Z254, Z257, Z258, Z259, Z260, Z261, Z263, Z264, Z265, Z266, Z267, Z268, Z269, Z270, Z271, Z272, Z274, and Z275; and / orAttorney Docket No.40056-0104WO1 wherein the OVBCMAt nucleotide sequence comprises nucleotides 6,817- 188,073 of SEQ ID NO:A1 or a variant thereof with up to 100, 200, or 300 nucleotide substitutions.

57. The OVBCMAt of claim 56, wherein the OVBCMAt nucleotide sequence comprises nucleotides 6,817-188,073 of SEQ ID NO:A1 or a variant thereof with up to 100 nucleotide substitutions (e.g., 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, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100 nucleotide substitutions).

58. The OVBCMAt of claim 56 or claim 57, wherein the oncolytic virus comprises at least 25, 50, 75, 100, 125, 150, 175, 200, 225, or 250 of SEQ ID NO: X1-X275.

59. The OVBCMAt of any one of claims 56-58, wherein the OVBCMAt does not encode any of an AFP, a CA125, a CD19 (e.g., a CD19t), a CD20, a CD33, a CD22, a CD123, a CD30, a CD38, a GPC-3, a CEA, a HER2, a GD2, a PSMA, a Claudin 18.2, a EpCAM, a GD2, a MSLN, an EGFR, an EGFRVIII, a Trop-2, a c-MET, a Nectin-4, a CD79b, a CCK4, a GPA33, a HLA-A2, a CLEC12A, a p-cadherin, a TDO2, a MART-I, a MUCI, a Pmel 17, a MAGE-I, a TRP-1, a TRP-2, a NY-ESQ, a PSA, a CDK4, a BCA225, a CA 125, a MG7-Ag, a NY-CO-I, a RCAS 1, a SDCCAG16, a TAAL6, and a TAG72, and optionally functional variants of one or more thereof.

60. The OVBCMAt of any one of claims 56-59, wherein the nucleotide sequence encoding BCMAt encodes the extracellular domain and the transmembrane domain of BCMA.

61. The OVBCMAt of any one of claims 56-60, wherein the nucleotide sequence encoding BCMAt does not encode the entirety of the cytoplasmic domain of BCMA.Attorney Docket No.40056-0104WO1 62. The OVBCMAt of any one of claims 56-61, wherein the BCMAt comprises an amino acid sequence that comprises or consists of SEQ ID NO: A3 or A4.

63. The OVBCMAt of any one of claims 56-62, wherein the nucleotide sequence encoding BCMAt is operably linked to a promoter.

64. An oncolytic virus expressing a truncated BCMA (OVBCMAt) comprising nucleotides 6,817-188,073 of SEQ ID NO: A1 or a variant thereof with up to 100 nucleotide modifications (e.g., 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, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100 nucleotide substitutions).

65. A CF33 virus expressing a truncated human BCMA (OVBCMAt), wherein the transgene encoding the truncated BCMA (BCMAt) does not include the entirety of the cytoplasmic domain of BCMA and is inserted into the J2R gene, wherein the OVBCMAt does not encode a functional thymidine kinase and does not encode a second tumor antigen.

66. The OVBCMAt of claim 65, wherein the BCMAt lacks signaling domain activity.

67. The OVBCMAt of claim 65 or claim 66, wherein the OVBCMAt does not encode any of an AFP, a CA125, a CD19 (e.g., a CD19t), a CD20, a CD33, a CD22, a CD123, a CD30, a CD38, a GPC-3, a CEA, a HER2, a GD2, a PSMA, a Claudin 18.2, a EpCAM, a GD2, a MSLN, an EGFR, an EGFRVIII, a Trop-2, a c-MET, a Nectin-4, a CD79b, a CCK4, a GPA33, a HLA-A2, a CLEC12A, a p-cadherin, a TDO2, a MART-I, a MUCI, a Pmel 17, a MAGE-I, a TRP-1, a TRP-2, a NY-ESQ, a PSA, a CDK4, a BCA225, a CA 125, a MG7-Ag, a NY-CO-I, a RCAS 1, a SDCCAG16, a TAAL6, and a TAG72, and optionally including truncations and / or functional variants of one or more thereof.Attorney Docket No.40056-0104WO1 68. The OVBCMAt of any one of claims 65-67, wherein the BCMAt comprises the extracellular domain and the transmembrane domain of BCMA.

69. The OVBCMAt of any one of claims 65-68, wherein the transgene comprises a promoter that drives expression the nucleotide sequence encoding a BCMAt.

70. The OVBCMAt of any one of claims 65-69, wherein the BCMAt comprises or consist of the amino acid sequence of SEQ ID NO: A3.

71. The OVBCMAt of any one of claims 65-69, wherein the BCMAt comprises or consist of the amino acid sequence of SEQ ID NO: A4.

72. A method of treating a subject having a solid tumor comprising: administering to the subject an effective amount of the OVBCMAt of any one of claims 46-71; and administering to the subject an effective amount of a BCMA-targeting therapy that binds to the BCMAt.

73. The method of any one of claims 1-11, 23-29, and 72, wherein the BCMA- targeting therapy comprises a protein comprising a BCMA-targeting domain.

74. The method of claim 73, wherein the BCMA-targeting domain comprises: (a) a heavy chain variable region (VH) comprising a VH complementarity determining region (CDR)1 comprising or consisting of a sequence that is identical to a VH CDR1 amino acid sequence set forth in Table A2; a VH CDR2 comprising or consisting of a sequence that is identical to a VH CDR2 amino acid sequence set forth in Table A2; and a VH CDR3 comprising or consisting of a sequence that is identical to a VH CDR3 amino acid sequence set forth in Table A2; and (b) a light chain variable region (VL) comprising a VL CDR1 comprising or consisting of a sequence that is identical to a VL CDR1 amino acid sequence set forth in Table A2; aAttorney Docket No.40056-0104WO1 VL CDR2 comprising or consisting of a sequence that is identical to a VL CDR2 amino acid sequence set forth in Table A2; and a VL CDR3 comprising or consisting of a sequence that is identical to a VL CDR3 amino acid sequence set forth in Table A2.

75. The method of claim 73, wherein the BCMA-targeting domain comprises: a VH comprising or consisting of an amino acid sequence that is identical to a VH amino acid sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2); and a VL comprising or consisting of an amino acid sequence that is identical to a VL amino acid sequence set forth in Table A2, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the modifications are not in the CDR regions (also as set forth in Table A2).

76. The method of claim 73, wherein the BCMA-targeting domain comprises: a VH comprising or consisting of the amino acid sequence SEQ ID NO: D6 or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in the CDR regions; and a VL comprising or consisting of the amino acid sequence SEQ ID NO: D5 or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., substitutions), wherein the amino acid modifications are not in the CDR regions.

77. The method of claim 73, wherein the BCMA-targeting domain comprises any one of: a variable light chain region having CDR1, CDR2, and CDR3 regions comprising or consisting of SEQ ID NOs: B1-B3 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising or consisting of SEQ ID NOs: B5-B7; a variable light chain region having CDR1, CDR2, and CDR3 regions comprising or consisting of SEQ ID NOs: B9-B11 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising or consisting of SEQ ID NOs: B13-B15;Attorney Docket No.40056-0104WO1 a variable light chain region having CDR1, CDR2, and CDR3 regions comprising or consisting of SEQ ID NOs: B17-B19 and a variable heavy chain region having CDR1, CDR2, and CDR3 regions comprising or consisting of SEQ ID NOs: B21-B23; a variable light chain region comprising or consisting of SEQ ID NO: B4 and a variable heavy region comprising or consisting of SEQ ID NO: B8; a variable light chain region comprising or consisting of SEQ ID NO: B12 and a variable heavy region comprising or consisting of SEQ ID NO: B16; a variable light chain region comprising or consisting of SEQ ID NO: B20 and a variable heavy region comprising or consisting of SEQ ID NO: B24; and a variable light chain region comprising or consisting of SEQ ID NO: D5 and a variable heavy region comprising or consisting of SEQ ID NO: D6.

78. The method of any one of claims 73-77, wherein the protein comprises a BCMA- targeting CAR and further comprises: a spacer comprising or consisting of an amino acid sequence of any one of SEQ ID NOs: 24-34; a transmembrane domain comprising or consisting of an amino acid sequence of any one of SEQ ID NOs: 15-23; a co-stimulatory domain comprising or consisting of an amino acid sequence of any one of SEQ ID NOs: 36-40; and a CD3zeta domain comprising or consisting of the amino acid sequence of SEQ ID NO:

35.

79. The method of claim 78, wherein the BCMA-targeting CAR is expressed on an immune cell (e.g., a BCMA CAR T cell or a BCMA CAR NK cell).

80. The method of any one of claims 73-78, wherein the protein comprises an antibody or an antibody fragment.

81. The method of claim 80, wherein the antibody or the antibody fragment is conjugated a drug, and optionally, wherein the drug is a chemotherapy.Attorney Docket No.40056-0104WO1 82. The method of claim 80 or 81, wherein the antibody or the antibody fragment is bispecific and comprises a second target domain.

83. The method of claim 82, wherein the second targeting domain comprises or consists of a CD3-targeting domain.

84. The method of any one of claims 73-78, wherein the protein comprises or consists of a bispecific T cell engager further comprising a CD3-targeting domain.

85. The method of claims 83 or 84, wherein the CD3-targeting domain comprises: (a) a variable heavy (VH) chain as set forth in table A3, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region; and (b) a variable light (VL) chain as set forth in table A3, or a variant thereof having 1, 2, 3, 4, or 5 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region.

86. The method of any one of claims 72-75 and 80-85, wherein the BCMA-targeting therapy comprises a BCMA-targeting domain comprising: a heavy chain (HC) comprising or consisting of the amino acid sequence SEQ ID NO: B26 or a variant thereof having 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region, and a light chain (LC) comprising or consisting of the amino acid sequence SEQ ID NO: B25 or a variant thereof having 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region.

87. The method of claim 86, wherein the BCMA-targeting therapy further comprises a CD3-targeting domain comprising:Attorney Docket No.40056-0104WO1 a HC comprising or consisting of the amino acid sequence SEQ ID NO: C51 or a variant thereof having 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region; and a LC comprising or consisting of the amino acid sequence SEQ ID NO: C50 or a variant thereof having 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 single amino acid modifications (e.g., conservative substitutions), wherein the modifications are not in a CDR region.

88. The method of any one of claims 1-45 and 72-87, wherein the therapy comprises any one or more of: Teclistamab, Elranatamab / PF-06863135, AMG -701, AMG-420, BI-836909, EM-901 / CC-93269, JNJ-64007957 / JNJ-7957, REGN-5458, TNB-383B, BlenRep / GSK2857916, GSK2857916, CC99712, SEA-BCMA, MEDI2228, AMG 224, REGN5459, HDP-101, FPA-151, HPN-217, TNB-381M, bb2121, bb2127, bb21217, LCAR-B38M, MCARH171 / ET140, DESCARTES-08, KITE-585, P- BCMA-10, and JCARH125.

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