T cell engagers and uses thereof

Abstract

Disclosed herein is a platform technology for designing T cell engagers. Examples of such T cell engagers and nucleic acids (e.g., mRNAs) encoding same as well as lipid nanoparticles comprising nucleic acids (e.g., mRNAs) encoding the T cell engagers are provided. Such T cell engagers can be used to treat cancers such as FCRH5+, GPRC5D+, and / or BCMA+ cancers, including hematological malignancies such as multiple myeloma (e.g., advanced MM, RRMM), B cell lymphoma, and myeloid cancers.

Description

[0001] Attorney Docket No.: 45817-0173WO1 T CELL ENGAGERS AND USES THEREOF CROSS-REFERENCE TO RELATED APPLICATIONS This application claims the benefit of priority of U.S. Provisional Application Nos.63 / 640,254 filed April 30, 2024; 63 / 675,826 filed July 26, 2024; 63 / 695,013 filed September 16, 2024; and 63 / 748,510 filed January 23, 2025, the contents of each of which are incorporated by reference herein in their entirety. SEQUENCE LISTING This application contains a Sequence Listing which has been submitted electronically in XML format and is hereby incorporated by reference in its entirety. Said XML copy, created on April 15, 2025, is named 45817- 0173WO1_SL.xml and is 762,117 bytes in size. BACKGROUND Bispecific antibodies are of increasingly relevance for therapeutic use. The conventional means of producing bispecific antibodies which are monovalent against CD3, i.e., include only one anti-CD3 binding moiety, is to produce them recombinantly to remove impurities that are bivalent against CD3. However, this is a costly and laborious process. Further, conventional means are limited by their inability to target more than a single tumor associated-antigen (TAA). Tumor heterogeneity, immune-escape, and diverse patient TAA expression profiles are common reasons for limited efficacy of a single TAA targeting antibody. The ability to bind to two different targets with the same antibody defines bispecific Ab function. To achieve this desired outcome bispecific antibodies are generally designed based on a heteromeric Fc antibody format using various strategies such as knobs-in-holes, electrostatic steering, or a common light chain to generate an antibody capable of binding two different targets. However, when a T cell binding specificity is included in the bispecific antibody, a functional Fc can drive crosslinking of activated T cells via the anti-CD3 binding and Fc mediated complement dependent cytotoxicity (CDC) or antibody-dependent cell-mediated cytotoxicity (ADCC) resulting in the potential depletion of activated T cells. This Attorney Docket No.: 45817-0173WO1 results in the undesirable depletion of the activated T cells that are required for elimination of the targeted cancer cells. An antibody-like format that ensures targeting of CD3 is monovalent, i.e., with no risk of cross-linking CD3, and which has a half- life adequate for therapy is needed in the art. The instant disclosure advances the art by providing such antibody-like formats. SUMMARY Provided herein is a platform technology for designing and using multi- specific binding molecules to treat disease (e.g., cancer such as a FCRH5 and / or GPRC5D, and / or BCMA positive cancer). Using mRNA multiplexing, mRNAs encoding these multi-specific binding molecules can be used to bind to several TAAs. The multi-specific binding molecule is comprised of a binding moiety (e.g., a Fab) that specifically binds to a T cell surface antigen (e.g., CD3). The binding moiety that specifically binds to a T cell surface antigen (e.g., CD3) is chosen so as to not lead to nonspecific T-cell activation. Appended to the C-terminus of the CH1 of the heavy chain of the Fab are at least two VHHs that specifically bind to tumor associated- antigen s (TAAs). The light chain of the Fab is modified by adding to the C-terminus of the CL, a VHH that binds to human serum albumin (HSA) so as to enhance the circulating half-life of the multi-specific binding molecule. In the context of the Fab- VHH-VHH format, a common light chain is employed to multiplex several TAA- targeting binding molecules such that they can be delivered in a single formulation. This approach is not possible with conventional protein delivery; however, it is achievable utilizing the mRNA delivery system described herein. mRNA multiplexing of the multi-specific binding molecules described herein facilitates proper assembly and expression of multiple therapeutic anti-CD3 multi-specific molecules in vivo. This disclosure demonstrates that it is possible to express multiple TAA-targeted anti- CD3 multi-specific binding molecules by co-formulating strands of mRNA encoding several heavy chains and one strand of mRNA encoding a common light chain with an anti-HSA binding domain. The Fab-VHH-VHH format overcomes the toxicity concerns observed with bivalent anti-CD3, the efficacy shortcomings of targeting Attorney Docket No.: 45817-0173WO1 only one TAA, and the short half-life of proteins. The constructs described herein enable the binding of multiple (e.g., 2, 3, 4, 5) TAAs and T cells to thereby bridge cancer cells, which can be diverse in terms of their antigen expression, and immune cells to facilitate elimination of the cancer cells. In some cases, the constructs bind FCRH5, GPRC5D, and BCMA. The mRNAs encoding these multi-specific binding molecules are formulated in a delivery vehicle such as a nanoparticle (e.g., a lipid nanoparticle). In some cases, the mRNAs are formulated in a single LNP. In other cases, the mRNAs are formulated in two or more LNPs. In certain cases, the LNP comprises an ionizable amino lipid, a PEG-lipid, a phospholipid, and a structural lipid. In some cases, the mRNAs are formulated in a LNP or LNPs comprising Compound 2, Compound I, cholesterol, and DSPC. Pharmaceutical compositions comprising a plurality of such lipid nanoparticles and a pharmaceutically acceptable carrier are also encompassed. The present disclosure provides, among other things, binding molecules that bind both CD3 (e.g., human CD3E) and a tumor associated-antigen(s), and nucleic acids (e.g., mRNAs) encoding the same. The CD3 binding molecule is monovalent. Such binding molecule formats are useful for targeting multiple TAAs, limiting CD3 mediated toxicity, and for extending the half-life of the binding molecule. Such binding molecules can be used to treat non-solid cancers, e.g., hematological malignancies. In some instances, the TAA is FCRH5, GPRC5D, and / or BCMA. These TAAs are useful to target multiple myeloma. In other instances, the TAA is CD19, CD20, or CD22. These TAAs are useful to target B cell cancers such as B cell lymphoma. In yet other instances, the TAA is CD33. Such a T cell engager is useful to treat a myeloid cancer such as acute myeloid leukemia. Provided herein is an mRNA-containing LNP-based therapeutic designed for participants with multiple myeloma (e.g., advanced multiple myeloma, relapsed refractory multiple myeloma). The therapeutic is comprised of 4 mRNAs: anti- GPRC5D HC×anti-CD3, anti-FcRH5 HC×anti-CD3, anti-BCMA HC×anti-CD3, and an anti-HSA common LC×anti-CD3 to increase circulating half-life (see, FIG. 24). These mRNAs encode 3 distinct bispecific TCEs that bind clinically validated TAAs (GPRC5D, FcRH5, and BCMA; and selectively engage and activate T cells, Attorney Docket No.: 45817-0173WO1 promoting T cell-mediated cytotoxicity of tumor cells. This approach leverages the specificity of antibody-target interaction combined with the potent effector function of T cells. Targeting multiple TAAs simultaneously is expected to overcome primary resistance by addressing tumor heterogeneity and acquired resistance by overcoming antigen escape, thereby achieving superior outcomes to single TAA-targeted TCEs. An additional advantage of an mRNA-LNP-based therapy is that the kinetic profile (i.e., delayed tmax and / or attenuated Emax) of the expressed proteins in systemic circulation more closely resembles the kinetic profile of recombinant T-cell bispecific antibodies administered subcutaneously, which have the potential to reduce the incidence of Grade 3 / 4 cytokine release syndrome (CRS) clinically compared to recombinant T-cell bispecifics administered intravenously. In some cases, the mRNA mass ratio of individual TAA-specific heavy chain (HC) mRNAs is as follows: 4 anti- GPRC5D VHH×anti-CD3 Fab HC mRNA: 2 anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: 1 anti-BCMA VHH×anti-CD3 Fab HC mRNA, and the mass ratio of the common light chain (anti-HSAxanti-CD3 Fab LC) is about 4.7. In certain instances, the four mRNAs are provided as follows: about 34% anti-GPRC5D VHH×anti-CD3 Fab HC mRNA: about 17.4% anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 8.6% anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 40% anti-HSAxanti-CD3 Fab LC. Preclinical pharmacology studies demonstrated that this mRNA-containing LNP-based therapeutic provided robust, dose-dependent, on-target cytotoxicity against TAA-positive cancer cells in vitro and ex vivo, exhibited potent antitumor efficacy in multiple tumor-bearing MM mouse models, and demonstrated substantial pharmacological activity in monkeys. In vitro pharmacology studies demonstrated that the TCEs encoded by the mRNAs of this therapeutic bound specifically and with high affinity to their target antigens (i.e., GPRC5D, FcRH5, and BCMA) on MM cells and CD3 on T cells. Specifically, in vitro and ex vivo studies showed selective cytotoxicity against TAA-positive MM cell lines and patient-derived malignant plasma cells. In preclinical in vivo mouse models, this mRNA-containing LNP-based therapeutic exhibited robust expression of the 3 TCE proteins and generated superior antitumor efficacy compared to single TAA-targeted TCEs. Weekly IV and SC doses of this mRNA-containing LNP-based therapeutic in monkeys resulted in Attorney Docket No.: 45817-0173WO1 therapeutically relevant protein expression levels, leading to potent on-target pharmacology as demonstrated by effective depletion of TAA-positive cells. In a first aspect, the disclosure features a lipid nanoparticle or a plurality of lipid nanoparticles comprising a first mRNA, a second mRNA, a third mRNA, and a fourth mRNA. The first mRNA comprises a nucleic acid sequence encoding a first polypeptide with the structure VH-CH1-Linker 1-VHH1a -Linker 2-VHH1b. The second mRNA comprises a nucleic acid sequence encoding a second polypeptide with the structure VH-CH1-Linker 1-VHH2a -Linker 2-VHH2b. The third mRNA comprises a nucleic acid sequence encoding a third polypeptide with the structure VH-CH1- Linker 1-VHH3a -Linker 2-VHH3b. The fourth mRNA comprises a nucleic acid sequence encoding a common polypeptide with the structure VL-CL-Linker 1-VHH4. The VH-CH1 of the first, second, and third polypeptides are from an Fab that specifically binds to human CD3, and the VL-CL of the fourth polypeptide is from Fab that specifically binds to human CD3. In some cases, the human CD3 is human CD3E. The first polypeptide associates with the common polypeptide, the second polypeptide associates with the common polypeptide, and the third polypeptide associates with the common polypeptide. VHH1aand VHH1bare single domain antibodies that specifically bind to a first tumor associated-antigen. In some cases, VHH1aand VHH1bhave the same amino acid sequence. VHH2aand VHH2bare single domain antibodies that specifically binds to a second tumor associated-antigen. In some cases, VHH2aand VHH2bhave the same amino acid sequence. VHH3aand VHH3b are single domain antibodies that specifically binds to a third tumor associated-antigen. In some cases, VHH3a and VHH3b have the same amino acid sequence. VHH4 is a single domain antibody that specifically binds to human serum albumin. In some cases, Linker 1 is a peptide linker (e.g., a glycine serine linker such as one comprising the amino acid sequence set forth in SEQ ID NO:4). In some cases, Linker 2 is a peptide linker (e.g., a glycine serine linker such as one comprising the amino acid sequence set forth in SEQ ID NO:5). In certain cases, the CH1 of the first, second, and third polypeptides are identical in sequence. In some instances, the tumor associated-antigens are multiple myeloma associated antigens. In some cases, the first tumor associated-antigen is FCRH5, the Attorney Docket No.: 45817-0173WO1 second tumor associated-antigen is GPRC5D, and the third tumor associated-antigen is BCMA. In other cases, the first tumor associated-antigen is CD19, the second tumor associated-antigen is CD20, and the third tumor associated-antigen is CD22. In certain instances, the first mRNA, the second mRNA, the third mRNA, and the fourth mRNA are modified mRNAs. In some cases, all the uracils in the mRNAs are N1-methylpseudouracils. In some instances, the first, second, third and fourth mRNAs, further comprise a 5’UTR and a 3’UTR. In some cases, the 3’UTR comprises one or more miR binding sites and / or an IDR. In certain instances, the first, second, third and fourth mRNAs further comprise a poly A tail. In some cases, the poly A tail is about 100 nucleotides in length. In one case, the poly A tail is 100 nucleotides in length (SEQ ID NO: 132). In some instances, the first, second, third and fourth mRNAs further comprise a 5’ terminal cap. In certain instances, the first, second, third and fourth mRNAs, further comprise: (i) a 5’ terminal cap, optionally comprising m7GpppGm; (ii) a 5’UTR, optionally comprising the sequence of SEQ ID NO:64; (iii) a signal sequence if not present in the first, second, third and fourth mRNAs; (iv) a 3’UTR, optionally wherein the 3’UTR comprises one or more miR binding sites and / or an IDR, and further optionally comprising the sequence of any one of SEQ ID NOs:127 to 130; and (v) a poly A tail, optionally wherein the poly A tail is about 100 nucleotides in length, optionally SEQ ID NO:132. In some instances, (i) the first mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:55, wherein the first mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to the N-terminus of the first VHH, the C-terminus of which in turn is linked to the N-terminus of the second VHH, wherein the first and second VHH bind to human FCRH5; (ii) the second mRNA comprises a sequence that encodes an amino acid sequence that is at least Attorney Docket No.: 45817-0173WO1 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:56, wherein the second mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C- terminus of the CH1 is linked to linked to the N-terminus of the third VHH, the C- terminus of which in turn is linked to the N-terminus of the fourth VHH, wherein the third and fourth VHH bind to human GPRC5D; (iii) the third mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:57, wherein the third mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the fifth VHH the C-terminus of which in turn is linked to the N-terminus of the sixth VHH, wherein the fifth and sixth VHH bind to human BCMA; and (iv) the fourth mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:58, wherein the fourth mRNA encodes a VL-CL chain of a Fab that binds to human CD3, wherein the C-terminus of the CL is linked to the N-terminus of the VHH that binds to human HSA. In some cases, all the uracils in the four mRNAs are N1- methylpseudouracils, or the uridines of the mRNA are N1-methylpseudouridines. In some instances, (i) the first mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:60, wherein the first mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to the N-terminus of the first VHH, the C-terminus of which in turn is linked to the N-terminus of the second VHH, wherein the first and second VHH bind to human FCRH5; (ii) the second mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least Attorney Docket No.: 45817-0173WO1 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:61, wherein the second mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the third VHH, the C-terminus of which in turn is linked to the N-terminus of the fourth VHH, wherein the third and fourth VHH bind to human GPRC5D; (iii) the third mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:62, wherein the third mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the fifth VHH the C-terminus of which in turn is linked to the N-terminus of the sixth VHH, wherein the fifth and sixth VHH bind to human BCMA; and (iv) the fourth mRNA comprises a sequence that that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:63, wherein the fourth mRNA encodes a VL-CL chain of a Fab that binds to human CD3, wherein the C- terminus of the CL is linked to the N-terminus of the VHH that binds to human HSA. In some cases, all the uracils in the four mRNAs are N1-methylpseudouracils, or the uridines of the mRNA are N1-methylpseudouridines. In some cases, the nanoparticle (e.g., LNP) is formulated with the four mRNAs of the disclosure with the following mRNA mass ratios: about 4 anti- GPRC5D VHH×anti-CD3 Fab HC mRNA: about 2 anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 1 anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 4.7 anti- HSAxanti-CD3 Fab LC. In certain instances, the nanoparticle (e.g., LNP) is formulated with the four mRNAs as follows: about 34% anti-GPRC5D VHH×anti- CD3 Fab HC mRNA: about 17.4% anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 8.6% anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 40% anti-HSAxanti- CD3 Fab LC. Attorney Docket No.: 45817-0173WO1 In certain instances, the lipid nanoparticle comprises an ionizable amino lipid, a structural lipid, a phospholipid, and a polyethylene glycol (PEG)-modified lipid. In some cases, the ionizable amino lipid is present at about 40 to 50 mole ratio%, the structural lipid is present at 35 to 45 mole ratio%, the phospholipid is present at 5 to 15 mole ratio%, and the PEG-modified lipid is present at 1.5 to 5 mole ratio%. In certain cases, the ionizable amino lipid is present at about 47.5 mole ratio%, the structural lipid is present at about 39 mole ratio%, the phospholipid is present at about 10.5 mole ratio%, and the PEG-modified lipid is present at about 3 mole ratio%. In some cases, the ionizable amino lipid is Compound 2. In certain cases, the structural lipid is cholesterol. In some cases, the phospholipid is DSPC. In some cases, the PEG-modified lipid is Compound I. In one case, the ionizable amino lipid is Compound 2 and is present at about 47.5 mole ratio%, the structural lipid is cholesterol and is present at about 39 mole ratio%, the phospholipid is DSPC and is present at about 10.5 mole ratio%, and the PEG-modified lipid is Compound I and is present at about 3 mole ratio%. In another aspect, the disclosure provides a pharmaceutical composition comprising a lipid nanoparticle(s) described herein, and a pharmaceutically acceptable carrier. In yet another aspect, the disclosure provides a method of treating a cancer in a human subject in need thereof. The method involves administering to the human subject a therapeutically effective amount of a lipid nanoparticle(s) described herein or the pharmaceutical composition described herein. In some cases, the cancer is a FCRH5+, a GPRC5D+, a BCMA+, a FCRH5+ and GPRC5D+, a FCRH5+ and BCMA+, a GPRC5D+ and BCMA+, or a FCRH5+, GPRC5D+, and BCMA+ cancer. In certain cases, the cancer is a hematological cancer such as multiple myeloma. In some cases, the multiple myeloma is relapsed multiple myeloma, refractory multiple myeloma, or relapsed refractory multiple myeloma. In certain cases, the treatment is a second, third, or later line treatment. In some cases, the therapeutically effective amount is 0.002 mg / kg administered intravenously once weekly or twice weekly. In some cases, the nanoparticle (e.g., LNP) is formulated with the four mRNAs of the disclosure with the following mRNA mass ratios: about 4 anti-GPRC5D VHH×anti- Attorney Docket No.: 45817-0173WO1 CD3 Fab HC mRNA: about 2 anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 1 anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 4.7 anti-HSAxanti-CD3 Fab LC. In certain instances, the nanoparticle (e.g., LNP) is formulated with the four mRNAs as follows: about 34% anti-GPRC5D VHH×anti-CD3 Fab HC mRNA: about 17.4% anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 8.6% anti-BCMA VHH×anti- CD3 Fab HC mRNA: about 40% anti-HSAxanti-CD3 Fab LC. In another aspect, the disclosure features a multi-specific binding molecule comprising a first polypeptide comprising from the N-terminus to C-terminus a VH and a CH1, wherein the C-terminus of the CH1 is linked directly or via a linker to at least one VHH that binds to a tumor associated-antigen (i.e., (VHH)n, where n is an integer indicating the number of VHH, e.g., n= 1, 2, 3, 4, 5, optionally n=2) ; and a second polypeptide comprising from the N-terminus to C-terminus a VL and a CL wherein the C-terminus of the CL is linked directly or via a linker to a VHH that binds to human serum albumin. The VH and CH1 associate with the VL and CL to form a Fab. The Fab specifically binds to human CD3 and the at least one VHH of the first polypeptide binds to FCRH5, BCMA, or GPRC5D (see Figure 1B). In some instances, the VH and a CH1 are linked directly or via a first linker through the C-terminus of the CH1 to a first VHH which in turn is linked via its C- terminus directly or via a second linker to the N terminus of a second VHH, wherein the first and second VHH each bind a tumor associated-antigen. In some cases, the tumor associated-antigen is a multiple myeloma associated antigen. In some cases, the tumor associated-antigen is expressed on B cell cancers such as B cell lymphoma. In other cases, the tumor associated-antigen is expressed on myeloid cell cancers such as acute myeloid leukemia (AML). Exemplary linkers and configurations are shown in FIG.1B. In certain instances, the first and second VHH are identical. In other instances, the first and second VHH are not identical. In yet other instances, the first and second VHH are not identical and bind to two different epitopes of the same tumor associated-antigen. In other instances, the first and second VHH bind to different TAAs. It will be apparent to those of skill in the art that the same sorts of combinations can be made with more than two VHHs. Attorney Docket No.: 45817-0173WO1 In some instances, the tumor associated-antigen is FCRH5, GPRc5D, or BCMA. In other instances, the tumor associated-antigen is CD19, CD20, or CD22. In yet other instances, the tumor associated-antigen is CD33. In certain instances, the linker or the first linker is a glycine serine linker. In some cases, the glycine serine linker is G4S (SEQ ID NO:4). In certain instances, the VH of the Fab that binds human CD3 (e.g., human CD3E) comprises a VH CDR1, a VH CDR2, and a VH CDR3 of the VH set forth in SEQ ID NO: 26. In some cases, the CDRs are based on the Kabat definition. In other cases, the CDRs are based on the Chothia definition. In yet other cases, the CDRs are based on the enhanced Chothia definition. In still other cases, the CDRs are based on the IMGT definition. In some instances, the VH of the Fab that binds human CD3 comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:26. The VH of the Fab that binds human CD3 (e.g., human CD3E) comprises a VH CDR1, a VH CDR2, and a VH CDR3 of the VH set forth in SEQ ID NO: 26. In certain instances, the VL of the Fab that binds human CD3 (e.g., human CD3E) comprises a VL CDR1, a VL CDR2, and a VL CDR3 of the VH set forth in SEQ ID NO: 27. In some cases, the CDRs are based on the Kabat definition. In other cases, the CDRs are based on the Chothia definition. In yet other cases, the CDRs are based on the enhanced Chothia definition. In still other cases, the CDRs are based on the IMGT definition. In some instances, the VL of the Fab that binds human CD3 comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:27. The VL of the Fab that binds human CD3 (e.g., human CD3E) comprises a VL CDR1, a VL CDR2, and a VL CDR3 of the VH set forth in SEQ ID NO: 26. In some instances, the VH of the Fab comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at Attorney Docket No.: 45817-0173WO1 least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO:26 and the VL of the Fab comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO:27. In certain cases, the VH of the Fab comprises an amino acid sequence of SEQ ID NO:26 except for 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, or 13 amino acid substitutions. In some cases, the VL of the Fab comprises an amino acid sequence of SEQ ID NO:27 except for 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, or 13 amino acid substitutions. In certain cases, the substitutions are conservative amino acid substitutions. In some instances, the VH of the Fab comprises an amino acid sequence that is identical to the amino acid sequence of SEQ ID NO:26 and the VL of the Fab comprises an amino acid sequence that is identical to the amino acid sequence of SEQ ID NO:27. In some instances, a first VHH that bind to a tumor associated-antigen is linked via a first linker to the C-terminus of the CH1 of the Fab and the C-terminus of the first VHH is linked to the N-terminus of the second VHH by a second linker. In some cases, the first linker is G4S (SEQ ID NO:4) and the second linker is (G4S)3(SEQ ID NO:5). In certain instances, the VHH that binds human serum albumin comprises a VHH CDR1, a VHH CDR2, and a VHH CDR3 of the VHH set forth in SEQ ID NO:44. In some cases, the CDRs are based on the Kabat definition. In other cases, the CDRs are based on the Chothia definition. In yet other cases, the CDRs are based on the enhanced Chothia definition. In still other cases, the CDRs are based on the IMGT definition. In some instances, the VHH that binds human serum albumin comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:44. In certain instances, the tumor associated-antigen is FCRH5 and the at least one VHH comprises a VHH CDR1, a VHH CDR2, and a VHH CDR3 of the VHH set Attorney Docket No.: 45817-0173WO1 forth in SEQ ID NO:34. In some cases, the CDRs are based on the Kabat definition. In other cases, the CDRs are based on the Chothia definition. In yet other cases, the CDRs are based on the enhanced Chothia definition. In still other cases, the CDRs are based on the IMGT definition. In other instances, the at least one VHH that binds FCRH5 comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:34. In some instances, the tumor associated-antigen is GPRc5D and the at least one VHH comprises a VHH CDR1, a VHH CDR2, and a VHH CDR3 of the VHH set forth in SEQ ID NO:39. In some cases, the CDRs are based on the Kabat definition. In other cases, the CDRs are based on the Chothia definition. In yet other cases, the CDRs are based on the enhanced Chothia definition. In still other cases, the CDRs are based on the IMGT definition. In other instances, the at least one VHH that binds GPRC5D comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:39. In some instances, the tumor associated-antigen is BCMA and the at least one VHH comprises a VHH CDR1, a VHH CDR2, and a VHH CDR3 of the VHH set forth in SEQ ID NO:41 or SEQ ID NO:42. In some cases, the CDRs are based on the Kabat definition. In other cases, the CDRs are based on the Chothia definition. In yet other cases, the CDRs are based on the enhanced Chothia definition. In still other cases, the CDRs are based on the IMGT definition. In other instances, the at least one VHH that binds BCMA comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:41 or SEQ ID NO:42. In certain instances, the tumor associated-antigen is CD19. In certain instances, the tumor associated-antigen is CD20. Attorney Docket No.: 45817-0173WO1 In certain instances, the tumor associated-antigen is CD22. In certain instances, the tumor associated-antigen is CD33. In some instances, the VH and a CH1 are linked directly or via a first linker through the C-terminus of the CH1 to a first VHH which in turn is linked via its C- terminus directly or via a second linker to the N terminus of a second VHH, wherein the first and second VHH each bind a tumor associated-antigen. In some cases, the tumor associated-antigen is a multiple myeloma associated antigen. In some cases, the tumor associated-antigen is expressed on B cell cancers such as B cell lymphoma. In other cases, the tumor associated-antigen is expressed on myeloid cell cancers such as acute myeloid leukemia (AML). In some instances, the first and second VHH are identical. In other instances, the first and second VHH are not identical. In yet other instances, the first and second VHH are not identical and bind to two different epitopes of the same tumor associated-antigen. In some instances, the tumor associated-antigen is FCRH5, GPRc5D, BCMA, CD19, CD20, CD22, or CD33. In some instances, the linker or the first linker is a glycine serine linker, optionally G4S (SEQ ID NO:4). In some instances, the VH of the Fab comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO:26 and the VL of the Fab comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the amino acid sequence of SEQ ID NO:27. In certain cases, the VH of the Fab comprises an amino acid sequence of SEQ ID NO:26 except for 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, or 13 amino acid substitutions. In some cases, the VL of the Fab comprises an amino acid sequence of SEQ ID NO:27 except for 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, or 13 amino acid substitutions. In certain cases, the substitutions are conservative amino acid substitutions. Attorney Docket No.: 45817-0173WO1 In some instances, the two VHHs that bind to a tumor associated-antigen are linked via the first linker to the C-terminus of the CH1 peptide, optionally wherein the first linker is G4S (SEQ ID NO:4) and the second linker is (G4S)3(SEQ ID NO:5). In some instances, the tumor associated-antigen is FCRH5 and the at least one VHH comprises a VHH CDR1, a VHH CDR2, and a VHH CDR3 of the VHH set forth in SEQ ID NO:34. In some cases, the CDRs are based on the Kabat definition. In other cases, the CDRs are based on the Chothia definition. In yet other cases, the CDRs are based on the enhanced Chothia definition. In still other cases, the CDRs are based on the IMGT definition. In some instances, the tumor associated-antigen is GPRc5D and the at least one VHH comprises a VHH CDR1, a VHH CDR2, and a VHH CDR3 of the VHH set forth in SEQ ID NO:39. In some cases, the CDRs are based on the Kabat definition. In other cases, the CDRs are based on the Chothia definition. In yet other cases, the CDRs are based on the enhanced Chothia definition. In still other cases, the CDRs are based on the IMGT definition. In some instances, the tumor associated-antigen is BCMA and the at least one VHH comprises a VHH CDR1, a VHH CDR2, and a VHH CDR3 of the VHH set forth in SEQ ID NO:41 or SEQ ID NO:42. In some cases, the CDRs are based on the Kabat definition. In other cases, the CDRs are based on the Chothia definition. In yet other cases, the CDRs are based on the enhanced Chothia definition. In still other cases, the CDRs are based on the IMGT definition. In some instances, the at least one VHH that binds BCMA comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:41 or SEQ ID NO:42. In certain instances, the tumor associated-antigen is CD19. In certain instances, the tumor associated-antigen is CD20. In certain instances, the tumor associated-antigen is CD22. In certain instances, the tumor associated-antigen is CD33. Attorney Docket No.: 45817-0173WO1 In another aspect, the disclosure provides a multi-specific binding molecule comprising: a first polypeptide comprising from the N-terminus to C-terminus a VH and a CH1 linked via the C-terminus of the CH1 directly or via a means for linking to the N-terminus of at least one means for binding to a tumor associated-antigen ; and a second polypeptide comprising from the N-terminus to C-terminus a VL and a CL linked via the C-terminus of the CL directly or via a means for linking to the N- terminus of a means for binding to human serum albumin, wherein the VH and CH1 associates with the VL and CL to form a Fab, and wherein the Fab is a means for binding to human CD3, optionally human CD3E. The disclosure also provides a multi-specific binding molecule comprising: a first polypeptide comprising from the N-terminus to C-terminus a VH and a CH1 linked via the C-terminus of the CH1 directly or via a means for linking to the N- terminus of at least one means for binding to a tumor associated-antigen ; and a second polypeptide comprising from the N-terminus to C-terminus a VL and a CL, wherein the VH and CH1 associates with the VL and CL to form a Fab, and wherein the Fab is a means for binding to human CD3, optionally human CD3E. In some instances, the VH and a CH1 are linked directly or via a first means for linking through the C-terminus of the CH1 to a first means for binding which in turn is linked via its C-terminus directly or via a second means for linking to the N terminus of a second means for binding, wherein the first and second means for binding each bind a tumor associated-antigen, optionally wherein the tumor associated-antigen is a multiple myeloma associated antigen. In some instances, the first and second means for binding are identical. In some instances, the first and second means for binding are not identical. In some instances, the first and second means for binding are not identical and bind to two different epitopes of the same tumor associated-antigen. In some instances, wherein the tumor associated-antigen is FCRH5. In some instances, wherein the tumor associated-antigen is GPRc5D. In some instances, wherein the tumor associated-antigen is BCMA. In some instances, wherein the tumor associated-antigen is CD19. In some instances, wherein the tumor associated-antigen is CD20. Attorney Docket No.: 45817-0173WO1 In some instances, wherein the tumor associated-antigen is CD22. In some instances, wherein the tumor associated-antigen is CD33. In another aspect, the disclosure provides a multi-specific polypeptide composition comprising a first polypeptide comprising from the N-terminus to C- terminus a VH and a CH1 linked via the C-terminus of the CH1 directly or via a linker to at least one VHH that binds to a first tumor associated-antigen. In some cases the C-terminus of the CH1 is linked directly or via a linker to the N-terminus of a first VHH and the C-terminus of the first VHH is linked directly or via a linker to the N- terminus of a second VHH, wherein the first and second VHH bind to a first tumor associated-antigen ; and a second polypeptide comprising from the N-terminus to C- terminus a VL and a CL linked via the C-terminus of the CL directly or via a linker to a VHH that binds to human serum albumin. The VH and CH1 associates with the VL and CL to form a Fab, wherein the Fab specifically bind human CD3. The multi-specific polypeptide composition further comprises a third polypeptide comprising from the N-terminus to C-terminus the VH and the CH1 linked via the C-terminus of the CH1 directly or via a linker to at least one VHH that binds to a second tumor associated-antigen, optionally wherein the C-terminus of the CH1 is linked directly or via a linker to a first VHH, the C-terminus of which is linked directly or via a linker to a second VHH, wherein the first and second VHH bind to the second tumor associated-antigen ; and the second polypeptide comprising from the N-terminus to C-terminus the VL and the CL linked via the C-terminus of the CL to the VHH that binds to human serum albumin, wherein the VH and CH1 associates with the VL and CL to form a Fab, and wherein the Fab specifically bind human CD3. The multi-specific polypeptide composition further comprises a fourth polypeptide comprising from the N-terminus to C-terminus the VH and the CH1 linked via the C-terminus of the CH1 directly or via a linker to at least one VHH that binds to a third tumor associated-antigen, optionally wherein the C-terminus of the CH1 is linked directly or via a linker to the N-terminus of a first VHH, and the C- terminus of the first VHH is linked to the N-terminus of a second VHH, wherein the first and second VHH bind to the third tumor associated-antigen ; and the second polypeptide comprising from the N-terminus to C-terminus the VL and the CL linked Attorney Docket No.: 45817-0173WO1 through its C-terminal directly or via a linker to a VHH that binds to human serum albumin, wherein the VH and CH1 associates with the VL and CL to form a Fab, and wherein the Fab specifically bind human CD3. In some instances, the first TAA is FCRH5, the second TAA is GPRC5D, and the third TAA is BCMA. In other instances, the first TAA is CD19, the second TAA is CD20, and the third TAA is CD22. In certain instances, the first polypeptide comprises an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:55; the third polypeptide comprises an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:56; the fourth polypeptide comprises an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:57; and the second polypeptide comprises an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:58. In some instances, the first, third, and fourth polypeptides each comprise two VHHs. In certain cases, the two VHHs are identical. In other cases, the two VHHs are not identical. In yet other cases, the two VHHs are not identical and bind to two different epitopes of the same tumor associated-antigen. The disclosure also provides a multi-specific polypeptide composition comprising: (i) a first polypeptide comprising from the N-terminus to C-terminus a VH and a CH1 linked via its C-terminal directly or via a means for linking to the N-terminal of at least one means for binding to a first tumor associated-antigen, optionally wherein the C-terminus of CH1 is Attorney Docket No.: 45817-0173WO1 linked directly or via a means for linking to the N-terminal of a first means for binding, the C-terminal of which is linked directly or via a means for linking to the N-terminal of a second means for binding, wherein the first and second means for binding bind to the first tumor associated-antigen ; and (ii) a second polypeptide comprising from the N-terminus to C-terminus a VL and a CL linked via its C-terminal directly or via a means for linking to the N-terminus of a means for binding to human serum albumin, wherein the VH and CH1 associates with the VL and CL to form a Fab, and wherein the Fab is a means for binding to human CD3; (iii) a third polypeptide comprising from the N-terminus to C-terminus the VH and the CH1 linked via its C-terminal directly or via a means for linking to the N-terminus of at least one means for binding to a second tumor associated-antigen, optionally wherein the C-terminus of the CH1 is linked directly or via a means for linking to the N-terminus of a first means for binding, the C-terminus of which is linked directly or via a means for linking to the N-terminus of a second means for binding, wherein the first and second means for binding bind to the second tumor associated-antigen ; and the second polypeptide comprising from the N-terminus to C-terminus the VL and the CL linked via its C-terminal directly or through a means for linking to the N-terminus of a means for binding to human serum albumin, wherein the VH and CH1 associates with the VL and CL to form a Fab, and wherein the Fab is a means for binding to human CD3; and (iv) a fourth polypeptide comprising from the N-terminus to C-terminus the VH and the CH1 linked via its C-terminal directly or via a means for linking to the N-terminus of at least one means for binding to a third tumor associated-antigen, optionally wherein the C-terminus of the CH1 is linked directly or via a means for linking to the N-terminus of a first means for binding, the C-terminus of which is linked directly Attorney Docket No.: 45817-0173WO1 or via a means for linking to the N-terminus of a second means for binding, wherein the first and second means for binding bind to the third tumor associated-antigen ; and the second polypeptide comprising from the N-terminus to C-terminus the VL and the CL linked via its C- terminal directly or via a means for linking to the N-terminus of a means for binding to human serum albumin, wherein the VH and CH1 associates with the VL and CL to form a Fab, and wherein the Fab is a means for binding to human CD3. In some instances, the first tumor associated-antigen is FCRH5, the second tumor associated-antigen is GPRC5D, and the third tumor associated-antigen is BCMA, or wherein the first tumor associated-antigen is CD19, the second tumor associated-antigen is CD20, and the third tumor associated-antigen is CD22. In some instances, the first, third, and fourth polypeptides each comprise two means for binding; optionally wherein the two means for binding are (i) identical, (ii) not identical, or (iii) not identical and bind to two different epitopes of the same tumor associated-antigen. In another aspect, the disclosure features polynucleotides that encode a multi- specific binding molecule or multi-specific polypeptide composition described above. In some cases, the polynucleotides are mRNAs. In some instances, the mRNAs further comprise a 5’UTR and a 3’UTR. In certain cases, the 3’UTR comprises one or more miR binding sites and / or an IDR. In certain instances, the mRNAs further comprise a poly A tail. In some cases, wherein the poly A tail is about 100 nucleotides in length. In some instances, mRNAs further comprise a 5’ terminal cap. In some instances, the mRNAs are chemically modified. In certain instances, the mRNAs comprise a 5’UTR, a 3’UTR, a poly A tail, and a 5’ terminal cap and are chemically modified (e.g., 100 percent of the uracil are replaced with N1-methylpseudouracil). In one aspect, provided herein are mRNAs comprising (i) a first ORF that encodes a VH and CH1 of an Fab that binds to CD3 (e.g., human CD3E) linked via the C-terminus of the CH1 to the N-terminus of a first amino acid sequence that binds Attorney Docket No.: 45817-0173WO1 human FCRH5, optionally wherein the first amino acid sequence is a single domain antibody; (ii) a second ORF that encodes a VH and CH1 of an Fab that binds to CD3 (e.g., human CD3E) linked via the C-terminus of the CH1 to the N-terminus of a second amino acid sequence that binds human GPRC5D, optionally wherein the second amino acid sequence is a single domain antibody; (iii) a third ORF that encodes a VH and CH1 of an Fab that binds to CD3 (e.g., human CD3E) linked via the C-terminus of the CH1 to the N-terminus of a third amino acid sequence that binds human BCMA, optionally wherein the third amino acid sequence is a single domain antibody; and (iv) a fourth ORF that encodes a VL and CL of an Fab that binds to CD3 (e.g., human CD3E) linked via the C-terminus of the CL to the N- terminus of a fourth amino acid sequence that binds human HSA, optionally wherein the fourth amino acid sequence is a single domain antibody. When the polypeptides encoded by the first and fourth ORFs associate those polypeptides bind to human CD3, human FCRH5, and HSA; wherein when the polypeptides encoded by second and fourth ORFs associate those polypeptides bind to human CD3, human GPRC5D, and HSA; and wherein when the polypeptides encoded by the third and fourth ORFs associate, those polypeptides bind to human CD3, human BCMA, and HSA. In certain instances, the human CD3 is human CD3E. In another aspect, the disclosure relates to mRNAs comprising: (i) a first ORF that is at least 75%, at least 80%, at least 85%, at least 95%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:60, wherein the ORF encodes the VH- CH1 chain of an anti-CD3 Fab linked to two VHHs that each bind to human FCRH5; (ii) a second ORF that is at least 75%, at least 80%, at least 85%, at least 95%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:61, wherein the ORF encodes the VH-CH1 chain of an anti-CD3 Fab linked to two VHHs that each bind to human GPRC5D; (iii) a third ORF that is at least 75%, at least 80%, at least 85%, at least 95%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:62, wherein the ORF encodes the VH-CH1 chain of an anti-CD3 Fab linked to two VHHs that each bind to human BCMA; and (iv) a fourth ORF that is at least 75%, at least 80%, at least 85%, at least 95%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:63, wherein the ORF encodes the VL-CL chain of Attorney Docket No.: 45817-0173WO1 an anti-CD3 Fab linked to a VHH that binds to human HSA. When the polypeptides encoded by the first and fourth ORFs associate, polypeptides encoded by the second and fourth ORFs associate, or polypeptides encoded by the third and fourth ORFs associate, those polypeptides bind to human CD3 (e.g., human CD3E). In some instances, the mRNAs further comprise: (i) a 5’ terminal cap, optionally comprising m7-GpppGm; (ii) a 5’UTR, optionally comprising the sequence of SEQ ID NO:64; (iii) a 3’UTR, optionally wherein the 3’UTR comprises one or more miR binding sites and / or an IDR, and further optionally comprising the sequence of any one of SEQ ID NOs:127 to 130; and (iv) a poly A tail, optionally wherein the poly A tail is about 100 nucleotides in length (e.g., SEQ ID NO:132). In some instances, all of the uracils of the mRNA are N1-methylpseudouracils. In certain cases, all of the uridines of the mRNA are N1-methylpseudouridines. In another aspect, the disclosure features a pharmaceutical composition comprising a multi-specific binding molecule, a multi-specific polypeptide composition, a polynucleotide(s), or mRNA(s) described above, and a pharmaceutically acceptable excipient. In another aspect, the disclosure provides a lipid nanoparticle comprising polynucleotides or mRNAs described above. In some instances, the lipid nanoparticle comprises at least four mRNAs. The mRNAs encode polypeptides that assemble to form three different T cell engager constructs that each bind both CD3 and a different tumor associated-antigen. In some instances, three different tumor associated-antigen s are bound by the TCE constructs. In some cases, the three different TAAs are FcRH5, GPRC5D, and BCMA. In some instances, the T cell engagers comprises the same light chain. The polypeptides encoded by these four mRNAs encode an Fab that binds CD3 and each comprises at least two VHHs that bind the same TAA (e.g., FcRH5, GPRC5D, and BCMA) and at least one VHH that binds HSA (see the schematic in FIG 1C). The at least two VHHs that bind a TAA are attached directly or via a linker to the C-terminus of the CH1 of the Fab. In some cases, the at least two VHHs that bind the same TAA are identical in sequence. The least one VHH that binds HSA is attached directly or via a linker to the C-terminus of the CL of the Fab. If more than one VHH is present in a TCE construct, the N-terminal of the second and Attorney Docket No.: 45817-0173WO1 subsequent VHHs are attached directly or via a linker to the C-terminus of the preceding VHH. In some cases, the linker is a glycine-serine linker such as G4S (SEQ ID NO:4) or (G4S)3(SEQ ID NO:5). In yet another aspect, the disclosure provides a plurality of lipid nanoparticles comprising polynucleotides or mRNAs described above. In some cases, the nanoparticle (e.g., LNP) is formulated with the four mRNAs of the disclosure with the following mRNA mass ratios: about 4 anti-GPRC5D VHH×anti-CD3 Fab HC mRNA: about 2 anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 1 anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 4.7 anti- HSAxanti-CD3 Fab LC. In certain instances, the nanoparticle (e.g., LNP) is formulated with the four mRNAs as follows: about 34% anti-GPRC5D VHH×anti- CD3 Fab HC mRNA: about 17.4% anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 8.6% anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 40% anti-HSAxanti- CD3 Fab LC. In one aspect, the lipid nanoparticle comprises four mRNA molecules. The first mRNA molecule encodes a first polypeptide comprising from the N-terminus to C-terminus a first VH and a first CH1 linked via the C-terminus of the first CH1 directly or via a linker to the N-terminus of a first VHH that binds to a first tumor associated-antigen and wherein the C-terminus of the first VHH is linked to the N- terminus of a second VHH that binds to the first tumor associated-antigen. In some cases, the C-terminus of the second VHH is linked to the N-terminus of a third VHH that binds to the first tumor associated-antigen. In certain cases, the first, second, and third VHHs are identical. The second mRNA molecule encodes a second polypeptide comprising from the N-terminus to C-terminus a second VH and a second CH1 linked via the C-terminus of the second CH1 directly or via a linker to the N-terminus of a fourth VHH that binds to a second tumor associated-antigen, and wherein the C- terminus of the fourth VHH is linked to the N-terminus of a fifth VHH that binds to the second tumor associated-antigen. In some cases, the C-terminus of the fifth VHH is linked to the N-terminus of a sixth VHH that binds to the second tumor associated- antigen. In certain cases, the fourth, fifth, and sixth VHHs are identical. The third mRNA molecule encodes a third polypeptide comprising from the N-terminus to C- terminus a third VH and a third CH1 linked via the C-terminus of the third CH1 Attorney Docket No.: 45817-0173WO1 directly or via a linker to the N-terminus of a seventh VHH that binds to a third tumor associated-antigen, and wherein the C-terminus of the seventh VHH is linked to directly or via a linker to the N-terminus of an eighth VHH that binds to the third tumor associated-antigen. In some instances, the C-terminus of the eighth VHH is linked to the N-terminus of a ninth VHH that binds to the third tumor associated- antigen. In certain cases, the seventh, eighth, and ninth VHHs are identical. The fourth mRNA molecule encodes a fourth polypeptide comprising from the N-terminus to C- terminus a VL and a CL linked via the C-terminus of the CL directly or via a linker to the N-terminus of a VHH that binds to human serum albumin. The VH and CH1 of the first, second and third polypeptides each separately pair with the VL and CL of the fourth polypeptide to form a first Fab, a second Fab, and a third Fab. The first Fab binds to human CD3 and to the first tumor associated-antigen on a tumor cell. The second Fab binds to human CD3 and to the second tumor associated-antigen on a tumor cell. The third Fab binds to human CD3 and to the third tumor associated- antigen on a tumor cell. In some cases, the first, second, and third CH1 are identical. In some instances, the first tumor antigen is FcRH5, the second tumor antigen is GPRC5D, and the third tumor antigen is BCMA. In some cases, the first mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:60, wherein the first mRNA encodes a first polypeptide that binds human FCRH5; the second mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:61, wherein the second mRNA encodes a second polypeptide that binds human GPRC5D; the third mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:62, wherein the third mRNA encodes a third polypeptide that binds human BCMA; and (iv) the fourth Attorney Docket No.: 45817-0173WO1 mRNA comprises a sequence that that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:63, wherein the fourth mRNA encodes a fourth polypeptide that binds human HSA. In certain cases, all the uracils are N1- methylpseudouracils, or the uridines of the mRNA are N1-methylpseudouridines. In some cases, the nanoparticle (e.g., LNP) is formulated with the four mRNAs of the disclosure with the following mRNA mass ratios: about 4 anti-GPRC5D VHH×anti- CD3 Fab HC mRNA: about 2 anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 1 anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 4.7 anti-HSAxanti-CD3 Fab LC. In certain instances, the nanoparticle (e.g., LNP) is formulated with the four mRNAs as follows: about 34% anti-GPRC5D VHH×anti-CD3 Fab HC mRNA: about 17.4% anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 8.6% anti-BCMA VHH×anti- CD3 Fab HC mRNA: about 40% anti-HSAxanti-CD3 Fab LC. In some instances, the lipid nanoparticle comprises an ionizable amino lipid, a structural lipid, a phospholipid, and a polyethylene glycol (PEG)-modified lipid. In some cases, the ionizable amino lipid is present at about 40 to 50 mole ratio%, the structural lipid is present at 35 to 45 mole ratio%, the phospholipid is present at 5 to 15 mole ratio%, and the PEG-modified lipid is present at 1.5 to 5 mole ratio%. In certain cases, the ionizable amino lipid is present at about 47.5 mole ratio%, the structural lipid is present at about 39 mole ratio%, the phospholipid is present at about 10.5 mole ratio%, and the PEG-modified lipid is present at about 3 mole ratio%. In certain cases, the ionizable amino lipid is present at 47.5 mole ratio%, the structural lipid is present at 39 mole ratio%, the phospholipid is present at 10.5 mole ratio%, and the PEG-modified lipid is present at 3 mole ratio%. In certain instances, the ionizable amino lipid is Compound 2 or a salt thereof. In some instances, the structural lipid is cholesterol. In other instances, the phospholipid is DSPC. In yet other instances, the PEG-modified lipid is Compound I. In certain instances, the LNP comprises Compound 2 or a salt thereof, cholesterol, DSPC or a salt thereof, and Compound I or a salt thereof. In other instances, the LNP comprises Compound 2, cholesterol, DSPC, and Compound I. In some cases, the Attorney Docket No.: 45817-0173WO1 ionizable amino lipid is present at about 40 to 50 mole ratio%, the structural lipid is present at 35 to 45 mole ratio%, the phospholipid is present at 5 to 15 mole ratio%, and the PEG-modified lipid is present at 1.5 to 5 mole ratio%. In certain cases, the ionizable amino lipid is present at about 47.5 mole ratio%, the structural lipid is present at about 39 mole ratio%, the phospholipid is present at about 10.5 mole ratio%, and the PEG-modified lipid is present at about 3 mole ratio%. In other instances, the ionizable amino lipid is Compound 2 and is present at about 47.5 mole ratio%, the structural lipid is cholesterol and is present at about 39 mole ratio%, the phospholipid is DSPC and is present at about 10.5 mole ratio%, and the PEG-modified lipid is Compound I and is present at about 3 mole ratio%. In some instances, the ionizable amino lipid is Compound 2 and is present at 47.5 mole ratio%, the structural lipid is cholesterol and is present at 39 mole ratio%, the phospholipid is DSPC and is present at 10.5 mole ratio%, and the PEG-modified lipid is Compound I and is present at 3 mole ratio%. In yet another aspect, the disclosure features a method of treating a cancer or tumor in a human subject in need thereof. In some cases, the cancer is FCRH5+, GPRC5D+, BCMA+, FCRH5+ and GPRC5D+, FCRH5+ and BCMA+, GPRC5D+ and BCMA+, or a FCRH5+, GPRC5D+, and BCMA+ cancer. In some cases, the cancer is CD19+, CD20+, CD22+, CD19+ and CD20+, CD19+ and CD22+, CD20+ and CD22+, or a CD19+, CD20+, and CD22+ cancer. In some cases, the cancer is a CD33+ cancer. The method comprises administering to the human subject a therapeutically effective amount of a multi-specific binding molecule, a multi-specific polypeptide composition, polynucleotides, mRNAs, the pharmaceutical composition, or the lipid nanoparticle described above. In one instance, the method comprises administering a therapeutically effective amount of a composition comprising a plurality of the lipid nanoparticles described above. In some cases, the therapeutically effective amount is 0.002 mg / kg administered intravenously once weekly or twice weekly. In some cases, the nanoparticle (e.g., LNP) is formulated with the four mRNAs of the disclosure with the following mRNA mass ratios: about 4 anti- GPRC5D VHH×anti-CD3 Fab HC mRNA: about 2 anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 1 anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 4.7 anti- Attorney Docket No.: 45817-0173WO1 HSAxanti-CD3 Fab LC. In certain instances, the nanoparticle (e.g., LNP) is formulated with the four mRNAs as follows: about 34% anti-GPRC5D VHH×anti- CD3 Fab HC mRNA: about 17.4% anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 8.6% anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 40% anti-HSAxanti- CD3 Fab LC. In some cases, the cancer is a hematological malignancy. In some cases, the cancer is multiple myeloma. In other cases, the cancer is an advanced multiple myeloma. In certain cases, the multiple myeloma is relapsed multiple myeloma. In other cases, the multiple myeloma is refractory multiple myeloma. In yet other cases, the multiple myeloma is relapsed refractory multiple myeloma. In some cases, the treatment is a second, third or later line treatment. Where the human subject is being treated for multiple myeloma, the TAAs that are targeted by the VHHs of the TCEs are one or more of FCRH5, GPRC5D, and BCMA. In some cases, the cancer is a B cell cancer such a B cell lymphoma. In such cases, the TAAs that are targeted by the VHHs of the TCEs are one or more of CD19, CD20, and CD22. In certain cases, the cancer is a myeloid cancer such as AML. In such cases, the TAAs that are targeted by the VHHs of the TCEs include CD33. BRIEF DESCRIPTION OF DRAWINGS FIG.1A is a diagrammatic description of the fact that delivery of mRNA molecules encoding two traditional antibodies results in multiple possible pairings of the heavy and light chains when proteins are translated. As illustrated in the figure, only 12.5% of the dose would result in the desired molecule. FIG.1B is a diagram of the proposed F(ab) engager format which utilizes a common light chain with an anti-HSA for half-life extension. The design prevents mispairing and ensures monovalent CD3 targeting. The squiggle between CH1 and VHH and CL and VHH are linkers, e.g., G4S (SEQ ID NO:4). The squiggle between the two VHHs is a linker, e.g., (G4S)3 (SEQ ID NO:5). FIG.1C is a schematic representation showing that the F(ab) engager allows delivery of multiple mRNA strands that encode for distinct secreted F(ab) engager proteins. In this instance four different mRNAs encode four polypeptides that assemble to form three distinct secreted TCE proteins that bind to three different Attorney Docket No.: 45817-0173WO1 TAAs. These TCEs each share a common light chain and bind to CD3 in a monovalent fashion. FIG.2A is a table showing multiple designs and orientations of the F(ab) engager that were tested with N-terminal designs. Figure discloses “G4S” as SEQ ID NO: 4 and “3xG4S” as SEQ ID NO: 5. FIG.2B is a table depicting multiple designs and orientations of the F(ab) engager were tested with C-terminal designs. Figure discloses “G4S” as SEQ ID NO: 4 and “3xG4S” as SEQ ID NO: 5. FIG.2C is a table depicting multiple designs and orientations of the F(ab) engager were tested with N and C-terminal designs. Figure discloses “G4S” as SEQ ID NO: 4 and “3xG4S” as SEQ ID NO: 5. FIG.3 illustrates the pharmacokinetics of the non-half-life extended (non-HLE) and half-life extended (HLE) F(ab) engager. VHSA1 TCE exhibits significantly higher and longer duration of expression compared to non-HLE TCE. In mRNA-dosed groups, the Cmax is ~21.8x higher and the AUC is ~39.2x higher. In protein-dosed groups, the Cmax is ~11.5x higher and the AUC is ~50.8x higher. Non-HLE TCEs are below the lower limit of detection (LLOQ) by day 4 post dose. FIG 4A depicts the biophysical properties of the FCRH5 F(ab) engager and shows the expected molecular weights by SDS-PAGE and high homogeneity by size- exclusion chromatography. FIG 4B depicts the biophysical properties of the GPRC5D F(ab) engager and shows the expected molecular weights by SDS-PAGE and high homogeneity by size- exclusion chromatography. FIG 4C depicts the biophysical properties of the BCMA F(ab) engager and shows the expected molecular weights by SDS-PAGE and high homogeneity by size- exclusion chromatography. FIG 4D depicts the biophysical properties of a FCRH5 F(ab) engager with an N-terminal anti-HSA VHH. The molecule did not have high homogeneity by size- exclusion chromatography and was not chosen for further evaluation. Attorney Docket No.: 45817-0173WO1 FIG 4E depicts the biophysical properties of a FCRH5 F(ab) engager with an N-terminal anti-HSA VHH. The molecule did not have high homogeneity by size- exclusion chromatography and was not chosen for further evaluation. FIG.5 is a graph showing that humanized anti-CD3 (ModSP34) is cytotoxic in the T cell F(ab) engager format with several therapeutically relevant TAAs. ModSP34- based anti-CD19, CD20, or CD22 TCEs exhibit potent cytotoxicity in target-expressing Raji cancer cells. FIG.6 graphically illustrates that an anti-FCRH5 VHH is cytotoxic in the T cell F(ab) engager format in vitro. N vs C-terminal placement of anti-FCRH5 on ModSP34 heavy chain demonstrated that the C-terminal position of the anti-FCRH5 VHH was more cytotoxic (EC50126 pM vs 956 pM) on RPMI cells. FIG.7 graphically shows that an anti-GPRC5D VHH is cytotoxic in the T cell F(ab) engager format in vitro. Several anti-GPRC5FD clones were tested in monovalent and bivalent format. The top 2 clones, JC11 and seq277, were tested head-to-head. It was found that the bivalent seq277 was the most potent with less than 1 pM EC50 value for cytotoxicity. FIG.8A graphically depicts that an anti-BCMA VHH is cytotoxic in the T cell F(ab) engager format in vitro. Several orientations of two anti-BCMA VHHs, that bind at non-overlapping epitopes, were evaluated as T cell F(ab) engagers for cytotoxicity. FIG.8B shows T cell F(ab) engagers cytotoxicity in the presence of soluble BCMA (1000 ng / mL) and HSA (1.5 mg / mL). HB2-HB3 TCE maintained the highest potency under these conditions. FIG.9 shows that addition of an anti-HSA VHH to the light chain of the F(ab) engager does not impact cytotoxicity. The C-terminal anti-HSA outperformed the N- terminal position in the F(ab) engager format. The C-terminal VHSA1 performed similarly to the standard light chain F(ab) engager and was still strongly cytotoxic with soluble HSA added. FIG.10 shows that the selected T cell F(ab) engager format retains strong binding affinity to CD3 on cells. The binding of FCRH5, GPRC5D, or BCMA T cell F(ab) engager to cell lines expressing human CD3 was assessed by flow Attorney Docket No.: 45817-0173WO1 cytometry. The binding of all three T cell F(ab) engagers was saturated on CD3 expressing cell lines. The binding affinities of ModSP34 of all tested F(ab) engagers to human CD3 ranged from 1-1.3 nM with standard media and 2-5.3 nM with saturating levels of HSA. FIG.11A shows that the selected T cell F(ab) engager format retains strong binding affinity to TAA on cells. The binding of FCRH5, T cell F(ab) engager to a cell line expressing human FcRH5 was assessed by flow cytometry. The binding of the T cell F(ab) engager was saturated on human TAA expressing cell lines in the presence of standard media. Binding affinities of the F(ab) engager to its human TAA is 5.2-25 fold weaker in the presence of 1.5 mg / mL HSA compared to standard media. FIG.11B shows that the selected T cell F(ab) engager format retains strong binding affinity to TAA on cells. The binding of GPRC5D T cell F(ab) engager to a cell line expressing human GPRC5D was assessed by flow cytometry. The binding of the T cell F(ab) engager was saturated on human TAA expressing cell lines in the presence of standard media. Binding affinities of the T cell F(ab) engager to its human TAA is 5.2-25 fold weaker in the presence of 1.5 mg / mL HSA compared to standard media. FIG.11C shows that the selected T cell F(ab) engager format retains strong binding affinity to TAA on cells. The binding of BCMA T cell F(ab) engager to a cell line expressing human BCMA was assessed by flow cytometry. The binding of the T cell F(ab) engager was saturated on human TAA expressing cell lines in the presence of standard media. Binding affinities of the F(ab) engager to its human TAA is 5.2-25 fold weaker in the presence of 1.5 mg / mL HSA compared to standard media. FIG.11D is a table summarizing the binding affinity to the respective TAA for each of the tested T cell F(ab) engagers. FIG.12A shows that the selected T cell F(ab) engager format retains strong cytotoxicity against target cells. The F(ab) engagers were cytotoxic against cell lines expressing their respective TAA (FcRH5). There was no unspecific killing of Molm13 cells that did not express the 3 TAAs. FIG.12B shows that the selected T cell F(ab) engager format retains strong cytotoxicity against target cells. The F(ab) engagers were cytotoxic against cell lines Attorney Docket No.: 45817-0173WO1 expressing their respective TAA (GPRC5D). There was no unspecific killing of Molm13 cells that did not express the 3 TAAs. FIG.12C shows that the selected T cell F(ab) engager format retains strong cytotoxicity against target cells. The F(ab) engagers were cytotoxic against cell lines expressing their respective TAA (BCMA). There was no unspecific killing of Molm13 cells that did not express the 3 TAAs. FIG.12D shows that there was no unspecific killing of Molm13 cells that did not express the three TAAs. FIG.12E is a table summarizing the cellular cytotoxicity of the selected T cell F(ab) engagers. FIG. 13A shows that the T cell F(ab) engagers have good pharmacokinetic properties when formulated separately. All three T cell F(ab) engagers expressed well in vivo when delivered by mRNA formulated in LNP. The calculated protein expression ratios were consistent between separate IV dosed groups for both AUC and Cmax. FIG. 13B shows that the T cell F(ab) engagers have good pharmacokinetic properties when co-formulated. All three T cell F(ab) engagers expressed well in vivo when delivered by mRNA formulated in LNP. The calculated protein expression ratios were consistent between coformulation IV dosed groups for both AUC and Cmax. FIG.14 shows that the T cell F(ab) engager can be delivered subcutaneously with good pharmacokinetic properties. The anti-FCRH5 T cell F(ab) engager expressed well in vivo when administered IV or SC in a non-human primate (NHP). The Cmax and AUC was higher for the IV group, however, the SC group still demonstrated favorable pharmacokinetic properties. FIG. 15A shows responses in an in vivo xenograft efficacy model with no human activated T cells (ATCs). FIG.15B shows responses in an in vivo xenograft efficacy model with ATCs. FIG.15C is a graphical depiction of responses observed following twice weekly (BiW) intravenous (IV) dosing of non-half-life extended (non-HLE) anti- FCRH5 T cell F(ab) Engager wherein the TCE is ModSP34-460hbestx2 + IgK- ModSP34-VL-Constant lambda. Attorney Docket No.: 45817-0173WO1 FIG.15D is a graphical depiction of responses observed following once weekly (QW) intravenous (IV) dosing of non-half-life extended (non-HLE) ModSP34-460hbestx2 + IgK-ModSP34-VL-Constant lambda. FIG.15E shows that anti-FCRH5 VHH is cytotoxic in the T cell F(ab) engager format in vivo. Complete response was observed following QW intravenous (IV) dosing of half-life extended (HLE) ModSP34-460hbestx2 + VHSA1-ModSP34- VL-Constant lambda. FIG.15F shows that anti-FCRH5 VHH is cytotoxic in the T cell F(ab) engager format in vivo. Complete response was observed following QW subcutaneous dosing of non-HLE TCE. FIG.16A depicts responses in an in vivo xenograft efficacy model with no ATCs. FIG.16B represents responses in an in vivo xenograft efficacy model with ATCs. FIG.16C shows that an anti-GPRC5D (Seq277) T cell F(ab) engager is cytotoxic in vivo. Several complete responses were observed following BIW IV dosing of anti-GPRC5D (Seq277) T cell F(ab) engager. FIG.16D shows that an anti-GPRC5D (Seq277) T cell F(ab) engager is cytotoxic in vivo. Several complete response was observed following QW IV dosing of anti-GPRC5D (Seq277) T cell F(ab) engager. FIG.16E shows that an anti-GPRC5D VHH is cytotoxic in the T cell F(ab) engager format in vivo. Complete response was observed following QW IV dosing of anti-GPRC5D (Seq277) T cell F(ab) engager with half-life extension (VHSA1). FIG.17A depicts responses in an in vivo xenograft efficacy model with no ATCs. FIG.17B shows responses in an in vivo xenograft efficacy model with ATCs. FIG. 17C shows that an anti-BCMA VHH is cytotoxic in the T cell F(ab) engager format in vivo. Complete responses were observed following QW IV dosing of a bivalent anti-BCMA (HB2-HB3) F(ab) engager with standard light chain and with C-terminal VHSA1 half-life extension Attorney Docket No.: 45817-0173WO1 FIG.17D shows that an anti-BCMA VHH is cytotoxic in the T cell F(ab) engager format in vivo. Complete responses were observed following QW IV dosing of a monovalent anti-BCMA (HB3) F(ab) engager with standard light chain. FIG.17E shows that an anti-BCMA VHH is cytotoxic in the T cell F(ab) engager format in vivo. Complete responses were observed following QW IV dosing of a bivalent anti-BCMA (HB2-HB3) F(ab) engager with standard light chain. FIG. 17F shows that an anti-BCMA VHH is cytotoxic in the F(ab) engager format in vivo. Complete response was observed following QW IV dosing of a bivalent anti-BCMA (HB2-HB3) F(ab) engager with C-terminal VHSA1 on the light chain for half-life extension. FIG.18A depicts responses in an in vivo xenograft efficacy model with no ATCs. FIG.18B depicts responses in an in vivo xenograft efficacy model with ATCs. FIG.18C shows that a combination of two anti-TAA T cell F(ab) engagers are cytotoxic in vivo in a xenograft efficacy model with anti-GPRC5D, and anti- BCMA T cell F(ab) Engagers. H929 model expresses GPRC5D and BCMA but not FCRH5. mRNAs encoding the two TCEs were formulated in separate LNPs and administered QW IV. FIG.18D shows that a combination of two anti-TAA T cell F(ab) engagers are cytotoxic in vivo in a xenograft efficacy model with anti-GPRC5D, and anti- BCMA T cell F(ab) Engagers. H929 model expresses GPRC5D and BCMA but not FCRH5. mRNAs encoding the two TCEs were coformulated in one LNP and administered QW IV. FIG.18E shows that a combination of three anti-TAA T cell F(ab) engagers are cytotoxic in vivo in a xenograft efficacy model with anti-FCRH5, anti-GPRC5D, and anti-BCMA T cell F(ab) Engagers. H929 model expresses GPRC5D and BCMA but not FCRH5. mRNAs encoding the TCEs were formulated in separate LNPs and administered QW IV. FIG.18F shows that a combination of the 3 anti-TAA T cell F(ab) engagers are cytotoxic in vivo. H929 model expresses GPRC5D and BCMA but not FCRH5. Attorney Docket No.: 45817-0173WO1 Co-formulated groups perform comparably to mRNAs formulated in separate LNPs, and drive anti-tumor activity using QW IV dosing. FIG.18G shows that a combination of the 3 anti-TAA T cell F(ab) engagers are cytotoxic in vivo. H929 model expresses GPRC5D and BCMA but not FCRH5. Co-formulated groups perform comparably to mRNAs formulated in separate LNPs, and drive anti-tumor activity using QW SC dosing. FIG.19A shows pharmacokinetic curves for the FCRH5 T cell F(ab) engager in cynomolgus monkeys following 0.5 mg per kg (mpk) IV dosing. A total of 4 doses were administered QW and levels of F(ab) engager remained mostly above the EC50 and EC90 for cytotoxicity. Representative graph of the FCRH5 F(ab) engager is shown and the trends are similar for GPRC5D and BCMA F(ab) engagers. FIG.19B shows pharmacokinetic curves for the FCRH5 T cell F(ab) engager in cynomolgus monkeys following 2 mg per kg (mpk) IV dosing. A total of 4 doses were administered QW and levels of F(ab) engager remained mostly above the EC50 and EC90 for cytotoxicity. Representative graph of the FCRH5 F(ab) engager is shown and the trends are similar for GPRC5D and BCMA F(ab) engagers. FIG.19C shows pharmacokinetic curves for the FCRH5 T cell F(ab) engager in cynomolgus monkeys following 5 mg per kg (mpk) IV dosing. A total of 4 doses were administered QW and levels of F(ab) engager remained mostly above the EC50 and EC90 for cytotoxicity. Representative graph of the FCRH5 F(ab) engager is shown and the trends are similar for GPRC5D and BCMA F(ab) engagers. FIG.19D shows pharmacokinetic curves for the FCRH5 T cell F(ab) engager in cynomolgus monkeys following 2 mg per kg (mpk) SC dosing. A total of 4 doses were administered QW. Representative graph of the FCRH5 F(ab) engager is shown and the trends are similar for GPRC5D and BCMA F(ab) engagers. FIG.19E shows B-cell depletion levels in peripheral blood 7 days post dose 1. Strong depletion was observed for all the dosing groups. FIG.19F shows Memory B-cell depletion levels in peripheral blood 7 days post dose 1. Strong depletion was observed for all the dosing groups. FIG.19G shows T-cell proliferation levels in peripheral blood 8 days post dose 1. Strong proliferation was observed for all the dosing groups. Attorney Docket No.: 45817-0173WO1 FIG.19H shows B-cell depletion levels in bone marrow 24 hours post dose 4. Strong depletion was observed for some of the dosing groups above 2 mpk. FIG.19I shows T-cell proliferation levels in bone marrow 24 hours post dose 4. Strong proliferation was observed for all the dosing groups above 2 mpk. FIG.20 are graphs comparing QW and Q2W and IV and SC dosing of mRNAs encoding a TCE that binds CD3 and FCRH5. FIG.21 are graphs comparing QW and Q2W and IV and SC dosing of mRNAs encoding a TCE that binds CD3 and FCRH5. FIG.22 are a series of graphs that show that mRNA-2808 (the combination of the four mRNAs formulated in a single LNP that together encode FCRH5-TCE, GPRC5D-TCE, and BCMA-TCE) causes T cell activation and proliferation in MM patient samples. FIGs.23A-23F show the data relating to the non-human primate PK / PD study described in Example 10. FIG.24 is a schematic diagram showing the mechanism of action of an exemplary drug product of this disclosure. DETAILED DESCRIPTION This disclosure features a platform technology for multi-specific binding molecules – both polypeptides and nucleic acids that encode these polypeptides (e.g., mRNAs) - that have been designed to simultaneously engage CD3 on human T cells and a tumor-associated antigen (TAA) on a tumorigenic cell to induce T-cell mediated cytotoxicity of the target cancer cell. These multi-specific binding molecules are referred to herein as T cell engagers. The CD3 targeting moiety of the T cell engager must be monovalent because cross-linking of CD3 can cause severe toxicity and death. The conventional means of producing these antibodies is to produce them recombinantly and purify impurities that are bivalent against CD3. However, this is a costly and laborious process. Further, conventional means are limited by their ability to develop and target a single TAA. Tumor heterogeneity, immune escape, and patient TAA expression profiles are common reasons for limited efficacy of antibodies targeting a single TAA. Attorney Docket No.: 45817-0173WO1 The anti-CD3 bispecific binding molecules of this disclosure, which are produced in vivo by administration of mRNA molecules, are designed to bind to one or more tumor antigens and to only induce a cytotoxic CD8+ T-cell response after complexing to a tumor associated-antigen, but not induce nonspecific cytotoxic T-cell activation. To meet these design goals, the bispecific binding molecules of this disclosure have several therapeutic design attributes. The binding molecules of this disclosure lack Fc functionality and so do not deplete the activated T cells that are required for elimination of the targeted cancer cells. In addition, the binding molecules have an antibody-like format that ensures targeting of CD3 is monovalent, i.e., with no risk of cross-linking CD3, and have the desired half-life for a therapeutic. The format of the binding molecules of this disclosure comprises an anti-CD3 binding Fab and TAA-targeting VHHs that are appended to the C-terminus of the CH1 of the Fab. Surprisingly, this format was found to yield superior results as compared to other formats tested. The light chain of the Fab comprises a VHH that binds to HSA at the C-terminus of the CL of the Fab to enhance the circulating half- life of the binding molecule. With the Fab-VHH-VHH format, a common light chain is used to multiplex antibodies allowing one mRNA product to target multiple TAAs at the same time using a single formulation. This approach is not possible with conventional protein delivery, but is possible when delivering this format as mRNA that encodes for the described protein components that assemble and express the desired therapeutic anti-CD3 binding molecules in vivo. This disclosure demonstrates that with a combination of 4 mRNAs it is possible to express 3 VHHs that bind TAAs by delivering 3 strands of mRNA encoding a heavy chain and 1 strand of mRNA encoding a common light with an anti-HSA binding domain. This proof of concept enables formulations comprising varying numbers of mRNAs and varying numbers of anti-TAA VHH moieties to arrive at the desired protein therapeutics in vivo. Such mRNA molecules can be delivered in the same or in separate delivery vehicles (e.g., LNPs), although it is preferable to deliver them in the same LNP. The Fab-VHH- VHH format overcomes toxicity concerns of bivalent anti-CD3, efficacy shortcomings of targeting only one TAA, and short half-life of proteins. Attorney Docket No.: 45817-0173WO1 In one aspect, the disclosure provides a platform technology that features a multi-specific binding molecule that is a T cell engager comprising a first polypeptide comprising from the N-terminus to C-terminus a VH and a CH1 linked directly or via a linker to at least one VHH that binds to a tumor associated-antigen ; and a second polypeptide comprising from the N-terminus to C-terminus a VL and a CL linked directly or via a linker to a VHH that binds to an agent for the purpose of half-life extension (e.g., human serum albumin). In some cases, the C-terminus of the CH1 is linked directly or via a linker to two or at least two VHHs that binds to a tumor associated-antigen. The VH and CH1 associates with the VL and CL to form a Fab, and the Fab specifically bind to human CD3 (e.g., human CD3E). In some cases, the TAA is FCRH5. In other cases, the TAA is GPRC5D. In yet other cases, the TAA is BCMA. Also provided are compositions comprising one, two, or three of these multi- specific binding molecules each of which bind a different TAA. Furthermore, the disclosure encompasses an mRNA encoding the multi-specific binding molecule as well compositions comprising a plurality of mRNAs that encode one, two, or three of these multi-specific molecules each of which bind a different TAA. The mRNA or plurality of mRNAs can be administered to a human subject formulated within a lipid nanoparticle. In some cases, the lipid nanoparticle comprises a structural lipid, a phospholipid, a PEG-lipid and an ionizable amino lipid. In some cases, the lipid nanoparticle comprises Compound 2, DSPC, cholesterol, and Compound I. In some cases, the LNP comprises about 47.5 mole ratio % Compound 2, about 10.5 mole ratio % DSPC, about 39 mole ratio %, and about 3 mol% Compound I. In some cases, the nanoparticle (e.g., LNP) is formulated with the four mRNAs of the disclosure with the following mRNA mass ratios: about 4 anti-GPRC5D VHH×anti-CD3 Fab HC mRNA: about 2 anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 1 anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 4.7 anti-HSAxanti-CD3 Fab LC. In certain instances, the nanoparticle (e.g., LNP) is formulated with the four mRNAs as follows: about 34% anti-GPRC5D VHH×anti-CD3 Fab HC mRNA: about 17.4% anti-FcRH5 VHH×anti-CD3 Fab HC mRNA: about 8.6% anti-BCMA VHH×anti-CD3 Fab HC mRNA: about 40% anti-HSAxanti-CD3 Fab LC. Attorney Docket No.: 45817-0173WO1 The disclosure features a T cell engager comprising a means for binding human CD3 (e.g., human CD3E) linked to (i) one, two, or more means for binding a TAA (e.g., FcRH5, GPRC5D, BCMA); and (ii) means for binding a moiety for the purpose of half-life extension (e.g., HSA). Nucleic acid molecules (e.g., mRNA molecules) encoding such engagers are also provided and allow for targeting multiple TAAs at the same time, thereby reducing the possibility of antigenic escape by tumor cells using one drug product. More specifically, the data in the instant Examples demonstrate that the messenger RNA (mRNA) platform enables multiplexing of four mRNA sequences to encode three T cell engagers (TCEs) in a single drug product. The three TCEs exemplified herein encode distinct bispecific TCEs directed against CD3 and the clinically validated MM TAAs BCMA, FcRH5, and GPRC5D. Targeting multiple tumor associated-antigen s (TAAs) simultaneously using this platform circumvent target-mediated resistance and achieve outcomes superior to those seen with single TAA targeting. Definitions As used herein, the term “about” refers to a stated numerical term and a value that is no more than 10% above or below the value being described. For example, the term “about 5 nM” indicates disclosure of both the stated value of 5 nM and a range of from 4.5 nM to 5.5 nM. When used with respect to time, e.g., “about” 1 week, the term “about” means + / - 3 days, so about 1 week refers to 1 week and a range of 4 days to 10 days. As used herein, the terms “conservative mutation,” “conservative substitution,” “conservative amino acid substitution,” and the like refer to a substitution of one or more amino acids for one or more different amino acids that exhibit similar physicochemical properties, such as polarity, electrostatic charge, and / or steric volume. These properties are summarized for each of the twenty naturally-occurring amino acids in Table 1 below. Attorney Docket No.: 45817-0173WO1 Table 1 – Representative Physicochemical Properties of Naturally-Occurring Amino Acids From this table it is appreciated that the conservative amino acid families include, e.g., (i) G, A, V, L, I, P, and M; (ii) D and E; (iii) C, S and T; (iv) H, K and R; (v) N and Q; and (vi) F, Y and W. A conservative mutation or substitution is therefore one that substitutes one amino acid for a member of the same amino acid family (e.g., a substitution of Ser for Thr or Lys for Arg). As used herein, the term “fusion protein” refers to a protein that is joined via a covalent bond to another molecule. Attorney Docket No.: 45817-0173WO1 As used herein, the term “lipid nanoparticle” refers to a transfer vehicle including one or more lipids (e.g., cationic lipids, non-cationic lipids, and PEG- modified lipids). Examples of lipid nanoparticles are formulated to deliver one or more mRNA molecules to one or more target cells in vivo. Examples of suitable lipids include, for example, ionizable amino lipids, phospholipids, cholesterol lipids, and PEG lipids. Other formulations will be known to those of skill in the art and such lipids can be used to formulate LNPs with nucleic acids (e.g., mRNA) or enhance the delivery of mRNA into the target cells. As used herein, the terms “percent (%) sequence identity,” “percent (%) identity,” and the like, with respect to a reference polynucleotide or polypeptide sequence, is defined as the percentage of nucleic acids or amino acids in a candidate sequence that are identical to the nucleic acids or amino acids in the reference polynucleotide or polypeptide sequence, after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity. Alignment for purposes of determining percent nucleic acid or amino acid sequence identity can be achieved in various ways that are within the capabilities of one of skill in the art, for example, using publicly available computer software such as BLAST, BLAST-2, or Megalign software. Those skilled in the art can determine appropriate parameters for aligning sequences, including any algorithms needed to achieve maximal alignment over the full length of the sequences being compared. For example, percent sequence identity values may be generated using the sequence comparison computer program BLAST. As an illustration, the percent sequence identity of a given nucleic acid or amino acid sequence, A, to, with, or against a given nucleic acid or amino acid sequence, B, (which can alternatively be phrased as a given nucleic acid or amino acid sequence, A that has a certain percent sequence identity to, with, or against a given nucleic acid or amino acid sequence, B) is calculated as: 100 multiplied by (the fraction X / Y) where X is the number of nucleotides or amino acids scored as identical matches by a sequence alignment program (e.g., BLAST) in that program’s alignment of A and B, and where Y is the total number of nucleic acids in B. It will be appreciated that where the length of nucleic acid or amino acid sequence A is not Attorney Docket No.: 45817-0173WO1 equal to the length of nucleic acid or amino acid sequence B, the percent sequence identity of A to B will not equal the percent sequence identity of B to A. As used herein, the phrase “specifically binds” refers to a binding reaction which is determinative of the presence of an antigen in a heterogeneous population of proteins and other biological molecules that is recognized, e.g., by an antibody or antigen-binding fragment thereof, with particularity, i.e., at levels above background binding. In one embodiment, an antibody or antigen-binding fragment thereof that specifically binds to an antigen will bind to the antigen with a KD of less than 100 nM. For example, an antibody or antigen-binding fragment thereof that specifically binds to an antigen via the antigen binding domain will bind to the antigen with a KD of up to 100 nM (e.g., between 1 pM and 100 nM). An antibody or antigen-binding fragment thereof that does not exhibit specific binding to a particular antigen or epitope thereof will exhibit a KD of greater than 100 nM (e.g., greater than 500 nm, 1 μM, 100 μM, 500 μM, or 1 mM) for that particular antigen or epitope thereof. A variety of immunoassay formats may be used to select antibodies specifically immunoreactive with a particular protein or carbohydrate. For example, solid-phase ELISA immunoassays are routinely used to select antibodies specifically immunoreactive with a protein or carbohydrate. See, Harlow & Lane, Antibodies, A Laboratory Manual, Cold Spring Harbor Press, New York (1988) and Harlow & Lane, Using Antibodies, A Laboratory Manual, Cold Spring Harbor Press, New York (1999), for a description of immunoassay formats and conditions that can be used to determine specific immunoreactivity. As used herein, the terms “treat” or “treatment” refer to therapeutic treatment, in which the object is to inhibit or slow down (lessen) an undesired physiological change or disorder, such as a cancer. Beneficial or desired clinical results of treatment include, without limitation, alleviation of symptoms, diminishment of extent of disease, stabilized (i.e., not worsening) state of disease, delay or slowing of disease progression, amelioration or palliation of the disease state, and remission (whether partial or total), whether detectable or undetectable. Those in need of treatment include those already having the condition or disorder, as well as those prone to have the condition or disorder or those in which the condition or disorder is to be inhibited. Attorney Docket No.: 45817-0173WO1 As used herein, the term “alkyl,” “alkyl group,” or “alkylene” means a linear or branched, saturated hydrocarbon including one or more carbon atoms (e.g., one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, twenty, or more carbon atoms), which is optionally substituted. The notation “C1-14alkyl” means an optionally substituted linear or branched, saturated hydrocarbon including 1-14 carbon atoms. Unless otherwise specified, an alkyl group described herein refers to both unsubstituted and substituted alkyl groups. As used herein, the term “alkenyl,” “alkenyl group,” or “alkenylene” means a linear or branched hydrocarbon including two or more carbon atoms (e.g., two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, twenty, or more carbon atoms) and at least one double bond, which is optionally substituted. The notation “C2-14 alkenyl” means an optionally substituted linear or branched hydrocarbon including 2-14 carbon atoms and at least one carbon-carbon double bond. An alkenyl group may include one, two, three, four, or more carbon-carbon double bonds. For example, C18alkenyl may include one or more double bonds. A C18alkenyl group including two double bonds may be a linoleyl group. Unless otherwise specified, an alkenyl group described herein refers to both unsubstituted and substituted alkenyl groups. As used herein, the term “alkynyl,” “alkynyl group,” or “alkynylene” means a linear or branched hydrocarbon including two or more carbon atoms (e.g., two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, twenty, or more carbon atoms) and at least one carbon-carbon triple bond, which is optionally substituted. The notation “C2-14 alkynyl” means an optionally substituted linear or branched hydrocarbon including 2- 14 carbon atoms and at least one carbon-carbon triple bond. An alkynyl group may include one, two, three, four, or more carbon-carbon triple bonds. For example, C18 alkynyl may include one or more carbon-carbon triple bonds. Unless otherwise specified, an alkynyl group described herein refers to both unsubstituted and substituted alkynyl groups. Attorney Docket No.: 45817-0173WO1 As used herein, the term “carbocycle” or “carbocyclic group” means an optionally substituted mono- or multi-cyclic system including one or more rings of carbon atoms. Rings may be three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty membered rings. The notation “C3-6carbocycle” means a carbocycle including a single ring having 3-6 carbon atoms. Carbocycles may include one or more carbon- carbon double or triple bonds and may be non-aromatic or aromatic (e.g., cycloalkyl or aryl groups). Examples of carbocycles include cyclopropyl, cyclopentyl, cyclohexyl, phenyl, naphthyl, and 1,2 dihydronaphthyl groups. The term “cycloalkyl” as used herein means a non-aromatic carbocycle and may or may not include any double or triple bond. Unless otherwise specified, carbocycles described herein refers to both unsubstituted and substituted carbocycle groups, i.e., optionally substituted carbocycles. As used herein, the term “heterocycle” or “heterocyclic group” means an optionally substituted mono- or multi-cyclic system including one or more rings, where at least one ring includes at least one heteroatom. Heteroatoms may be, for example, nitrogen, oxygen, or sulfur atoms. Rings may be three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, or fourteen membered rings. Heterocycles may include one or more double or triple bonds and may be non- aromatic or aromatic (e.g., heterocycloalkyl or heteroaryl groups). Examples of heterocycles include imidazolyl, imidazolidinyl, oxazolyl, oxazolidinyl, thiazolyl, thiazolidinyl, pyrazolidinyl, pyrazolyl, isoxazolidinyl, isoxazolyl, isothiazolidinyl, isothiazolyl, morpholinyl, pyrrolyl, pyrrolidinyl, furyl, tetrahydrofuryl, thiophenyl, pyridinyl, piperidinyl, quinolyl, and isoquinolyl groups. The term “heterocycloalkyl” as used herein means a non-aromatic heterocycle and may or may not include any double or triple bond. Unless otherwise specified, heterocycles described herein refers to both unsubstituted and substituted heterocycle groups, i.e., optionally substituted heterocycles. As used herein, the term “heteroalkyl,” “heteroalkenyl,” or “heteroalkynyl” refers respectively to an alkyl, alkenyl, alkynyl group, as defined herein, which further comprises one or more (e.g., 1, 2, 3, or 4) heteroatoms (e.g., oxygen, sulfur, nitrogen, Attorney Docket No.: 45817-0173WO1 boron, silicon, phosphorus) wherein the one or more heteroatoms is inserted between adjacent carbon atoms within the parent carbon chain and / or one or more heteroatoms is inserted between a carbon atom and the parent molecule, i.e., between the point of attachment. Unless otherwise specified, heteroalkyls, heteroalkenyls, or heteroalkynyls described herein refers to both unsubstituted and substituted heteroalkyls, heteroalkenyls, or heteroalkynyls, i.e., optionally substituted heteroalkyls, heteroalkenyls, or heteroalkynyls. As used herein, a “biodegradable group” is a group that may facilitate faster metabolism of a lipid in a mammalian entity. A biodegradable group may be selected from the group consisting of, but is not limited to, -C(O)O-, -OC(O)-, -C(O)N(R')-, -N(R')C(O)-, -C(O)-, -C(S)-, -C(S)S-, -SC(S)-, -CH(OH)-, -P(O)(OR')O-, -S(O)2-, an aryl group, and a heteroaryl group. As used herein, an “aryl group” is an optionally substituted carbocyclic group including one or more aromatic rings. Examples of aryl groups include phenyl and naphthyl groups. As used herein, a “heteroaryl group” is an optionally substituted heterocyclic group including one or more aromatic rings. Examples of heteroaryl groups include pyrrolyl, furyl, thiophenyl, imidazolyl, oxazolyl, and thiazolyl. Both aryl and heteroaryl groups may be optionally substituted. For example, M and M' can be selected from the non- limiting group consisting of optionally substituted phenyl, oxazole, and thiazole. In the Formulas herein, M and M' can be independently selected from the list of biodegradable groups above. Unless otherwise specified, aryl or heteroaryl groups described herein refers to both unsubstituted and substituted groups, i.e., optionally substituted aryl or heteroaryl groups. Alkyl, alkenyl, and cyclyl (e.g., carbocyclyl and heterocyclyl) groups may be optionally substituted unless otherwise specified. Optional substituents may be selected from the group consisting of, but are not limited to, a halogen atom (e.g., a chloride, bromide, fluoride, or iodide group), a carboxylic acid (e.g., C(O)OH), an alcohol (e.g., a hydroxyl, OH), an ester (e.g., C(O)OR OC(O)R), an aldehyde (e.g., C(O)H), a carbonyl (e.g., C(O)R, alternatively represented by C=O), an acyl halide (e.g., C(O)X, in which X is a halide selected from bromide, fluoride, chloride, and iodide), a carbonate (e.g., OC(O)OR), an alkoxy (e.g., OR), an acetal (e.g., Attorney Docket No.: 45817-0173WO1 C(OR)2R"", in which each OR are alkoxy groups that can be the same or different and R"" is an alkyl or alkenyl group), a phosphate (e.g., P(O)43-), a thiol (e.g., SH), a sulfoxide (e.g., S(O)R), a sulfinic acid (e.g., S(O)OH), a sulfonic acid (e.g., S(O)2OH), a thial (e.g., C(S)H), a sulfate (e.g., S(O)42-), a sulfonyl (e.g., S(O)2), an amide (e.g., C(O)NR2, or N(R)C(O)R), an azido (e.g., N3), a nitro (e.g., NO2), a cyano (e.g., CN), an isocyano (e.g., NC), an acyloxy (e.g., OC(O)R), an amino (e.g., NR2, NRH, or NH2), a carbamoyl (e.g., OC(O)NR2, OC(O)NRH, or OC(O)NH2), a sulfonamide (e.g., S(O)2NR2, S(O)2NRH, S(O)2NH2, N(R)S(O)2R, N(H)S(O)2R, N(R)S(O)2H, or N(H)S(O)2H), an alkyl group, an alkenyl group, and a cyclyl (e.g., carbocyclyl or heterocyclyl) group. In any of the preceding, R is an alkyl or alkenyl group, as defined herein. In some embodiments, the substituent groups themselves may be further substituted with, for example, one, two, three, four, five, or six substituents as defined herein. For example, a C1-6 alkyl group may be further substituted with one, two, three, four, five, or six substituents as described herein. Compounds of the disclosure that contain nitrogens can be converted to N- oxides by treatment with an oxidizing agent (e.g., 3-chloroperoxybenzoic acid (mCPBA) and / or hydrogen peroxides) to afford other compounds of the disclosure. Thus, all shown and claimed nitrogen-containing compounds are considered, when allowed by valency and structure, to include both the compound as shown and its N-oxide derivative (which can be designated as N O or N+-O). Furthermore, in otherinstances, the nitrogens in the compounds of the disclosure can be converted to N- hydroxy or N-alkoxy compounds. For example, N-hydroxy compounds can be prepared by oxidation of the parent amine by an oxidizing agent such as m CPBA. All shown and claimed nitrogen-containing compounds are also considered, when allowed by valency and structure, to cover both the compound as shown and its N- hydroxy (i.e., N-OH) and N-alkoxy (i.e., N-OR, wherein R is substituted or unsubstituted C1-C6 alkyl, C1-C6 alkenyl, C1-C6 alkynyl, 3-14-membered carbocycle or 3-14-membered heterocycle) derivatives. T cell Engager Structure Attorney Docket No.: 45817-0173WO1 The T cell engagers of this disclosure comprise a binding moiety that binds specifically to human CD3 (e.g., human CD3E) linked to a binding moiety or binding moieties that bind to a tumor associated-antigen (s) (TAA(s)). In certain instances, the TAA is present on a non-solid tumor, such as a hematologic tumor. For example, in one embodiment, the TAA is FCRH5, GPRC5D, or BCMA. The T cell engager also comprises a binding moiety that specifically binds to an agent for the purpose of half- life extension (e.g., a human serum albumin (HSA)). In some instances, the binding moiety that binds specifically to human CD3 (e.g., human CD3E) is a Fab comprising a VH-CH1 and a VL-CL. In certain instances, the binding moieties that bind to a TAA and HSA are VHHs. In one case, the C-terminus of the CH1 of the Fab that binds specifically to human CD3 (e.g., human CD3E) is linked directly or via a linker (e.g., G4S (SEQ ID NO:4)) to the N-terminus of a VHH that binds to a TAA. In certain cases, the C-terminus of that VHH is linked directly or via a linker (e.g., (G4S)3 (SEQ ID NO: 5)) to the N-terminus of another VHH that binds to the same TAA. The two VHHs may be identical or sequence or may have different sequences (e.g., they may bind different epitopes of the same TAA). In some cases, the C- terminus of the CL of the Fab that binds specifically to human CD3 (e.g., human CD3E) is linked directly or via a linker (e.g., G4S (SEQ ID NO:4)) to the N-terminus of a VHH that binds to an agent for the purpose of half-life extension (e.g., HSA). The disclosure features The individual components of these T cell engagers are discussed in more detail below. Anti-CD3 Binding Moiety Cluster of Differentiation 3 (CD3) is a protein complex and T cell co-receptor that is involved in activating both the cytotoxic T cell (CD8+naive T cells) and T helper cells (CD4+naive T cells). It is composed of four distinct chains. In mammals,the complex contains a CD3 chain, a CD3 chain, and two CD3 chains. Thesechains associate with the T-cell receptor (TCR) and the CD3-zeta ( -chain) togenerate an activation signal in T lymphocytes. The TCR, CD3-zeta, and the other CD3 molecules together constitute the TCR complex. Attorney Docket No.: 45817-0173WO1 As part of the TCR-CD3 complex, CD3 epsilon is present on the surface of T- lymphocyte and plays an essential role in the adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains – i.e., CD3 delta (CD3D), CD3 epsilon (CD3E), CD3 gamma (CD3G) and CD3 zeta (CD3Z). All the CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition to this role in signal transduction in T- cell activation, CD3E plays an essential role in T-cell development. It initiates the TCR-CD3 complex assembly by forming the two heterodimers CD3D / CD3E and CD3G / CD3E. It also participates in internalization and cell surface down-regulation of TCR-CD3 complexes via endocytosis sequences present in CD3E cytosolic region. The amino acid sequence of mature full length human CD3E is provided below: DGNEEMGGITQTPYKVSISGTTVILTCPQYPGSEILWQHNDKN IGGDEDDKNIGSDEDHLSLKEFSELEQSGYYVCYPRGSKPEDA NFYLYLRARVCENCMEMDVMSVATIVIVDICITGGLLLLVYY WSKNRKAKAKPVTRGAGAGGRQRGQNKERPPPVPNPDYEPI RKGQRDLYSGLNQRRI (SEQ ID NO:1) The amino acid sequence of mature full length cynomolgus CD3E is provided below: QDGNEEMGSITQTPYQVSISGTTVILTCSQHLGSEAQWQHNGKNKEDSGDRL FLPEFSEMEQSGYYVCYPRGSNPEDASHHLYLKARVCENCMEMDVMAVATI VIVDICITLGLLLLVYYWSKNRKAKAKPVTRGAGAGGRQRGQNKERPPPVPN PDYEPIRKGQQDLYSGLNQRRI (SEQ ID NO:2) The amino acid sequence of the extracellular domain of mature human CD3E is provided below: DGNEEMGGITQTPYKVSISGTTVILTCPQYPGSEILWQHNDKNIGGDEDDKNI GSDEDHLSLKEFSELEQSGYYVCYPRGSKPEDANFYLYLRARVCENCMEMD (SEQ ID NO:3) Attorney Docket No.: 45817-0173WO1 The T cell targeting component of the T cell engagers of this disclosure specifically bind to CD3. In certain instances, the T cell targeting component of the T cell engagers of this disclosure specifically bind to human CD3E. In some instances, the T cell targeting component of the T cell engagers of this disclosure specifically bind to human and cynomolgus CD3E. In certain cases, the T cell targeting component of the T cell engagers of this disclosure specifically bind to the extracellular domain of human CD3E. In some cases, the T cell targeting component of the T cell engagers of this disclosure specifically bind to the extracellular domain of human and cynomolgus CD3E. Provided herein are binding polypeptides (e.g., Fab) that specifically bind to CD3 (e.g., human CD3E) and comprise the six CDRs of an anti-CD3 antibody. Table 2 provides the six CDR sequences of a non-limiting example of an anti-CD3 antibody (humanized SP34) based on common CDR definitions known in the art. V Attorney Docket No.: 45817-0173WO1 This disclosure relates in part to a binding molecule (e.g., Fab) that specifically binds to CD3 (e.g., human and / or cyno CD3) comprising the six CDRs of an anti-CD3 antibody described herein. In some cases, these binding molecules bind CD3E (e.g., human and / or cyno CD3E). In some instances, these binding molecules comprise the six CDRs of an anti-CD3 antibody based on the Kabat definition. In some instances, these binding molecules comprise the six CDRs of an anti-CD3 antibody based on the Chothia definition. In some instances, these binding molecules comprise the six CDRs of an anti-CD3 antibody based on the enhanced Chothia definition. In some instances, these binding molecules comprise the six CDRs of an anti-CD3 antibody based on the contact definition. In some instances, these binding molecules comprise the six CDRs of an anti-CD3 antibody based on the IMGT definition. In some cases, the VH and VL CDRs in Table 2 can include any of the amino acid substitutions of any one or more of SEQ ID NOs.: 54 or 72 to 83 listed in Table 1 of US 2017 / 0355767, which is incorporated by reference herein. This disclosure also relates to binding polypeptides (e.g., Fab) that bind CD3 (e.g., human and / or cyno CD3) comprising the VH and VL of a humanized SP34 described herein. In some cases, these binding polypeptides bind CD3E (e.g., human and / or cyno CD3E). Table 3 provides the amino acid sequences of an exemplary humanized VH and VL of humanized SP34. Table 3: Humanized SP34 VH and VL amino acid sequences S Attorney Docket No.: 45817-0173WO1 In some cases, the VH comprises an amino acid sequence that in association with a VL binds human CD3E and is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:26. In some cases, the VH comprises an amino acid sequence set forth in SEQ ID NO:26, except for 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15 amino acid substitutions, wherein the VH in association with a VL binds human CD3E. In some cases, the VL comprises an amino acid sequence that in association with a VH binds human CD3E and is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:27. In some cases, the VL comprises an amino acid sequence set forth in SEQ ID NOs:27, except for 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acid substitutions, wherein the VL in association with a VH binds human CD3E. In some instances, the variability in the VH and VL, when present, is in the framework regions and not in the CDRs. In some cases, the binding molecule comprises an anti-CD3E binding VH and VL described in WO 2007 / 042261, US 2017 / 0355767, US 10407501, US 9587021, or US 8236308. In other cases, the VH and VL are not any one of the anti-CD3E binding VH or VL described in WO 2007 / 042261, US 2017 / 0355767, US 10407501, US 9587021, or US 8236308. For example, in some instances, this disclosure does not encompass binding molecules comprising the VHs set forth in SEQ ID NOs: 6-9 or the VLs set forth in SEQ ID NOs:10-12 of US 2017 / 0355767. In one instance, the binding polypeptide that binds CD3 (e.g., human CD3E) in the T cell engager is a Fab and comprises a VH comprising the sequence set forth in SEQ ID NO:26 and a VL comprising the sequence set forth in SEQ ID NO:27. In some instances, the C-terminal of the VH is linked directly or via a linker (e.g., peptide, chemical) to a CH1 of a human immunoglobulin (e.g., IgG1, IgG2, IgG3, IgG4). In some cases, the CH1 comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence: Attorney Docket No.: 45817-0173WO1 ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKV (SEQ ID NO:28). In some cases, the CH1 comprises an amino acid sequence that differs from SEQ ID NO:28 at 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 positions a result of amino acid substitutions and / or deletions. In some cases, the C-terminal of the CH1 is linked to an upper hinge region of a human immunoglobulin (e.g., IgG1, IgG2, IgG3, IgG4). In some cases, the upper hinge region comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence: EPKSCDKTHT (SEQ ID NO:29). In some cases, the upper hinge comprises an amino acid sequence that differs from SEQ ID NO:29 at 0, 1, 2, 3, or 4 positions a result of amino acid substitutions and / or deletions. In some instances, the VL is linked directly or via a linker (e.g., peptide, chemical) to a CL of a human immunoglobulin (human lambda or human kappa). In some cases, the CL comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence: GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAG VETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTE C (SEQ ID NO:30). In some cases, the CL comprises an amino acid sequence that differs from SEQ ID NO:30 at 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 positions a result of amino acid substitutions and / or deletions. In some cases, the CL comprises an S or SG at the C- terminus of SEQ ID NO:30 Non-limiting examples of CD3E binding polypeptides are provided in Table 4 below. Table 4: Humanized Anti-CD3 Fab sequences Attorney Docket No.: 45817-0173WO1 In some cases, the VH:CH1:upper hinge construct in association with a VL binds human CD3E and comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:31. In some cases, the VH:CH1:upper hinge construct comprises an amino acid sequence set forth in SEQ ID NO:31, except for 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15 amino acid substitutions, wherein the VH:CH1:upper hinge construct in association with a VL binds human CD3E. In some cases, the VL:CL construct in association with a VH binds human CD3E and comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:32. In some cases, the VL:CL construct comprises an amino acid sequence set forth in SEQ ID NO:32, except for 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acid substitutions, wherein the VL:CL construct in association with a VH binds human CD3E. The variability in the VH:CH1: upper hinge and VL when present is generally in the framework regions, constant region and / or hinge region and not in the CDRs. In some instances, the VH and VL of these constructs are one of the anti-CD3E Attorney Docket No.: 45817-0173WO1 binding VH or VL described in WO 2007 / 042261 or US 2017 / 0355767. In other instances, the VH and VL of these constructs are not any one of the anti-CD3E binding VH or VL described in WO 2007 / 042261 or US 2017 / 0355767. In one instance, the binding polypeptide that binds CD3 (e.g., human CD3E) in the T cell engager is a Fab and comprises the sequences set forth in SEQ ID NO:31 and SEQ ID NO:32. Anti-TAA Binding Moieties The T cell engager molecules of this disclosure also comprise a binding moiety or binding moieties that specifically bind to a TAA. In some instances, the TAA is FCRH5. In other instances, the TAA is GPRC5D. In yet other instances, the TAA is BCMA. In some instances, the T cell engager comprises at least two binding moieties that specifically bind to a TAA. In some cases, the at least two binding moieties have the same amino acid sequence. In other instances, the at least two binding moieties have different amino acid sequences. In some cases, the at least two binding moieties that have different amino acid sequences bind to different epitopes of the same TAA. In certain cases, the binding moieties that specifically bind to a TAA described above are VHHs. In some cases, the C-terminus of the CH1 of the Fab that binds to CD3 is linked directly or via a linker (e.g., G4S (SEQ ID NO:4)) to the N-terminus of a VHH that specifically binds to a TAA. In certain cases, when there are two or more VHHs that bind to a TAA, the VHHs are linked via a linker (e.g., (G4S)3 (SEQ ID NO:5)). In one instance, the Fab polypeptide comprising the VH-CH1 that binds human CD3 is linked via the C-terminal of the CH1 to a linker (e.g., SEQ ID NO:4), the C-terminus of which is linked to the N-terminus of a first VHH that specifically binds to a TAA and the C-terminal of the first VHH is linked via a linker (e.g., SEQ ID NO:5), the C-terminal of which is linked to the N-terminus of a second VHH that specifically binds to a TAA. In some cases, the first and second VHH are identical. In other cases, the first and second VHH are not identical. In some cases, the first and second VHH bind the same TAA but bind different epitopes. In some instances, the Fab polypeptide comprising the VL-CL that binds human CD3 is linked via the C-terminal of the CL to a linker (e.g., SEQ ID NO:4), the C-terminus of Attorney Docket No.: 45817-0173WO1 which is linked to the N-terminus of a first VHH that specifically binds to an agent for the purpose of half-life extension (e.g., HSA). FCRH5 FcRH5 is a cell surface marker enriched on malignant plasma cells when compared to other hematologic malignancies and normal tissues. The amino acid sequence of the extracellular domain of FCRH5 is provided below: QFARTPRPIIFLQPPWTTVFQGERVTLTCKGFRFYSPQKTKWYHRYLGKEILRE TPDNILEVQESGEYRCQAQGSPLSSPVHLDFSSASLILQAPLSVFEGDSVVLRC RAKAEVTLNNTIYKNDNVLAFLNKRTDFHIPHACLKDNGAYRCTGYKESCCP VSSNTVKIQVQEPFTRPVLRASSFQPISGNPVTLTCETQLSLERSDVPLRFRFFR DDQTLGLGWSLSPNFQITAMWSKDSGFYWCKAATMPYSVISDSPRSWIQVQI PASHPVLTLSPEKALNFEGTKVTLHCETQEDSLRTLYRFYHEGVPLRHKSVRC ERGASISFSLTTENSGNYYCTADNGLGAKPSKAVSLSVTVPVSHPVLNLSSPE DLIFEGAKVTLHCEAQRGSLPILYQFHHEGAALERRSANSAGGVAISFSLTAE HSGNYYCTADNGFGPQRSKAVSLSVTVPVSHPVLTLSSAEALTFEGATVTLH CEVQRGSPQILYQFYHEDMPLWSSSTPSVGRVSFSFSLTEGHSGNYYCTADNG FGPQRSEVVSLFVTVPVSRPILTLRVPRAQAVVGDLLELHCEAPRGSPPILYWF YHEDVTLGSSSAPSGGEASFNLSLTAEHSGNYSCEANNGLVAQHSDTISLSVI VPVSRPILTFRAPRAQAVVGDLLELHCEALRGSSPILYWFYHEDVTLGKISAPS GGGASFNLSLTTEHSGIYSCEADNGLEAQRSEMVTLKVAVPVSRPVLTLRAPG THAAVGDLLELHCEALRGSPLILYRFFHEDVTLGNRSSPSGGASLNLSLTAEH SGNYSCEADNGLGAQRSETVTLYITGLTANRSGPFATG (SEQ ID NO:33) In some instances, the T cell engagers of this disclosure comprise a binding moiety that specifically binds to human FCRH5. In some cases, the binding moiety is a VHH. Table 5 provides the three VHH CDR sequences of a non-limiting example of an anti-FCRH5 VHH (FCR460hbest) based on common CDR definitions known in the art. Table 5: CDR Sequences of a VHH that Specifically Binds to FCRH5 (FCR460hbest) Attorney Docket No.: 45817-0173WO1 ) ) R ) This disclosure relates in part to a binding molecule that specifically binds to FCRH5 (e.g., human) comprising the three VHH CDRs of an anti-FCRH5 antibody described herein. In some instances, these binding molecules comprise the three VHH CDRs of an anti-FCRH5 antibody based on the Kabat definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-FCRH5 antibody based on the Chothia definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-FCRH5 antibody based on the enhanced Chothia definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-FCRH5 antibody based on the contact definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-FCRH5 antibody based on the IMGT definition. In some cases, the T cell engager comprises two VHHs that bind to FCRH5, both of which have the same three CDRs. The three CDRs can be based on any one CDR definition set out in Table 5. In one instance, the FCRH5-binding VHH comprises the amino acid sequence provided below (the CDRs based on IMGT definition are underlined): QVQLQESGGGLVQPGGSLRLSCAASGRTYNNYAMGWFRQAPGKEREFVAGI SRSGGMTGYAESVKGRFTISRDNSKNTVYLQMNSLRAEDTAVYYCAAYVGG FSTARRDYSYWGQGTQVTVSS (SEQ ID NO:34) In some cases, the VHH specifically binds to human FCRH5 and comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:34. In some cases, VHH specifically binds to human FCRH5 and comprises an amino acid sequence set forth Attorney Docket No.: 45817-0173WO1 in SEQ ID NO:34, except for 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15 amino acid substitutions. In some instances, the variability in the VHH when present is in the framework regions and not in the CDRs. In some cases, the T cell engager comprises two VHHs that bind to FCRH5. The two VHHs of such a T cell engager may each comprise an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:34. In some cases, the two VHHs are linked via a linker (e.g., SEQ ID NO:5). In certain cases, both VHHs are 100% identical to SEQ ID NO:34. GPRC5D G protein–coupled receptor class C group 5 member D (GPRC5D) is a protein that is highly expressed in multiple myeloma cells. The amino acid sequence of the extracellular domains of GPRC5D are provided below: Extracellular Region 1: MYKDCIESTGDYFLLCDAEGPWGIILE (SEQ ID NO:35) Extracellular Region 2: NQQTAPVRY (SEQ ID NO:36) Extracellular Region 3: TEYVTLIMTRGMMFVNMTPCQLN (SEQ ID NO:37) Extracellular Region 4: RGNPQFQRQPQWDD (SEQ ID NO:38) In some instances, the T cell engagers of this disclosure comprise a binding moiety that specifically binds to GPRC5D. In some cases, the binding moiety is a VHH. Table 6 provides the three VHH CDR sequences of a non-limiting example of an anti-GPRC5D VHH (Seq277h5) based on common CDR definitions known in the art. Table 6: CDR Sequences of a VHH that Specifically Binds to GPRC5D Attorney Docket No.: 45817-0173WO1 ) ) ) This disclosure relates in part to a binding molecule that specifically binds to GPRC5D (e.g., human) comprising the three VHH CDRs of an anti-GPRC5D antibody described herein. In some instances, these binding molecules comprise the three VHH CDRs of an anti-GPRC5D antibody based on the Kabat definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti- GPRC5D antibody based on the Chothia definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-GPRC5D antibody based on the enhanced Chothia definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-GPRC5D antibody based on the contact definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti- GPRC5D antibody based on the IMGT definition. In some cases, the T cell engager comprises two VHHs that bind to GPRC5D, both of which have the same three CDRs. The three CDRs can be based on any one CDR definition set out in Table 6. In one instance, the GPRC5D-binding VHH comprises the amino acid sequence provided below (the CDRs based on IMGT definition are underlined): QVQLVESGGGLVQAGGSLRLSCAASGRTASAYVMGWFRQAPGKERDFVAGI SGGAYYADSVKGRFTIARDNAKNTVYLQMNSLKPEDTAVYYCAAERGMRR LTESYQYDYWGQGTQVTVSS (SEQ ID NO:39) Attorney Docket No.: 45817-0173WO1 In some cases, the VHH specifically binds to human GPRC5D and comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:39. In some cases, VHH specifically binds to human GPRC5D and comprises an amino acid sequence set forth in SEQ ID NO:39, except for 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15 amino acid substitutions. In some instances, the variability in the VHH when present is in the framework regions and not in the CDRs. In some cases, the T cell engager comprises two VHHs that bind to GPRC5D. The two VHHs of such a T cell engager may each comprise an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:39. In some cases, the two VHHs are linked via a linker (e.g., SEQ ID NO:5). In certain cases, both VHHs are 100% identical to SEQ ID NO:39. BCMA B cell maturation protein (BCMA) is a member of the TNF receptor superfamily (TNFRSF17) and its overexpression and activation are associated with MM in preclinical models and humans. The amino acid sequence of the extracellular domain of BCMA is provided below: MLQMAGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKGT NA (SEQ ID NO:40) In some instances, the T cell engagers of this disclosure comprise a binding moiety that specifically binds to BCMA. In some cases, the binding moiety is a VHH. Tables 7 and 8 provides the three VHH CDR sequences of two non-limiting examples of anti-BCMA VHHs (HB2h3 and HB3h9) based on common CDR definitions known in the art. Table 7: CDR Sequences of a VHH that Specifically Binds to BCMA (HB2h3) Attorney Docket No.: 45817-0173WO1 E Table 8: CDR Sequences of another VHH that Specifically Binds to BCMA ) ) ) This disclosure relates in part to a binding molecule that specifically binds to BCMA (e.g., human) comprising the three VHH CDRs of an anti-BCMA antibody described herein. In some instances, these binding molecules comprise the three VHH CDRs of an anti-BCMA antibody based on the Kabat definition. In some Attorney Docket No.: 45817-0173WO1 instances, these binding molecules comprise the three VHH CDRs of an anti-BCMA antibody based on the Chothia definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-BCMA antibody based on the enhanced Chothia definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-BCMA antibody based on the contact definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-BCMA antibody based on the IMGT definition. In some cases, the T cell engager comprises two VHHs that bind to BCMA. The two VHHs of such a T cell engager may comprise a first VHH with three VHH CDRs based on any one CDR definition set forth in Table 7 and a second VHH with three VHH CDRs based on any one CDR definition set forth in Table 8. In some cases, the two VHHs are linked via a linker (e.g., SEQ ID NO:5). In one instance, the BCMA-binding VHH comprises the amino acid sequence provided below (the CDRs based on IMGT definition are underlined): QVQLVESGGGLVQTGGSLRLSCAASGRTLNNYVVAWFRQAPGKEREFVATM WWSGGSPWYSDNVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCAATWV GTSEYRHWGQGTLVTVSS (SEQ ID NO:41) In another instance, the BCMA-binding VHH comprises the amino acid sequence provided below (the CDRs based on IMGT definition are underlined): QVQLVESGGGVVQPGGSLRLSCAASGSIFAYHVMGWYRQAPGKQRELVALI TSGGSTNYTDSVKGRFTISRDNSKNTVYLQMNSLRAEDTAVYYCAIGYYSGS YYWERSGDYWGQGTLVTVSS (SEQ ID NO:42) In some cases, the VHH specifically binds to human BCMA and comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:41 or 42. In some cases, VHH specifically binds to human BCMA and comprises an amino acid sequence set forth in SEQ ID NO:41 or 42, except for 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15 amino acid substitutions. In some instances, the variability in the VHH when present is in the framework regions and not in the CDRs. In some cases, the T cell engager comprises two VHHs that bind to BCMA. The two VHHs of such a T cell engager may comprise a first VHH with an amino Attorney Docket No.: 45817-0173WO1 acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:41 and a second VHH with an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:42. In some cases, the two VHHs are linked via a linker (e.g., SEQ ID NO:5). Anti-HSA Binding Moiety The T cell engagers of this disclosure also comprise a binding moiety that specifically binds to human serum albumin. Such binding moieties are useful to extend the half-life of the T cell engager. In certain instances, the binding moiety that specifically binds to human serum albumin is linked via a linker (e.g., SEQ ID NO:4) to the VL-CL of the Fab that specifically binds to human CD3 (e.g., human CD3E). In one instance, the C-terminus of the CL is linked to linker (e.g., SEQ ID NO:4), the C- terminus of which is linked to the N-terminus of the binding moiety that specifically binds to human serum albumin. In certain cases, the binding moiety that specifically binds to human serum albumin is a VHH. The amino acid sequence of HSA is provided below: MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQ YLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLR ETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEE TFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDE LRDEGKASSAKQGLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLV TDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSH CIAEVENDEMPADLPSLAADFVGSKDVCKNYAEAKDVFLGMFLYEYARRHP DYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQN CELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEA KRMPCAEDCLSVFLNQLCVLHEKTPVSDRVTKCCTESLVNGRPCFSALEVDE TYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAV MDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL (SEQ ID NO:43) Attorney Docket No.: 45817-0173WO1 In some instances, the binding moiety that specifically binds to HSA is a VHH. Table 9 provides the three VHH CDR sequences a non-limiting example of an anti-HSA VHH (VHSA1) based on common CDR definitions known in the art. Table 9: CDR Sequences of a VHH that Specifically Binds to HSA (VHSA1) ) ) ) This disclosure relates in part to a binding molecule that specifically binds to HSA comprising the three VHH CDRs of an anti-HSA antibody described herein. In some instances, these binding molecules comprise the three VHH CDRs of an anti- HSA antibody based on the Kabat definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-HSA antibody based on the Chothia definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-HSA antibody based on the enhanced Chothia definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti- HSA antibody based on the contact definition. In some instances, these binding molecules comprise the three VHH CDRs of an anti-HSA antibody based on the IMGT definition. In some cases, the T cell engager comprises a VHH that bind to HSA which has three CDRs based on any one CDR definition set out in Table 9. In one instance, the HSA-binding VHH comprises the amino acid sequence provided below (the CDRs based on IMGT definition are underlined): EVQLVESGGGLVQPGNSLRLSCAASGFTFSSFGMSWVRQAPGKGLEWVSSIS GSGSDTLYADSVKGRFTISRDNAKTTLYLQMNSLRPEDTAVYYCTIGGSLSRS SQGTLVTVSS (SEQ ID NO:44) Attorney Docket No.: 45817-0173WO1 In some cases, the VHH specifically binds to HSA and comprises an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:44. In some cases, VHH specifically binds to HSA and comprises an amino acid sequence set forth in SEQ ID NO:44, except for 0, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15 amino acid substitutions. In some instances, the variability in the VHH when present is in the framework regions and not in the CDRs. In some cases, the T cell engager comprises a VHH that binds to HSA. The VHH of such a T cell engager may comprise an amino acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to the sequence set forth in SEQ ID NO:44. The C-terminal of the CL of the Fab is linked to the N- terminus of a linker (e.g., SEQ ID NO:4). In some cases, the C-terminal of the linker (e.g., SEQ ID NO:4) is connected to the N-terminus of the VHH. In certain cases, the VHH is 100% identical to SEQ ID NO:44. Linkers The disclosed T cell engagers can contain a linker or linkers, which connect two domains of the T cell engager. In some embodiments, a linker or linkers connect the different binding domains of a T cell engager. In some embodiments, a linker connects a binding domain such as a Fab with a VHH. In some embodiments, a linker connects the C-terminus of a Fab with the N-terminal of a VHH. In some embodiments, a linker connects the C-terminus of a CH1 domain of a Fab with the N- terminal of a VHH. In other embodiments, a linker connects the C-terminus of a CL domain of a Fab with the N-terminal of a VHH. In some embodiments, a T cell engager may comprise two separate linkers, each of which connect different domains of the T cell engager. For example, a first linker connects a Fab and a VHH and a second linker connects the VHHs. The linkers used in the disclosed T cell engagers can be encoded in vivo via expression of an mRNA. The linker may be flexible. The linker may comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, or 50 Attorney Docket No.: 45817-0173WO1 or more amino acids. A linker may comprise glycine (G), serine (S), or various repeats or combinations thereof. Suitable linkers can include, but are not limited to GGGGS (SEQ ID NO: 4); i.e., a “G4S linker”), GSGG (SEQ ID NO:45), GSGGSG (SEQ ID NO:46), GSGGGG (SEQ ID NO:47), GSG, GSGGSGGSGGSGGG (SEQ ID NO:48), GGGSGGGSGG (SEQ ID NO:49), GGGG (SEQ ID NO:50), GGG, SGG, GGGSGGSG (SEQ ID NO:51), GGSGGSGGGS (SEQ ID NO:52), and GGGGGS (SEQ ID NO:53). In some embodiments, the linker comprises GGGGS (SEQ ID NO:4). In other embodiments, the linker comprises (GGGGS)3 (SEQ ID NO:5). In some cases, the linker comprises (GGGGS)n, wherein n = 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 (SEQ ID NO:54). Exemplary T Cell Engager Polypeptides The disclosure features several non-limiting examples of T cell engager polypeptides. Below is the amino acid sequence of a VH:CH1 chain of an Fab that includes VHHs that bind FCRH5 (the linkers are underlined). EVQLVESGGGLVQPGGSLRLSCAASGFTFNTYAMNWVRQAPGKGLEWVARI RSKYNNYATYYADSVKDRFTISRDDSKSILYLQMNNLRAEDTAVYYCARHG NFGNSYVSWFAYWGQGTLVTVSAASTKGPSVFPLAPSSKSTSGGTAALGCLV KDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC NVNHKPSNTKVDKKVEPKSCDKTHTGGGGSQVQLQESGGGLVQPGGSLRLS CAASGRTYNNYAMGWFRQAPGKEREFVAGISRSGGMTGYAESVKGRFTISR DNSKNTVYLQMNSLRAEDTAVYYCAAYVGGFSTARRDYSYWGQGTQVTVS SGGGGSGGGGSGGGGSQVQLQESGGGLVQPGGSLRLSCAASGRTYNNYAM GWFRQAPGKEREFVAGISRSGGMTGYAESVKGRFTISRDNSKNTVYLQMNSL RAEDTAVYYCAAYVGGFSTARRDYSYWGQGTQVTVSS (SEQ ID NO:55) Below is the amino acid sequence of a VH:CH1 chain of a Fab that includes VHHs that bind GPRC5D (the linkers are underlined). EVQLVESGGGLVQPGGSLRLSCAASGFTFNTYAMNWVRQAPGKGLEWVARI RSKYNNYATYYADSVKDRFTISRDDSKSILYLQMNNLRAEDTAVYYCARHG Attorney Docket No.: 45817-0173WO1 NFGNSYVSWFAYWGQGTLVTVSAASTKGPSVFPLAPSSKSTSGGTAALGCLV KDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC NVNHKPSNTKVDKKVEPKSCDKTHTGGGGSQVQLVESGGGLVQPGGSLRLS CAASGRTASAYVMGWFRQAPGKEREFVAGISGGAYYADSVKGRFTISRDNS KNTVYLQMNSLRAEDTAVYYCAAERGMRRLTESYQYDYWGQGTLVTVSSG GGGSGGGGSGGGGSQVQLVESGGGLVQPGGSLRLSCAASGRTASAYVMGW FRQAPGKEREFVAGISGGAYYADSVKGRFTISRDNSKNTVYLQMNSLRAEDT AVYYCAAERGMRRLTESYQYDYWGQGTLVTVSS (SEQ ID NO:56) Below is the amino acid sequence of a VH:CH1 chain of a Fab that includes VHHs that bind BCMA (the linkers are underlined). EVQLVESGGGLVQPGGSLRLSCAASGFTFNTYAMNWVRQAPGKGLEWVARI RSKYNNYATYYADSVKDRFTISRDDSKSILYLQMNNLRAEDTAVYYCARHG NFGNSYVSWFAYWGQGTLVTVSAASTKGPSVFPLAPSSKSTSGGTAALGCLV KDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC NVNHKPSNTKVDKKVEPKSCDKTHTGGGGSQVQLVESGGGLVQTGGSLRLS CAASGRTLNNYVVAWFRQAPGKEREFVATMWWSGGSPWYSDNVKGRFTIS RDNSKNTLYLQMNSLRPEDTAVYYCAATWVGTSEYRHWGQGTLVTVSSGG GGSGGGGSGGGGSQVQLVESGGGVVQPGGSLRLSCAASGSIFAYHVMGWYR QAPGKQRELVALITSGGSTNYTDSVKGRFTISRDNSKNTVYLQMNSLRAEDT AVYYCAIGYYSGSYYWERSGDYWGQGTLVTVSS (SEQ ID NO: 57) Below is the amino acid sequence of a VL:CL chain of a Fab that includes a VHH that binds to HSA (the linker is underlined). QAVVTQEPSLTVSPGGTVTLTCRSSTGAVTTSNYANWVQQKPGQAFRGLIGG TNKRAPGVPARFSGSLIGDKAALTITGAQPEDEAEYFCALWYSNLWVFGGGT KLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSP VKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTV APTECGGGGSEVQLVESGGGLVQPGNSLRLSCAASGFTFSSFGMSWVRQAPG KGLEWVSSISGSGSDTLYADSVKGRFTISRDNAKTTLYLQMNSLRPEDTAVY YCTIGGSLSRSSQGTLVTVSS (SEQ ID NO: 58) The disclosure encompasses T cell engager polypeptides that specifically bind to CD3 (e.g., human CD3E), FCRH5 (e.g., human FCRH5), and HSA, and that have Attorney Docket No.: 45817-0173WO1 at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the sequences set forth in SEQ ID NOs: 55 and 58, respectively. In one instance the T cell engager comprises the sequences set forth in SEQ ID NOs: 55 and 58, respectively. The disclosure also encompasses T cell engager polypeptides that specifically bind to CD3 (e.g., human CD3E), GPRC5D (e.g., human GPRC5D), and HSA, and that have at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the sequences set forth in SEQ ID NOs: 56 and 58, respectively. In one instance the T cell engager comprises the sequences set forth in SEQ ID NOs: 56 and 58, respectively. The disclosure further encompasses T cell engager polypeptides that specifically bind to CD3 (e.g., human CD3E), BCMA (e.g., human BCMA), and HSA, and that have at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to the sequences set forth in SEQ ID NOs: 57 and 58, respectively. In one instance the T cell engager comprises the sequences set forth in SEQ ID NOs: 57 and 58, respectively. In all of the above cases, variability can be achieved by altering the sequence of framework regions of the VH, VL, VHH, and / or by changing the linkers. Nucleic Acids Encoding T cell Engagers The compositions of the disclosure can be administered in protein form, but preferably in the form of nucleic acids which are expressed in vivo. The nucleic acids described herein may be used to deliver any one or more (e.g., 1, 2, 3) of the disclosed T cell engagers to a subject. In some cases nucleic acids (e.g., mRNA) encoding one or more (e.g., 1, 2, 3) of the T cell engagers are provided in the same delivery vehicle (e.g., LNP). These nucleic acids (e.g., RNAs, such as mRNAs) may be used as therapeutic agents to express the T cell engagers of the disclosure as a therapy to treat a target disease (e.g., cancer such as multiple myeloma). The present disclosure provides nucleic acid, such as mRNA, encoding the disclosed T cell engagers. The nucleic acids, such as mRNA, can be used as Attorney Docket No.: 45817-0173WO1 therapeutics, which can be administered to a subject in order to treat a disease. In some cases, the disease is cancer. In one instance, the cancer is a hematological malignancy. In one instance, the cancer is a FCRH5+ cancer. In another instance, the cancer is a GPRC5D+ cancer. In yet another instance, the cancer is a BCMA+ cancer. In one instance, the cancer is a FCRH5+ GPRC5D+ cancer. In one instance, the cancer is a FCRH5+ BCMA+ cancer. In one instance, the cancer is a BCMA+ GPRC5D+ cancer. In one instance, the cancer is multiple myeloma. In some cases, the nucleic acids are used as a second, third, or even later line treatment for relapsed and / or refractory multiple myeloma. The present disclosure provides methods of expressing at least one or multiple (e.g., 2, 3) of the disclosed T cell engagers in vivo in a subject by administering to the subject one or more nucleic acids (e.g., mRNA) that encode the various T cell engagers. The mRNAs encoding one or more of the T cell engagers can be delivered in a lipid nanoparticle. In some cases, mRNAs encoding one, two, or three T cell engagers are administered in a delivery vehicle such as an LNP. In some cases, the lipid nanoparticle comprises an ionizable amino lipid (e.g., Compound 2); a structural lipid (e.g., cholesterol), a phospholipid (e.g., DSPC); and a PEG-lipid (e.g., Compound I). For example, two or more different T cell engagers of the present disclosure can be concurrently expressed in a subject by administering to the subject three or more different mRNAs, e.g.,: a first mRNA encoding a VH-of a Fab that (when paired with the appropriate VL) binds to human CD3 (e.g., human CD3E), the C-terminal of which is linked to one or two or more VHHs that bind to a first TAA (e.g., FCRH5); a second mRNA encoding a VL-of a Fab that (when paired with the appropriate VH) binds to human CD3 (e.g., human CD3E), the C-terminal of which is linked to a binding molecule that binds to a moiety for the purpose of half-life extension (e.g., HSA); and a third mRNA encoding a VH-of a Fab that (when paired with the appropriate VL) binds to human CD3 (e.g., human CD3E), the C-terminal of which is linked to one or two VHHs that bind to a second TAA (e.g., GPRC5D). Each of the polypeptides encoded by the mRNAs coding for the VH-containing Fabs associate Attorney Docket No.: 45817-0173WO1 independently with the VL-containing Fab to form two separate T cell engagers: one of which binds to CD3 and FCRH5 and the second which binds to CD3 and GPRc5D. As will be apparent to those of skill in the art, additional mRNAs can be added to increase the TAA binding potential of the encoded T cell engagers. For instance, another example of T cell engagers involves the following three different mRNAs: a first mRNA encoding a VH-CH1 of a Fab that (when paired with the appropriate VL-CL) binds to human CD3 (e.g., human CD3E), the C-terminal of the CH1 is linked to one or two VHHs that bind to a first TAA (e.g., FCRH5); a second mRNA encoding a VL-CL of a Fab that (when paired with the appropriate VH-CH1) binds to human CD3 (e.g., human CD3E), the C-terminal of the CL is linked to a binding molecule that binds to a moiety for the purpose of half-life extension (e.g., HSA); and a third mRNA encoding a VH-CH1 of a Fab that (when paired with the appropriate VL) binds to human CD3 (e.g., human CD3E), the C- terminal of the CH1 is linked to one or two VHHs that bind to a second TAA (e.g., BCMA). The polypeptides encoded by the mRNAs coding for the VH-CH1 of a Fab that binds to CD3 associate with the VL-CL of a Fab that binds to CD3 to form two separate T cell engagers: one of which binds to CD3, FCRH5, and HSA and the second which binds to CD3, BCMA, and HSA. Yet another example of T cell engagers includes the following three different mRNAs: a first mRNA encoding a VH-CH1 of a Fab that (when paired with the appropriate VL-CL) that binds to human CD3 (e.g., human CD3E), the C-terminal of the CH1 is linked to one or two VHHs that bind to a first TAA (e.g., GPRC5D); a second mRNA encoding a VL-CL of a Fab that (when paired with the appropriate VH-CH1) that binds to human CD3 (e.g., human CD3E), the C-terminal of the CL is linked to a binding molecule that binds to a moiety for the purpose of half-life extension (e.g., HSA); and a third mRNA encoding a VH-CH1 of a Fab that (when paired with the appropriate VL) that binds to human CD3 (e.g., human CD3E), the C- terminal of the CH1 is linked to one or two VHHs that bind to a second TAA (e.g., BCMA). The polypeptides encoded by the mRNAs coding for the VH of a Fab that binds to CD3 associate with the VL of a Fab that binds to CD3 to form two separate T Attorney Docket No.: 45817-0173WO1 cell engagers: one of which binds to CD3,GPRC5D, and HSA and the second which binds to CD3, BCMA, and HSA. In some cases, the disclosure features three different T cell engagers encoded by four mRNAs: a first mRNA encoding a VH-CH1 of a Fab that binds to CD3 associate with the VL-CL of a Fab that binds to CD3 that binds to human CD3 (e.g., human CD3E), the C-terminal of the CH1 is linked to one or two VHHs that bind to a first TAA (e.g., FCRH5); a second mRNA encoding a VL-CL of a Fab that binds to CD3 associate with the VH-CH1 of a Fab that binds to CD3 that binds to human CD3 (e.g., human CD3E), the C-terminal of the CL is linked to a binding molecule that binds to a moiety for the purpose of half-life extension (e.g., HSA); a third mRNA encoding a VH-CH1 of a Fab that binds to CD3 associate with the VL-CL of a Fab that binds to CD3 binds to human CD3 (e.g., human CD3E), the C-terminal of the CH1 is linked to one or two VHHs that bind to a second TAA (e.g., GPRC5D); and a fourth mRNA encoding a VH-CH1 of a Fab that binds to CD3 associate with the VL- CL of a Fab that binds to CD3 that binds to human CD3 (e.g., human CD3E), the C- terminal of the CH1 is linked to one or two VHHs that bind to a third TAA (e.g., BCMA). The polypeptides encoded by the mRNAs coding for the VH-CH1 of a Fab that binds to CD3 associate with the VL-CL of a Fab that binds to CD3 to form three separate T cell engagers: one of which binds to CD3, FCRH5, and HSA. The second of which binds to CD3, GPRC5D, and HSA; and the third which binds to CD3, BCMA and HSA. As these illustrative examples show, the T cell engagers can be combined in various ways, as needed, to successfully target heterologous populations of cancer / tumor cells. As will be appreciated by one of ordinary skill in the art armed with the present disclosure, by employing humanized camelid single domain antibodies (huVHHs) to avoid the issue of mixing light and heavy chains that can occur when expressing a multitude of bispecific antibodies, it is possible to express X number of Fab engager proteins with X + 1 mRNA as shown in FIG.1C Attorney Docket No.: 45817-0173WO1 An example of an open reading frame (ORF) of an mRNA encoding CD3-VH- CH1 linked to two VHHs that bind to FCRH5 is provided below (without the mRNA encoding the signal sequence and wherein all uracils are N1-methylpseudouracils): GAGGUGCAGUUAGUGGAAUCUGGCGGCGGACUGGUUCAACCUGGAGGC AGCCUGCGGCUGUCUUGCGCCGCUUCAGGCUUCACCUUCAACACCUACG CCAUGAACUGGGUGAGACAGGCCCCUGGUAAGGGCCUGGAGUGGGUGG CCAGGAUCCGGAGCAAGUACAACAACUACGCCACCUACUACGCCGAUAG CGUGAAAGACCGGUUCACUAUCAGCAGAGACGACAGCAAGAGCAUCCU GUAUCUCCAGAUGAACAACCUGCGGGCCGAAGAUACCGCCGUGUACUAU UGCGCCCGGCACGGCAACUUCGGCAACAGCUACGUUAGCUGGUUCGCCU ACUGGGGUCAGGGCACCCUGGUGACUGUGUCUGCCGCUAGCACCAAGGG CCCCAGCGUGUUUCCCCUGGCCCCUAGCAGCAAGUCCACCAGCGGAGGC ACCGCAGCUCUGGGCUGCCUGGUGAAGGACUACUUCCCCGAGCCCGUGA CAGUGAGCUGGAACAGCGGCGCCUUGACUAGCGGCGUGCACACCUUCCC CGCCGUGCUCCAGAGCAGCGGCCUGUACAGCCUGAGCAGCGUGGUCACC GUGCCCAGCAGCAGCCUGGGCACCCAGACCUACAUCUGCAACGUGAACC ACAAGCCCAGCAACACCAAGGUGGACAAGAAGGUGGAGCCCAAGUCCUG CGACAAGACCCAUACCGGAGGUGGCGGAAGCCAGGUGCAGCUGCAGGA GAGCGGCGGCGGCCUGGUGCAGCCCGGCGGCAGCCUGAGACUGAGCUGC GCCGCCAGCGGCAGAACCUACAAUAACUACGCAAUGGGCUGGUUCAGAC AGGCGCCAGGCAAGGAGAGAGAGUUCGUGGCCGGCAUCAGCAGAAGCG GCGGCAUGACCGGCUACGCCGAGAGCGUGAAGGGCAGAUUCACGAUCUC ACGAGACAACAGCAAGAACACCGUGUACCUGCAGAUGAACUCACUGAG AGCCGAGGACACAGCUGUGUAUUACUGUGCUGCCUACGUGGGCGGCUU CAGCACCGCCAGAAGAGACUACAGCUACUGGGGCCAGGGCACACAGGUG ACCGUGAGCUCUGGAGGAGGCGGCUCAGGCGGUGGAGGAUCCGGCGGA GGAGGUUCACAGGUCCAGUUACAGGAAUCCGGCGGCGGAUUAGUGCAA CCUGGCGGCUCGCUCCGACUGAGUUGCGCGGCAAGCGGUAGGACUUAUA AUAAUUACGCGAUGGGUUGGUUCAGGCAAGCACCUGGAAAGGAGCGCG AAUUCGUAGCUGGAAUCUCGAGGUCUGGAGGUAUGACGGGAUACGCUG Attorney Docket No.: 45817-0173WO1 CCGUCUACCUGCAAAUGAACUCUCUCCGUGCUGAAGACACUGCCGUAUA CUACUGCGCUGCAUACGUCGGUGGUUUCUCCACCGCGCGGCGGGAUUAU AGCUAUUGGGGCCAAGGCACUCAAGUAACAGUGUCCAGC (SEQ ID NO:60) An example of an open reading frame (ORF) of an mRNA encoding CD3-VH- CH1 linked to two VHHs that bind to GPRC5D is provided below (without the mRNA encoding the signal sequence and wherein all uracils are N1- methylpseudouracils): GAGGUGCAACUGGUGGAAAGCGGUGGAGGUCUGGUGCAGCCGGGCGGU UCCCUGAGGCUGAGCUGCGCCGCAAGCGGCUUCACCUUCAACACCUACG CCAUGAACUGGGUGCGGCAAGCCCCUGGCAAGGGCCUGGAGUGGGUGG CCCGGAUACGGAGCAAGUACAACAACUACGCCACAUACUACGCAGACAG CGUGAAAGACCGGUUCACAAUCAGCCGGGACGACAGUAAGAGCAUCCU GUACCUCCAGAUGAAUAACCUGCGGGCCGAGGACACAGCCGUCUAUUAU UGUGCCCGGCACGGCAACUUCGGCAACAGCUACGUGUCCUGGUUCGCCU ACUGGGGCCAGGGCACACUGGUUACCGUGUCUGCCGCCAGCACCAAGGG CCCCAGCGUGUUCCCACUGGCGCCAAGCAGCAAGUCAACCUCUGGUGGG ACUGCCGCGCUCGGUUGCCUGGUGAAGGACUACUUCCCCGAGCCCGUGA CGGUGAGCUGGAACAGCGGCGCCUUGACCAGCGGCGUGCACACCUUCCC CGCCGUGCUGCAGAGCAGCGGCCUGUACAGCCUGAGCAGCGUGGUGACC GUGCCCAGCAGCAGCCUGGGCACCCAGACCUACAUCUGCAACGUGAACC ACAAGCCCAGCAACACCAAGGUGGACAAGAAGGUGGAGCCCAAGAGCU GCGACAAGACCCACACCGGAGGAGGCGGAAGCCAGGUCCAGCUGGUGGA GUCCGGCGGAGGCCUGGUCCAACCCGGCGGUAGCCUGCGGCUGUCUUGC GCGGCCAGCGGUCGGACAGCAAGCGCCUACGUCAUGGGGUGGUUCCGCC AAGCCCCAGGCAAGGAGAGAGAGUUUGUGGCUGGCAUCAGUGGCGGCG CUUACUACGCUGACAGCGUCAAGGGCAGGUUCACCAUUAGCCGGGAUA ACUCAAAGAAUACCGUAUACCUGCAGAUGAACAGCCUACGGGCCGAAG ACACCGCCGUGUAUUACUGCGCAGCCGAGAGAGGCAUGAGGCGCCUGAC UGAGAGCUAUCAGUACGAUUACUGGGGACAGGGCACCCUCGUGACCGU Attorney Docket No.: 45817-0173WO1 AUCUCAGGUGCAGCUAGUGGAGAGCGGAGGCGGCCUGGUGCAACCCGG AGGCAGCUUGCGCCUGAGCUGUGCAGCCAGUGGCCGGACCGCCUCUGCC UACGUGAUGGGCUGGUUCCGGCAGGCUCCCGGCAAAGAGCGGGAGUUC GUGGCCGGCAUUAGCGGAGGAGCCUACUACGCCGAUAGCGUGAAGGGC CGGUUUACCAUCAGCAGGGACAACUCCAAGAACACCGUGUAUCUGCAAA UGAACUCCCUGCGCGCCGAGGAUACCGCGGUGUACUACUGUGCCGCUGA GCGGGGCAUGCGGCGGCUGACCGAGAGCUACCAGUACGACUAUUGGGG CCAAGGCACCCUGGUGACUGUGAGCAGC (SEQ ID NO:61) An example of an open reading frame (ORF) of an mRNA encoding CD3-VH- CH1 linked to two VHHs that bind to BCMA is provided below (without the mRNA encoding the signal sequence and wherein all uracils are N1-methylpseudouracils): GAGGUGCAGCUAGUCGAGUCUGGCGGCGGGCUAGUGCAACCUGGCGGU AGCCUGCGGUUGUCUUGCGCCGCAAGCGGGUUCACCUUCAACACCUACG CCAUGAACUGGGUACGGCAGGCUCCCGGUAAGGGCCUGGAGUGGGUUG CCCGCAUCCGGAGCAAGUACAACAACUACGCCACCUACUACGCCGACAG UGUGAAAGACCGGUUUACCAUCAGCCGGGACGACAGCAAGAGCAUCCU GUACCUGCAAAUGAACAACCUGCGGGCCGAGGACACAGCUGUGUACUAC UGCGCCCGGCACGGCAACUUCGGCAACAGCUACGUGAGCUGGUUCGCCU ACUGGGGACAGGGCACCCUGGUGACCGUUAGCGCCGCCUCAACCAAGGG GCCCAGCGUGUUUCCCCUGGCCCCUAGCAGCAAGAGCACAAGCGGCGGA ACCGCUGCACUGGGCUGCCUGGUGAAGGACUACUUCCCCGAGCCCGUGA CCGUGAGCUGGAACAGUGGCGCCCUGACCAGUGGCGUGCACACCUUCCC CGCCGUGCUGCAGAGCAGCGGCCUGUACAGCCUGAGCAGCGUGGUGACC GUGCCCAGCAGCAGCCUGGGCACCCAGACCUACAUCUGCAACGUGAACC ACAAGCCCAGCAACACCAAGGUGGACAAGAAGGUGGAGCCCAAGAGCU GCGACAAGACGCAUACAGGAGGCGGAGGCAGCCAGGUGCAGCUGGUGG AAUCAGGUGGCGGCCUGGUGCAGACUGGCGGCUCUCUGCGGCUGAGCU GUGCCGCCAGCGGCAGAACCCUGAACAACUACGUGGUGGCCUGGUUUCG GCAGGCUCCAGGCAAGGAGCGGGAGUUCGUGGCCACCAUGUGGUGGUC CGGCGGAAGCCCUUGGUACAGCGACAACGUGAAGGGCAGAUUCACCAUC Attorney Docket No.: 45817-0173WO1 CGACCCGAGGACACCGCUGUGUACUAUUGUGCCGCCACCUGGGUGGGAA CCAGCGAGUACCGGCAUUGGGGCCAGGGAACUCUGGUGACCGUGUCAA GUGGCGGAGGCGGAUCAGGAGGAGGUGGCUCAGGCGGUGGAGGAAGCC AGGUGCAGUUAGUGGAGAGCGGAGGCGGAGUGGUGCAGCCAGGCGGCA GUCUCCGGUUGUCCUGUGCAGCCAGCGGGAGCAUCUUCGCCUACCACGU GAUGGGCUGGUACAGGCAGGCGCCUGGUAAGCAGCGCGAACUGGUGGC CCUGAUCACCAGCGGCGGCAGCACCAACUACACCGACAGCGUGAAGGGC CGGUUCACAAUCAGCCGGGAUAACAGCAAGAACACCGUGUACCUGCAGA UGAAUAGCCUGCGGGCCGAAGAUACCGCCGUGUACUACUGUGCCAUCGG CUACUACAGCGGCAGCUACUACUGGGAGCGGAGCGGCGACUACUGGGGC CAGGGCACACUGGUGACCGUGAGCAGC (SEQ ID NO:62) An example of an open reading frame (ORF) of an mRNA encoding CD3-VL- CL linked to a VHH that binds to HSA is provided below (without the mRNA encoding the signal sequence and wherein all uracils are N1-methylpseudouracils): CAGGCCGUGGUGACCCAGGAGCCCAGCCUGACUGUGAGCCCCGGAGGCA CAGUGACUCUGACCUGCCGGUCAAGCACAGGCGCGGUGACCACCAGCAA CUACGCCAACUGGGUGCAGCAGAAGCCCGGCCAAGCCUUCCGGGGCCUG AUCGGUGGCACCAACAAACGGGCCCCAGGCGUUCCAGCCCGGUUCUCCG GAUCACUGAUCGGCGACAAGGCCGCCCUGACCAUCACCGGCGCCCAACC CGAAGACGAGGCCGAGUACUUCUGCGCCCUGUGGUACAGCAACCUGUGG GUGUUCGGCGGCGGCACCAAGCUGACCGUGCUGGGCCAGCCCAAGGCAG CGCCCAGCGUGACCCUGUUCCCGCCUAGCAGCGAGGAGCUGCAGGCCAA CAAGGCCACCUUGGUGUGCCUGAUCAGCGACUUCUACCCCGGCGCCGUG ACAGUGGCCUGGAAGGCCGAUAGCAGCCCCGUGAAGGCCGGCGUGGAG ACUACCACCCCUAGCAAGCAGAGCAACAACAAGUACGCCGCAAGCAGCU ACCUGAGCCUGACCCCAGAGCAGUGGAAGAGCCACCGGAGCUACAGCUG CCAGGUGACUCACGAGGGCAGCACCGUGGAGAAGACCGUGGCCCCAACC GAGUGCGGUGGCGGAGGGAGCGAGGUGCAGCUGGUGGAGUCCGGCGGU GGGCUGGUGCAACCAGGCAACAGCCUGCGGCUGAGCUGCGCCGCCAGCG GCUUCACCUUCAGCAGCUUCGGCAUGAGCUGGGUGCGGCAAGCUCCGGG Attorney Docket No.: 45817-0173WO1 CUUAUACGCCGACAGCGUGAAGGGCCGGUUCACCAUCAGCCGGGACAAC GCCAAGACCACCCUGUACCUGCAGAUGAACAGCUUAAGACCCGAGGACA CCGCCGUGUACUACUGCACCAUCGGCGGCAGCCUGAGCCGGAGCAGCCA GGGCACCCUGGUGACCGUGAGCAGC (SEQ ID NO:63) In some instances, the disclosure features mRNAs encoding a T cell engager comprising a first nucleotide sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to a sequence of SEQ ID NO: 60 and a second nucleotide sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to a sequence of SEQ ID NO: 63. In other instances, the disclosure features mRNAs encoding a T cell engager comprising a first nucleotide sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to a sequence of SEQ ID NO: 61 and a second nucleotide sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to a sequence of SEQ ID NO: 63. In yet other instances, the disclosure features mRNAs encoding a T cell engager comprising a first nucleotide sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to a sequence of SEQ ID NO: 62 and a second nucleotide sequence that is at least 80%, at least 85%, at least 90%, at least 95%, or 100% identical to a sequence of SEQ ID NO: 63. In some instances, the disclosure features a population of T cell engagers that bind to one, two, or three different TAAs. In some cases, the mRNAs encoding the T cell engagers further include a signal sequence. Non-limiting examples of nucleic acids encoding signal sequences that can be part of the mRNAs of this disclosure are: AUGGAGACACCCGCCCAGCUGCUGUUCCUGCUACUGCUGUGGCUGCCCG ACACCACAGGC (SEQ ID NO: 65); AUGGAGACGCCCGCCCAGCUGCUGUUCCUGCUGCUCCUGUGGCUGCCCG ACACCACCGGC (SEQ ID NO: 66); AUGGAGACCCCUGCGCAGCUGCUGUUCCUGCUGCUGCUGUGGCUGCCCG ACACCACCGGU (SEQ ID NO: 67); or AUGGAGACUCCCGCCCAGCUGCUGUUCCUGCUGCUUCUGUGGCUGCCCG ACACCACCGGC (SEQ ID NO: 68). Attorney Docket No.: 45817-0173WO1 In some cases, the signal sequence in the mRNA has a nucleic acid sequence that is at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% identical to any one of the sequences set forth in SEQ ID NOs.: 65 to 68. In certain cases, the signal sequence in the mRNA is a nucleic acid sequence that encodes an amino acid sequence that is at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence METPAQLLFLLLLWLPDTTG(SEQ ID NO:131). Using the genetic code and the amino acid sequences encoded by the subject engagers, various nucleotide sequences encoding the engagers of the invention can be designed using methods known in the art. In some instances, the polynucleotide of the present disclosure (e.g., a RNA, e.g., an mRNA) comprises: a 5’ terminal cap (e.g., m7Gp-ppGm-n (where n is an optional nucleoside), e.g., Cap1, or an analog thereof); a 5’ UTR; nucleotide sequences (e.g., ORFs) encoding a secreted T cellengager; a 3 -UTR ; and a poly A tail (e.g., about 100 nucleotides in length). In someinstances, the poly A tail is protected (e.g., with an inverted deoxy-thymidine). In some instances, the poly A tail comprises or consists of A100-UCUAG-A20-inverted deoxy-thymidine (SEQ ID NO: 59). The nucleic acid molecules of the disclosure may include one or more alterations. Herein, in a nucleotide, nucleoside, or polynucleotide (such as the nucleic acids of the disclosure (e.g., an mRNA or an oligonucleotide)), the terms “alteration” or, as appropriate, “alternative” refer to alteration with respect to A, G, U or C ribonucleotides. In one embodiment, the polynucleotide comprises at least one chemically modified nucleobase, e.g., N1-methylpseudouracil or 5-methoxyuracil. In certain instances, all uracils in the polynucleotide are N1-methylpseudouracils. The alterations may be various distinct alterations. In some instances, where the nucleic acid is an mRNA, the coding region, the flanking regions, and / or the terminal regions may contain one, two, or more (optionally different) nucleoside or nucleotide alterations. In some instances, an alternative polynucleotide introduced to a cell may exhibit reduced degradation in the cell, as compared to an unaltered polynucleotide. Attorney Docket No.: 45817-0173WO1 In some instances, an mRNA mass ratio of 4:2:1:4.7 for the individual TAA- specific mRNAs for anti-GPRC5D VHH×anti-CD3 Fab HC, anti-FcRH5 VHH×anti- CD3 Fab HC, anti-BCMA VHH×anti-CD3 Fab HC, and anti-HSA VHH x anti-CD3 Fab LC, respectively, is employed. In certain instances, the four mRNAs are provided as follows: 34% GPRC5D : 17.4% FCRH5 : 8.6% BCMA : 40% LC. Modified Nucleotide Sequences Encoding T cell Engagers In some instances, the polynucleotide (e.g., a RNA, e.g., an mRNA) of the present disclosure comprises a chemically modified nucleobase, for example, a chemically modified uracil, e.g., pseudouracil, N1-methylpseudouracil, 5- methoxyuracil, or the like. In some instances, the mRNA is a uracil-modified sequence comprising an ORF encoding an Engager polypeptide, wherein the mRNA comprises a chemically modified nucleobase, for example, a chemically modified uracil, e.g., pseudouracil, N1-methylpseudouracil, or 5-methoxyuracil. In certain aspects of the present disclosure, when the modified uracil base is connected to a ribose sugar, as it is in polynucleotides, the resulting modified nucleoside or nucleotide is referred to as modified uridine. In some instances, uracil in the polynucleotide is at least about 25%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least 90%, at least 95%, at least 99%, or about 100% modified uracil. In some instances, uracil in the polynucleotide is at least 95% modified uracil. In some instances, uracil in the polynucleotide is 100% modified uracil. In certain instances, uracil in the polynucleotide is 100% N1-methylpseudouracil. In instances where uracil in the polynucleotide is at least 95% modified uracil overall uracil content can be adjusted such that an mRNA provides suitable protein expression levels while inducing little to no immune response. In some instances, the uracil content of the ORF is between about 100% and about 150%, between about 100% and about 110%, between about 105% and about 115%, between about 110% and about 120%, between about 115% and about 125%, between about 120% and about 130%, between about 125% and about 135%, between about 130% and about Attorney Docket No.: 45817-0173WO1 140%, between about 135% and about 145%, between about 140% and about 150% of the theoretical minimum uracil content in the corresponding wild-type ORF (%UTM). In other instances, the uracil content of the ORF is between about 121% and about 136% or between 123% and 134% of the %UTM. In some instances, the uracil content of the ORF encoding an Engager polypeptide is about 115%, about 120%, about 125%, about 130%, about 135%, about 140%, about 145%, or about 150% of the %UTM. In this context, the term "uracil" can refer to modified uracil and / or naturally occurring uracil. In some instances, the uracil content in the ORF of the mRNA encoding an Engager polypeptide of the present disclosure is less than about 30%, about 25%, about 20%, about 15%, or about 10% of the total nucleobase content in the ORF. In some instances, the uracil content in the ORF is between about 10% and about 20% of the total nucleobase content in the ORF. In other instances, the uracil content in the ORF is between about 10% and about 25% of the total nucleobase content in the ORF. In some instances, the uracil content in the ORF of the mRNA encoding an Engager polypeptide is less than about 20% of the total nucleobase content in the open reading frame. In this context, the term "uracil" can refer to modified uracil and / or naturally occurring uracil. In further instances, the ORF of the mRNA encoding an Engager polypeptide having modified uracil and adjusted uracil content has increased Cytosine (C), Guanine (G), or Guanine / Cytosine (G / C) content (absolute or relative). In some instances, the overall increase in C, G, or G / C content (absolute or relative) of the ORF is at least about 2%, at least about 3%, at least about 4%, at least about 5%, at least about 6%, at least about 7%, at least about 10%, at least about 15%, at least about 20%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90%, at least about 95%, or at least about 100% relative to the G / C content (absolute or relative) of the wild-type ORF. In some instances, the G, the C, or the G / C content in the ORF is less than about 100%, less than about 90%, less than about 85%, or less than about 80% of the theoretical maximum G, C, or G / C content of the corresponding wild type nucleotide sequence Attorney Docket No.: 45817-0173WO1 encoding the Engager polypeptide (%GTMX; %CTMX, or %G / CTMX). In some instances, the increases in G and / or C content (absolute or relative) described herein can be conducted by replacing synonymous codons with low G, C, or G / C content with synonymous codons having higher G, C, or G / C content. In other instances, the increase in G and / or C content (absolute or relative) is conducted by replacing a codon ending with U with a synonymous codon ending with G or C. In further instances, the ORF of the mRNA encoding an Engager polypeptide of the present disclosure comprises modified uracil and has an adjusted uracil content containing less uracil pairs (UU) and / or uracil triplets (UUU) and / or uracil quadruplets (UUUU) than the corresponding wild-type nucleotide sequence encoding the Engager polypeptide. In some instances, the ORF of the mRNA encoding an Engager polypeptide of the present disclosure contains no uracil pairs and / or uracil triplets and / or uracil quadruplets. In some instances, uracil pairs and / or uracil triplets and / or uracil quadruplets are reduced below a certain threshold, e.g., no more than 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 occurrences in the ORF of the mRNA encoding the Engager polypeptide. In a particular embodiment, the ORF of the mRNA encoding the Engager polypeptide of the present disclosure contains less than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 non-phenylalanine uracil pairs and / or triplets. In some embodiments, the ORF of the mRNA encoding the Engager polypeptide contains no non-phenylalanine uracil pairs and / or triplets. In further instances, the ORF of the mRNA encoding an Engager polypeptide of the present disclosure comprises modified uracil and has an adjusted uracil content containing fewer uracil-rich clusters than the corresponding wild-type nucleotide sequence encoding the Engager polypeptide. In some instances, the ORF of the mRNA encoding the Engager polypeptide of the present disclosure contains uracil- rich clusters that are shorter in length than corresponding uracil-rich clusters in the corresponding wild-type nucleotide sequence encoding the Engager polypeptide. Attorney Docket No.: 45817-0173WO1 In further instances, alternative lower frequency codons are employed. At least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 55%, at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 99%, or 100% of the codons in the Engager polypeptide–encoding ORF of the modified uracil-comprising mRNA are substituted with alternative codons, each alternative codon having a codon frequency lower than the codon frequency of the substituted codon in the synonymous codon set. The ORF also has adjusted uracil content, as described above. In some instances, at least one codon in the ORF of the mRNA encoding the Engager polypeptide is substituted with an alternative codon having a codon frequency lower than the codon frequency of the substituted codon in the synonymous codon set. Methods for Modifying Polynucleotides The disclosure includes modified polynucleotides comprising a polynucleotide described herein (e.g., a polynucleotide, e.g. mRNA, comprising a nucleotide sequence encoding an Engager polypeptide). The modified polynucleotides can be chemically modified and / or structurally modified. When the polynucleotides of the present disclosure are chemically and / or structurally modified the polynucleotides can be referred to as "modified polynucleotides." The present disclosure provides for modified nucleosides and nucleotides of a polynucleotide (e.g., RNA polynucleotides, such as mRNA polynucleotides) encoding an Engager polypeptide. A "nucleoside" refers to a compound containing a sugar molecule (e.g., a pentose or ribose) or a derivative thereof in combination with an organic base (e.g., a purine or pyrimidine) or a derivative thereof (also referred to herein as "nucleobase"). A “nucleotide" refers to a nucleoside including a phosphate group. Modified nucleotides can be synthesized by any useful method, such as, for example, chemically, enzymatically, or recombinantly, to include one or more modified or non-natural nucleosides. Polynucleotides can comprise a region or Attorney Docket No.: 45817-0173WO1 regions of linked nucleosides. Such regions can have variable backbone linkages. The linkages can be standard phosphodiester linkages, in which case the polynucleotides would comprise regions of nucleotides. The modified polynucleotides disclosed herein can comprise various distinct modifications. In some instances, the modified polynucleotides contain one, two, or more (optionally different) nucleoside or nucleotide modifications. In some instances, a modified polynucleotide, introduced to a cell can exhibit one or more desirable properties, e.g., improved protein expression, reduced immunogenicity, or reduced degradation in the cell, as compared to an unmodified polynucleotide. In some instances, a polynucleotide of the present disclosure (e.g., a polynucleotide comprising a nucleotide sequence encoding an Engager polypeptide) is structurally modified. As used herein, a "structural" modification is one in which two or more linked nucleosides are inserted, deleted, duplicated, inverted or randomized in a polynucleotide without significant chemical modification to the nucleotides themselves. Because chemical bonds will necessarily be broken and reformed to effect a structural modification, structural modifications are of a chemical nature and hence are chemical modifications. However, structural modifications will result in a different sequence of nucleotides. For example, the polynucleotide "ATCG" can be chemically modified to "AT-5meC-G". The same polynucleotide can be structurally modified from "ATCG" to "ATCCCG". Here, the dinucleotide "CC" has been inserted, resulting in a structural modification to the polynucleotide. Therapeutic compositions of the present disclosure comprise, in some instances, at least one nucleic acid (e.g., RNA) having an open reading frame encoding a secreted engager wherein the nucleic acid comprises nucleotides and / or nucleosides that can be standard (unmodified) or modified as is known in the art. In some instances, nucleotides and nucleosides of the present disclosure comprise modified nucleotides or nucleosides. Such modified nucleotides and nucleosides can be naturally-occurring modified nucleotides and nucleosides or non-naturally occurring modified nucleotides and nucleosides. Such modifications can include Attorney Docket No.: 45817-0173WO1 those at the sugar, backbone, or nucleobase portion of the nucleotide and / or nucleoside as are recognized in the art. In some instances, a naturally-occurring modified nucleotide or nucleotide of the disclosure is one as is generally known or recognized in the art. Non-limiting examples of such naturally occurring modified nucleotides and nucleotides can be found, inter alia, in the widely recognized MODOMICS database. In some instances, a non-naturally occurring modified nucleotide or nucleoside of the disclosure is one as is generally known or recognized in the art. Non-limiting examples of such non-naturally occurring modified nucleotides and nucleosides can be found, inter alia, in published US Application Nos. PCT / US2012 / 058519; PCT / US2013 / 075177; PCT / US2014 / 058897; PCT / US2014 / 058891; PCT / US2014 / 070413; PCT / US2015 / 36773; PCT / US2015 / 36759; PCT / US2015 / 36771; or PCT / IB2017 / 051367 all of which are incorporated by reference herein. In some instances, at least one RNA (e.g., mRNA) of the present disclosure is not chemically modified and comprises the standard ribonucleotides consisting of adenosine, guanosine, cytosine and uridine. In some instances, nucleotides and nucleosides of the present disclosure comprise standard nucleoside residues such as those present in transcribed RNA (e.g. A, G, C, or U). In some instances, nucleotides and nucleosides of the present disclosure comprise standard deoxyribonucleosides such as those present in DNA (e.g. dA, dG, dC, or dT). Hence, nucleic acids of the disclosure (e.g., DNA nucleic acids and RNA nucleic acids, such as mRNA nucleic acids) can comprise standard nucleotides and nucleosides, naturally-occurring nucleotides and nucleosides, non-naturally-occurring nucleotides and nucleosides, or any combination thereof. Nucleic acids of the disclosure (e.g., RNA nucleic acids, such as mRNA nucleic acids), in some instances, comprise various (more than one) different types of standard and / or modified nucleotides and nucleosides. In some instances, a particular Attorney Docket No.: 45817-0173WO1 region of a nucleic acid contains one, two or more (optionally different) types of standard and / or modified nucleotides and nucleosides. In some instances, a modified RNA nucleic acid (e.g., a modified mRNA nucleic acid), introduced to a cell or organism, exhibits reduced degradation in the cell or organism, respectively, relative to an unmodified nucleic acid comprising standard nucleotides and nucleosides. In some instances, a modified RNA nucleic acid (e.g., a modified mRNA nucleic acid), introduced into a cell or organism, may exhibit reduced immunogenicity in the cell or organism, respectively (e.g., a reduced innate response) relative to an unmodified nucleic acid comprising standard nucleotides and nucleosides. Nucleic acids (e.g., RNA nucleic acids, such as mRNA nucleic acids), in some instances, comprise non-natural modified nucleotides that are introduced during synthesis or post-synthesis of the nucleic acids to achieve desired functions or properties. The modifications may be present on internucleotide linkages, purine or pyrimidine bases, or sugars. The modification may be introduced with chemical synthesis or with a polymerase enzyme at the terminal of a chain or anywhere else in the chain. Any of the regions of a nucleic acid may be chemically modified. The present disclosure provides for modified nucleosides and nucleotides of a nucleic acid (e.g., RNA nucleic acids, such as mRNA nucleic acids). A “nucleoside” refers to a compound containing a sugar molecule (e.g., a pentose or ribose) or a derivative thereof in combination with an organic base (e.g., a purine or pyrimidine) or a derivative thereof (also referred to herein as “nucleobase”). A “nucleotide” refers to a nucleoside, including a phosphate group. Modified nucleotides may by synthesized by any useful method, such as, for example, chemically, enzymatically, or recombinantly, to include one or more modified or non-natural nucleosides. Nucleic acids can comprise a region or regions of linked nucleosides. Such regions may have variable backbone linkages. The linkages can be standard phosphodiester linkages, in which case the nucleic acids would comprise regions of nucleotides. Attorney Docket No.: 45817-0173WO1 Modified nucleotide base pairing encompasses not only the standard adenosine-thymine, adenosine-uracil, or guanosine-cytosine base pairs, but also base pairs formed between nucleotides and / or modified nucleotides comprising non- standard or modified bases, wherein the arrangement of hydrogen bond donors and hydrogen bond acceptors permits hydrogen bonding between a non-standard base and a standard base or between two complementary non-standard base structures, such as, for example, in those nucleic acids having at least one chemical modification. One example of such non-standard base pairing is the base pairing between the modified nucleotide inosine and adenine, cytosine or uracil. Any combination of base / sugar or linker may be incorporated into nucleic acids of the present disclosure. In some instances, modified nucleobases in nucleic acids (e.g., RNA nucleicacids, such as mRNA nucleic acids) comprise N1-methyl-pseudouridine (m1 ), 1-ethyl-pseudouridine (e1 ), 5-methoxy-uridine (mo5U), 5-methyl-cytidine (m5C),and / or pseudouridine ( ). In some instances, modified nucleobases in nucleic acids(e.g., RNA nucleic acids, such as mRNA nucleic acids) comprise 5-methoxymethyl uridine, 5-methylthio uridine, 1-methoxymethyl pseudouridine, 5-methyl cytidine, and / or 5-methoxy cytidine. In some instances, the polyribonucleotide includes a combination of at least two (e.g., 2, 3, 4 or more) of any of the aforementioned modified nucleobases, including but not limited to chemical modifications. In some instances, a RNA nucleic acid of the disclosure comprises N1-methyl-pseudouridine (m1 ) substitutions at one or more or all uridine positions of thenucleic acid. In some instances, a RNA nucleic acid of the disclosure comprises N1-methyl-pseudouridine (m1 ) substitutions at one or more or all uridine positions of thenucleic acid and 5-methyl cytidine substitutions at one or more or all cytidine positions of the nucleic acid. In some instances, a RNA nucleic acid of the disclosure comprisespseudouridine ( ) substitutions at one or more or all uridine positions of the nucleicacid. Attorney Docket No.: 45817-0173WO1 In some instances, a RNA nucleic acid of the disclosure comprisespseudouridine ( ) substitutions at one or more or all uridine positions of the nucleicacid and 5-methyl cytidine substitutions at one or more or all cytidine positions of the nucleic acid. In some instances, a RNA nucleic acid of the disclosure comprises uridine at one or more or all uridine positions of the nucleic acid. In some instances, nucleic acids (e.g., RNA nucleic acids, such as mRNA nucleic acids) are uniformly modified (e.g., fully modified, modified throughout the entire sequence) for a particular modification. For example, a nucleic acid can be uniformly modified with N1-methyl-pseudouridine, meaning that all uridine residues in the mRNA sequence are replaced with N1-methyl-pseudouridine. Similarly, a nucleic acid can be uniformly modified for any type of nucleoside residue present in the sequence by replacement with a modified residue such as those set forth above. The nucleic acids of the present disclosure may be partially or fully modified along the entire length of the molecule. For example, one or more or all or a given type of nucleotide (e.g., purine or pyrimidine, or any one or more or all of A, G, U, C) may be uniformly modified in a nucleic acid of the disclosure, or in a predetermined sequence region thereof (e.g., in the mRNA including or excluding the poly A tail). In some instances, all nucleotides X in a nucleic acid of the present disclosure (or in a sequence region thereof) are modified nucleotides, wherein X may be any one of nucleotides A, G, U, C, or any one of the combinations A+G, A+U, A+C, G+U, G+C, U+C, A+G+U, A+G+C, G+U+C or A+G+C. The nucleic acid may contain from about 1% to about 100% modified nucleotides (either in relation to overall nucleotide content, or in relation to one or more types of nucleotide, i.e., any one or more of A, G, U or C) or any intervening percentage (e.g., from 1% to 20%, from 1% to 25%, from 1% to 50%, from 1% to 60%, from 1% to 70%, from 1% to 80%, from 1% to 90%, from 1% to 95%, from 10% to 20%, from 10% to 25%, from 10% to 50%, from 10% to 60%, from 10% to 70%, from 10% to 80%, from 10% to 90%, from 10% to 95%, from 10% to 100%, Attorney Docket No.: 45817-0173WO1 from 20% to 25%, from 20% to 50%, from 20% to 60%, from 20% to 70%, from 20% to 80%, from 20% to 90%, from 20% to 95%, from 20% to 100%, from 50% to 60%, from 50% to 70%, from 50% to 80%, from 50% to 90%, from 50% to 95%, from 50% to 100%, from 70% to 80%, from 70% to 90%, from 70% to 95%, from 70% to 100%, from 80% to 90%, from 80% to 95%, from 80% to 100%, from 90% to 95%, from 90% to 100%, and from 95% to 100%). It will be understood that any remaining percentage is accounted for by the presence of unmodified A, G, U, or C. The nucleic acids may contain at a minimum 1% and at maximum 100% modified nucleotides, or any intervening percentage, such as at least 5% modified nucleotides, at least 10% modified nucleotides, at least 25% modified nucleotides, at least 50% modified nucleotides, at least 80% modified nucleotides, or at least 90% modified nucleotides. For example, the nucleic acids may contain a modified pyrimidine such as a modified uracil or cytosine. In some instances, at least 5%, at least 10%, at least 25%, at least 50%, at least 80%, at least 90% or 100% of the uracil in the nucleic acid is replaced with a modified uracil (e.g., a 5-substituted uracil). The modified uracil can be replaced by a compound having a single unique structure, or can be replaced by a plurality of compounds having different structures (e.g., 2, 3, 4 or more unique structures). In some instances, at least 5%, at least 10%, at least 25%, at least 50%, at least 80%, at least 90% or 100% of the cytosine in the nucleic acid is replaced with a modified cytosine (e.g., a 5-substituted cytosine). The modified cytosine can be replaced by a compound having a single unique structure, or can be replaced by a plurality of compounds having different structures (e.g., 2, 3, 4 or more unique structures). Messenger RNA The present disclosure features compositions including two or more mRNAs, where each pair of mRNAs encodes at least one (e.g., 2, 4, 6, or more) T cell engager as described herein. mRNAs of the disclosure may each include (i) a 5’-cap structure; (ii) a 5’-UTR; (iii) an open reading frame encoding a polypeptide of the T cell engager; (iv) a 3’-untranslated region (3’-UTR); and (v) a poly A region. Attorney Docket No.: 45817-0173WO1 In some instances, the mRNA includes from about 30 to about 3,000 (e.g., from 30 to 50, from 30 to 100, from 30 to 250, from 30 to 500, from 30 to 750, from 30 to 1,000, from 30 to 1,500, from 30 to 2,000, from 30 to 2,500, from 50 to 100, from 50 to 250, from 50 to 500, from 50 to 750, from 50 to 1,000, from 50 to 1,500, from 50 to 2,000, from 50 to 2,500, from 50 to 3,000, from 100 to 500, from 100 to 750, from 100 to 1,000, from 100 to 1,500, from 100 to 2,000, from 100 to 2,500, from 100 to 3,000, from 500 to 750, from 500 to 1,000, from 500 to 1,500, from 500 to 2,000, from 500 to 2,500, from 500 to 3,000, from 1,000 to 1,500, from 1,000 to 2,000, from 1,000 to 2,500, from 1,000 to 3,000, from 1,500 to 2,000, from 1,500 to 2,500, from 1,500 to 3,000, from 2,000 to 3,000, from 2,000 to 2,500, or from 2,500 to 3,000) nucleotides. More specifically, provided herein are nucleic acids that encode T cell engagers of the disclosure. Any of the proteins disclosed herein may be encoded by an open reading frame (ORF) of an mRNA(s). In some instances, the ORF of the mRNA of a T cell engager that, when assembled, binds to CD3, FCRH5, and HSA comprises a nucleic acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequences set forth in SEQ ID NOs.: 60 and 63 (wherein all uracils are N1-methylpseudouracils). In other instances, the ORF of the mRNA of a T cell engager that, when assembled, binds CD3, GPRC5D, and HSA comprises a nucleic acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequences set forth in SEQ ID NOs.: 61 and 63 (wherein all uracils are N1-methylpseudouracils). In yet other instances, the ORF of the mRNA of a T cell engager that, when assembled, binds CD3, BCMA, and HSA comprises a nucleic acid sequence that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequences set forth Attorney Docket No.: 45817-0173WO1 in SEQ ID NOs.: 62 and 63 (wherein all uracils are N1-methylpseudouracils). It should be noted that these ORFs may further include a signal sequence. Similar such open reading frames can be designed from the protein sequences disclosed herein using the genetic code and the codon optimization strategies known to one of ordinary skill in the art. Untranslated Regions (UTRs) Untranslated regions (UTRs) are nucleic acid sections of a polynucleotidebefore a start codon (5 UTR) and after a stop codon (3 UTR) that are not translated.In some instances, a polynucleotide (e.g., a ribonucleic acid (RNA), e.g., a messenger RNA (mRNA)) of the present disclosure comprising an open reading frame (ORF)encoding an Engager polypeptide further comprises a UTR (e.g., a 5 UTR orfunctional fragment thereof, a 3 UTR or functional fragment thereof, or acombination thereof). AUTR (e.g., 5 UTR or 3 UTR) can be homologous or heterologous to thecoding region in a polynucleotide. In some instances, the UTR is homologous to the ORF encoding the Engager polypeptide. In some instances, the UTR is heterologous to the ORF encoding the Engager polypeptide. In some instances, the polynucleotide comprises one 5 UTR or a functionalfragment thereof. In some instances, the polynucleotide comprises one 3 UTR or afunctional fragment thereof. In some instances, the 5 UTR or functional fragment thereof, 3 UTR orfunctional fragment thereof, or any combination thereof is sequence optimized. In some instances, the 5 UTR or functional fragment thereof, 3 UTR orfunctional fragment thereof, or any combination thereof comprises at least one chemically modified nucleobase, e.g., N1-methylpseudouracil or 5-methoxyuracil. Attorney Docket No.: 45817-0173WO1 UTRs can have features that provide a regulatory role, e.g., increased or decreased stability, localization and / or translation efficiency. A polynucleotide comprising a UTR can be administered to a cell, tissue, or organism, and one or more regulatory features can be measured using routine methods. In some instances, afunctional fragment of a 5 UTR or 3 UTR comprises one or more regulatory featuresof a full length 5 or 3 UTR, respectively.Natural 5 UTRs bear features that play roles in translation initiation. Theyharbor signatures like Kozak sequences that are commonly known to be involved in the process by which the ribosome initiates translation of many genes. Kozak sequences have the consensus CCR(A / G)CCAUGG, where R is a purine (adenine or guanine) three bases upstream of the start codon (AUG), which is followed by another‘G’. 5 UTRs also have been known to form secondary structures that are involved inelongation factor binding. By engineering the features typically found in abundantly expressed genes of specific target organs, one can enhance the stability and protein production of apolynucleotide. For example, introduction of 5 UTR of liver-expressed mRNA, suchas albumin, serum amyloid A, Apolipoprotein A / B / E, transferrin, alpha fetoprotein, erythropoietin, or Factor VIII, can enhance expression of polynucleotides in hepaticcell lines or liver. Likewise, use of 5 UTR from other tissue-specific mRNA toimprove expression in that tissue is possible for muscle (e.g., MyoD, Myosin, Myoglobin, Myogenin, Herculin), for endothelial cells (e.g., Tie-1, CD36), for myeloid cells (e.g., C / EBP, AML1, G-CSF, GM-CSF, CD11b, MSR, Fr-1, i-NOS), for leukocytes (e.g., CD45, CD18), for adipose tissue (e.g., CD36, GLUT4, ACRP30, adiponectin) and for lung epithelial cells (e.g., SP-A / B / C / D). In some instances, UTRs are selected from a family of transcripts whose proteins share a common function, structure, feature or property. For example, an encoded polypeptide can belong to a family of proteins (i.e., that share at least one function, structure, feature, localization, origin, or expression pattern), which are expressed in a particular cell, tissue or at some time during development. The UTRs Attorney Docket No.: 45817-0173WO1 from any of the genes or mRNA can be swapped for any other UTR of the same or different family of proteins to create a new polynucleotide. In some instances, the 5 UTR and the 3 UTR can be heterologous. In someinstances, the 5 UTR can be derived from a different species than the 3 UTR. Insome instances, the 3 UTR can be derived from a different species than the 5 UTR.Co-owned International Patent Application No. PCT / US2014 / 021522 (Publ. No. WO / 2014 / 164253, incorporated herein by reference in its entirety) provides a listing of exemplary UTRs that can be utilized in the polynucleotide of the present disclosure as flanking regions to an ORF. Additional exemplary UTRs of the application include, but are not limited to,one or more 5 UTR and / or 3 UTR derived from the nucleic acid sequence of: a globin,such as an - or -globin (e.g., a Xenopus, mouse, rabbit, or human globin); a strong Kozak translational initiation signal; a CYBA (e.g., human cytochrome b-245polypeptide); an albumin (e.g., human albumin7); a HSD17B4 (hydroxysteroid (17- )dehydrogenase); a virus (e.g., a tobacco etch virus (TEV), a Venezuelan equine encephalitis virus (VEEV), a Dengue virus (DENV), a cytomegalovirus (CMV) (e.g., CMV immediate early 1 (IE1)), a hepatitis virus (e.g., hepatitis B virus), a sindbis virus, or a PAV barley yellow dwarf virus); a heat shock protein (e.g., Hsp70); a translation initiation factor (e.g., elF4G); a glucose transporter (e.g., hGLUT1 (human glucose transporter 1)); an actin (e.g., human or actin); a GAPDH; a tubulin; ahistone; a citric acid cycle enzyme; a topoisomerase (e.g., a 5 UTR of a TOP genelacking the 5 TOP motif (the oligopyrimidine tract)); a ribosomal protein Large 32(L32); a ribosomal protein (e.g., human or mouse ribosomal protein, such as, for example, rps9); an ATP synthase (e.g., ATP5A1 or the subunit of mitochondrial H+- ATP synthase); a growth hormone (e.g., bovine (bGH) or human (hGH)); an elongation factor (e.g., elongation factor 1 1 (EEF1A1)); a manganese superoxide dismutase (MnSOD); a myocyte enhancer factor 2A (MEF2A); a -F1-ATPase, a creatine kinase, a myoglobin, a granulocyte-colony stimulating factor (G-CSF); a collagen (e.g., collagen type I, alpha 2 (Col1A2), collagen type I, alpha 1 (Col1A1), Attorney Docket No.: 45817-0173WO1 collagen type VI, alpha 2 (Col6A2), collagen type VI, alpha 1 (Col6A1)); a ribophorin (e.g., ribophorin I (RPNI)); a low density lipoprotein receptor-related protein (e.g., LRP1); a cardiotrophin-like cytokine factor (e.g., Nnt1); calreticulin (Calr); a procollagen-lysine, 2-oxoglutarate 5-dioxygenase 1 (Plod1); and a nucleobindin (e.g., Nucb1). In some instances, the 5 UTR is selected from the group consisting of a -globin 5 UTR; a 5 UTR containing a strong Kozak translational initiation signal; acytochrome b-245 polypeptide (CYBA) 5 UTR; a hydroxysteroid (17- )dehydrogenase (HSD17B4) 5 UTR; a Tobacco etch virus (TEV) 5 UTR; aVenezuelan equine encephalitis virus (VEEV) 5 UTR; a 5 proximal open readingframe of rubella virus (RV) RNA encoding nonstructural proteins; a Dengue virus(DEN) 5 UTR; a heat shock protein 70 (Hsp70) 5 UTR; a eIF4G 5 UTR; a GLUT15 UTR; functional fragments thereof and any combination thereof.In some embodiment, the mRNA comprises a 5’-UTR comprising a nucleic acid sequence of (wherein all uracils are N1-methylpseudouracils) AGGAAAUCGCAAAAUUUGCUCUUCGCGUUAGAUUUCUUUUAGUUUUCU CGCAACUAGCAAGCUUUUUGUUCUCGCC (SEQ ID NO: 64). In some embodiment, the mRNA comprises a 3’-UTR comprising any one of the following nucleic acid sequences (wherein all uracils are N1-methylpseudouracils) UAAAGCUCCCCGGGGGCCUCGGUGGCCUAGCUUCUUGCCCCUUGGGCCU CCCCCCAGCCCCUCCUCCCCUUCCUGCAGGGCUUGUAUAAAGUGGUCUU UGAAUAAAGUCUGAGUGGGCGGC (SEQ ID NO: 127); UAAAGCUCCCCGGGGGCCUCGGUGGCCUAGCUUCUUGCCCCUUGGGCCU CCCCCCAGCCCCUCCUCCCCUUCCUGCAAUAAAUUAAUUAUUUGUGGUC UUUGAAUAAAGUCUGAGUGGGCGGC (SEQ ID NO: 128); UAAAGCUCCCCGGGGGCCUCGGUGGCCUAGCUUCUUGCCCCUUGGGCCU CCCCCCAGCCCCUCCUCCCCUUCCUGCAAAGAAAUAAAUAAAUUUGUGG UCUUUGAAUAAAGUCUGAGUGGGCGGC (SEQ ID NO: 129); or Attorney Docket No.: 45817-0173WO1 UAAAGCUCCCCGGGGGCCUCGGUGGCCUAGCUUCUUGCCCCUUGGGCCU CCCCCCAGCCCCUCCUCCCCUUCCUGCAUUUGUAAUAAAUAAAUAAAGU GGUCUUUGAAUAAAGUCUGAGUGGGCGGC (SEQ ID NO: 130). In some instances, the 3 UTR is selected from the group consisting of a -globin 3 UTR; a CYBA 3 UTR; an albumin 3 UTR; a growth hormone (GH) 3UTR; a VEEV 3 UTR; a hepatitis B virus (HBV) 3 UTR; -globin 3 UTR; a DEN 3UTR; a PAV barley yellow dwarf virus (BYDV-PAV) 3 UTR; an elongation factor 11 (EEF1A1) 3 UTR; a manganese superoxide dismutase (MnSOD) 3 UTR; asubunit of mitochondrial H(+)-ATP synthase ( -mRNA) 3 UTR; a GLUT1 3 UTR; aMEF2A 3 UTR; a -F1-ATPase 3 UTR; functional fragments thereof, andcombinations thereof. Wild-type UTRs derived from any gene or mRNA can be incorporated into the polynucleotides of the present disclosure. In some instances, a UTR can be altered relative to a wild type or native UTR to produce a variant UTR, e.g., by changing the orientation or location of the UTR relative to the ORF; or by inclusion of additional nucleotides, deletion of nucleotides, swapping or transposition of nucleotides. Insome instances, variants of 5 or 3 UTRs can be utilized, for example, mutants of wildtype UTRs, or variants wherein one or more nucleotides are added to or removed from a terminus of the UTR. Additionally, one or more synthetic UTRs can be used in combination with one or more non-synthetic UTRs. See, e.g., Mandal and Rossi, Nat. Protoc.2013 8(3):568-82, the contents of which are incorporated herein by reference in their entirety. UTRs or portions thereof can be placed in the same orientation as in the transcript from which they were selected or can be altered in orientation or location.Hence, a 5 and / or 3 UTR can be inverted, shortened, lengthened, or combined withone or more other 5 UTRs or 3 UTRs.In some instances, the polynucleotide comprises multiple UTRs, e.g., adouble, a triple or a quadruple 5 UTR or 3 UTR. For example, a double UTR Attorney Docket No.: 45817-0173WO1 comprises two copies of the same UTR either in series or substantially in series. Forexample, a double beta-globin 3 UTR can be used (see US2010 / 0129877, the contentsof which are incorporated herein by reference in its entirety). The polynucleotides of the present disclosure can comprise combinations offeatures. For example, the ORF can be flanked by a 5 UTR that comprises a strongKozak translational initiation signal and / or a 3 UTR comprising an oligo(dT)sequence for templated addition of a poly A tail. A 5 UTR can comprise a firstpolynucleotide fragment and a second polynucleotide fragment from the same and / or different UTRs (see, e.g., US2010 / 0293625, herein incorporated by reference in its entirety). Other non-UTR sequences can be used as regions or subregions within the polynucleotides of the present disclosure. For example, introns or portions of intron sequences can be incorporated into the polynucleotides of the present disclosure. Incorporation of intronic sequences can increase protein production as well as polynucleotide expression levels. In some instances, the polynucleotide of the present disclosure comprises an internal ribosome entry site (IRES) instead of or in addition to a UTR (see, e.g., Yakubov et al., Biochem. Biophys. Res. Commun.2010 394(1):189-193, the contents of which are incorporated herein by reference in theirentirety). In some instances, the polynucleotide comprises an IRES instead of a 5UTR sequence. In some instances, the polynucleotide comprises an ORF and a viralcapsid sequence. In some instances, the polynucleotide comprises a synthetic 5 UTRin combination with a non-synthetic 3 UTR.In some instances, the UTR can also include at least one translation enhancer polynucleotide, translation enhancer element, or translational enhancer elements (collectively, "TEE," which refers to nucleic acid sequences that increase the amount of polypeptide or protein produced from a polynucleotide. As a non-limiting example, the TEE can be located between the transcription promoter and the start codon. Insome instances, the 5 UTR comprises a TEE. Attorney Docket No.: 45817-0173WO1 In one aspect, a TEE is a conserved element in a UTR that can promote translational activity of a nucleic acid such as, but not limited to, cap-dependent or cap-independent translation. 5UTR sequences5 UTR sequences are important for ribosome recruitment to the mRNA andhave been reported to play a role in translation (Hinnebusch A, et al., (2016) Science, 352:6292: 1413-6). Disclosed herein, inter alia, are polynucleotide, e.g., mRNAs, comprising open reading frames (e.g., any of SEQ ID NOs: 60 and 63, 61 and 63, and 62 and 63)encoding an Engager polypeptide, which polynucleotides have a 5 UTR that confersan increased half-life, increased expression and / or increased activity of the polypeptide encoded by said polynucleotide, or of the polynucleotide itself. In someinstances, a polynucleotide disclosed herein comprises: (a) a 5 -UTR (e.g., asprovided in Table 10 or a variant or fragment thereof); (b) a coding region comprisinga stop element (e.g., as described herein); and (c) a 3 -UTR (e.g., as described herein),and LNP compositions comprising the same. In some instances, the polynucleotidecomprises a 5 -UTR comprising a sequence provided in Table 10 or a variant orfragment thereof (e.g., a functional variant or fragment thereof). In some instances, the polynucleotide having a 5 UTR sequence provided inTable 10 or a variant or fragment thereof, has an increase in the half-life of the polynucleotide, e.g., about 1.5-20-fold increase in half-life of the polynucleotide. In some instances, the increase in half-life is about 1.5-, 2-, 3-, 4-, 5-, 6-, 7-, 8-, 9-, 10-, 11-, 12-, 13-, 14-, 15-, 16-, 17-, 18-, 19- or 20-fold, or more. In some instances, the increase in half life is about 1.5-fold or more. In some instances, the increase in half life is about 2-fold or more. In some instances, the increase in half life is about 3-fold or more. In some instances, the increase in half life is about 4-fold or more. In some instances, the increase in half life is about 5-fold or more. Attorney Docket No.: 45817-0173WO1 In some instances, the polynucleotide having a 5 UTR sequence provided inTable 10 or a variant or fragment thereof, results in an increased level and / or activity, e.g., output, of the polypeptide encoded by the polynucleotide. In some instances, the5 UTR results in about 1.5-20-fold increase in level and / or activity, e.g., output, of thepolypeptide encoded by the polynucleotide. In some instances, the increase in level and / or activity is about 1.5-, 2-, 3-, 4-, 5-, 6-, 7-, 8-, 9-, 10-, 11-, 12-, 13-, 14-, 15-, 16- , 17-, 18-, 19- or 20-fold, or more. In some instances, the increase in level and / or activity is about 1.5-fold or more. In some instances, the increase in level and / or activity is about 2-fold or more. In some instances, the increase in level and / or activity is about 3-fold or more. In some instances, the increase in level and / or activity is about 4-fold or more. In some instances, the increase in level and / or activity is about 5-fold or more. In some instances, the increase is compared to an otherwise similarpolynucleotide which does not have a 5 UTR, has a different 5 UTR, or does nothave a 5 UTR described in, SEQ ID NO:64, Table 10 or a variant or fragmentthereof. In some instances, the increase in half-life of the polynucleotide is measured according to an assay that measures the half-life of a polynucleotide. In some instances, the increase in level and / or activity, e.g., output, of the polypeptide encoded by the polynucleotide is measured according to an assay that measures the level and / or activity of a polypeptide. In some instances, the 5 UTR comprises a sequence provided in SEQ IDNO:64, Table 10 or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%,99% or 100% identity to a 5 UTR sequence provided in SEQ ID NO:64, Table 10,or a variant or a fragment thereof. In some instances, the 5 UTR comprises asequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 64, SEQ ID NO: 69, SEQ ID NO: 70, SEQ ID NO: 71, SEQ ID NO: 72, SEQ ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 76, SEQ ID NO: 77, or SEQ ID NO: 78. Attorney Docket No.: 45817-0173WO1 In some instances, the 5 UTR comprises a sequence with at least 80%, 85%,90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 64. In someinstances, the 5 UTR comprises a sequence with at least 80%, 85%, 90%, 95%, 96%,97%, 98%, 99% or 100% identity to SEQ ID NO: 69. In some instances, the 5 UTRcomprises a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or100% identity to SEQ ID NO: 70. In some instances, the 5 UTR comprises asequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identityto SEQ ID NO: 71. In some instances, the 5 UTR comprises a sequence with at least80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 72. Insome instances, the 5 UTR comprises a sequence with at least 80%, 85%, 90%, 95%,96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 73. In some instances, the 5UTR comprises a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%or 100% identity to SEQ ID NO: 74. In some instances, the 5 UTR comprises asequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identityto SEQ ID NO: 75. In some instances, the 5 UTR comprises a sequence with at least80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 76. Insome instances, the 5 UTR comprises a sequence with at least 80%, 85%, 90%, 95%,96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 77. In some instances, the 5UTR comprises a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 78. In some instances, the 5 UTR comprises the sequence of SEQ ID NO: 64. Insome instances, the 5 UTR consists of the sequence of SEQ ID NO: 64. In someinstances, the 5 UTR comprises the sequence of SEQ ID NO: 69. In some instances,the 5 UTR consists of the sequence of SEQ ID NO: 69. In some instances, the 5UTR comprises the sequence of SEQ ID NO: 74. In some instances, the 5 UTRconsists of the sequence of SEQ ID NO: 74. In some instances, the 5 UTR comprisesthe sequence of SEQ ID NO: 75. In some instances, the 5 UTR consists of thesequence of SEQ ID NO: 75. In some instances, the 5 UTR comprises the sequenceof SEQ ID NO: 97. In some instances, the 5 UTR consists of the sequence of SEQID NO: 97. Attorney Docket No.: 45817-0173WO1 In some instances, a 5 UTR sequence provided in Table 10 has a firstnucleotide (not shown) which is an A. In some instances, a 5 UTR sequence providedin Table 10 has a first nucleotide (not shown) which is a G. Table 10 – 5’ UTR Sequences G C C C C x Attorney Docket No.: 45817-0173WO1 x C G C Attorney Docket No.: 45817-0173WO1 A C In some instances, the 5 UTR comprises SEQ ID NO:64 or a variant of SEQID NO:64. In some instances, the variant of SEQ ID NO: 69 comprises a nucleic acid sequence of Formula A: G G A A A U C G C A A A A (N2)X(N3)XC U (N4)X(N5)XC G C G U U A G A U U U C U U U U A G U U U U C U N6N7C A A C U A G C A A G C U U U U U G U U C U C G C C (N8C C)x (SEQ ID NO:78), wherein: (N2)x is a uracil and x is an integer from 0 to 5, e.g., wherein x =3 or 4; (N3)x is a guanine and x is an integer from 0 to 1; (N4)x is a cytosine and x is an integer from 0 to 1; (N5)x is a uracil and x is an integer from 0 to 5, e.g., wherein x =2 or 3; N6 is a uracil or cytosine; N7 is a uracil or guanine; and N8 is adenine or guanine and x is an integer from 0 to 1. In some instances (N2)x is a uracil and x is 0. In some instances (N2)x is a uracil and x is 1. In some instances (N2)xis a uracil and x is 2. In some instances (N2)x Attorney Docket No.: 45817-0173WO1 is a uracil and x is 3. In some instances, (N2)xis a uracil and x is 4. In some instances (N2)xis a uracil and x is 5. In some instances, (N3)xis a guanine and x is 0. In some instances, (N3)xis a guanine and x is 1. In some instances, (N4)x is a cytosine and x is 0. In some instances, (N4)x is a cytosine and x is 1. In some instances, (N5)x is a uracil and x is 0. In some instances, (N5)x is a uracil and x is 1. In some instances, (N5)x is a uracil and x is 2. In some instances, (N5)x is a uracil and x is 3. In some instances, (N5)x is a uracil and x is 4. In some instances (N5)x is a uracil and x is 5. In some instances, N6 is a uracil. In some instances, N6 is a cytosine. In some instances, N7 is a uracil. In some instances, N7 is a guanine. In some instances, N8 is an adenine and x is 0. In some instances, N8 is an adenine and x is 1. In some instances, N8 is a guanine and x is 0. In some instances, N8 is a guanine and x is 1. In some instances, the 5 UTR comprises a variant of SEQ ID NO: 69, SEQ IDNO: 74, SEQ ID NO: 75, or SEQ ID NO: 97. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, or 80%. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 5%. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 10%. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 20%. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 30%. In some Attorney Docket No.: 45817-0173WO1 instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 40%. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 50%. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 60%. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 70%. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises a uridine content of at least 80%. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises at least 2, 3, 4, 5, 6 or 7 consecutive uridines (e.g., a polyuridine tract). In some instances, the polyuridine tract in the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises at least 1-7, 2-7, 3-7, 4-7, 5-7, 6-7, 1-6, 1-5, 1-4, 1-3, 1-2, 2-6, or 3-5 consecutive uridines. In some instances, the polyuridine tract in the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises 4 consecutive uridines. In some instances, the polyuridine tract in the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises 5 consecutive uridines. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15 polyuridine tracts. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises 3 polyuridine tracts. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises 4 polyuridine tracts. In some instances, the variant of SEQ ID NO: 69, SEQ ID NO: 74, SEQ ID NO: 75, or SEQ ID NO: 97 comprises 5 polyuridine tracts. Attorney Docket No.: 45817-0173WO1 In some instances, one or more of the polyuridine tracts are adjacent to a different polyuridine tract. In some instances, each of, e.g., all, the polyuridine tracts are adjacent to each other, e.g., all of the polyuridine tracts are contiguous. In some instances, one or more of the polyuridine tracts are separated by 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 2, 13, 14, 15, 16, 17, 18.19, 20, 30, 40, 50 or 60 nucleotides. In some instances, each of, e.g., all of, the polyuridine tracts are separated by 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 2, 13, 14, 15, 16, 17, 18.19, 20, 30, 40, 50 or 60 nucleotides. In some instances, a first polyuridine tract and a second polyuridine tract are adjacent to each other. In some instances, a subsequent, e.g., third, fourth, fifth, sixth or seventh, eighth, ninth, or tenth, polyuridine tract is separated by 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 2, 13, 14, 15, 16, 17, 18.19, 20, 30, 40, 50 or 60 nucleotides from the first polyuridine tract, the second polyuridine tract, or any one of the subsequent polyuridine tracts. In some instances, a first polyuridine tract is separated by 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 2, 13, 14, 15, 16, 17, 18.19, 20, 30, 40, 50 or 60 nucleotides from a subsequent polyuridine tract, e.g., a second, third, fourth, fifth, sixth or seventh, eighth, ninth, or tenth polyuridine tract. In some instances, one or more of the subsequent polyuridine tracts are adjacent to a different polyuridine tract. In some instances, the 5 UTR comprises a Kozak sequence, e.g., a GCCRCCnucleotide sequence wherein R is an adenine or guanine. In some instances, theKozak sequence is disposed at the 3 end of the 5 UTR sequence.In one aspect, polynucleotides (e.g., mRNAs) comprising open reading frames (e.g., SEQ ID NOs: 60 and 63; SEQ ID NOs: 61 and 63; SEQ ID NOs: 62 and 63)encoding an Engager polypeptide and comprising a 5 UTR sequence disclosed hereinis formulated as an LNP. In some cases, the 5’UTR comprises the sequence of SEQ ID NO: 64. In some instances, the LNP composition comprises: (i) an ionizable amino lipid (e.g., Compound 2); (ii) a structural lipid (e.g., cholesterol); (iii) a phospholipid (e.g., DSPC); and (iv) a PEG-lipid (e.g., Compound I). Attorney Docket No.: 45817-0173WO1 In another aspect, the LNP compositions of the disclosure are used in a method of treating multiple myeloma in a human subject. In another aspect, an LNP composition comprising polynucleotides disclosed herein encoding an Engager polypeptide(s), e.g., as described herein, can be administered with an additional agent, e.g., as described herein. 3UTR sequences3 UTR sequences have been shown to influence translation, half-life, andsubcellular localization of mRNAs (Mayr C., Cold Spring Harb. Persp. Biol.2019 Oct 1;11(10):a034728). Disclosed herein, inter alia, is a polynucleotide, e.g., mRNA, comprising an open reading frames (e.g., any of SEQ ID NOs: 60 and 63; SEQ ID NOs: 61 and 63; or SEQ ID NOs: 62 and 63) encoding an Engager polypeptide, which polynucleotidehas a 3 UTR that confers an increased half-life, increased expression and / or increasedactivity of the polypeptide encoded by said polynucleotide, or of the polynucleotideitself., a polynucleotide disclosed herein comprises: (a) a 5 -UTR (e.g., as describedherein); (b) a coding region comprising a stop element (e.g., as described herein); and(c) a 3 -UTR (e.g., as provided in SEQ ID NO: 127, SEQ ID NO: 128, SEQ ID NO:129, SEQ ID NO: 130, or Table 11 or a variant or fragment thereof), and LNP compositions comprising the same. In some instances, the polynucleotide comprises a3 -UTR comprising a sequence provided in Table 11 or a variant or fragment thereof.In some instances, the polynucleotide having a 3 UTR sequence provided inSEQ ID NO: 127, SEQ ID NO: 128, SEQ ID NO: 129, SEQ ID NO: 130, or Table 11 or a variant or fragment thereof, results in an increased half-life of the polynucleotide, e.g., about 1.5-10-fold increase in half-life of the polynucleotide. In some instances, the increase in half-life is about 1.5-, 2-, 3-, 4-, 5-, 6-, 7-, 8-, 9-, or 10-fold, or more. In some instances, the increase in half-life is about 1.5-fold or more. In some instances, the increase in half-life is about 2-fold or more. In some instances, the increase in half-life is about 3-fold or more. In some instances, the increase in half-life Attorney Docket No.: 45817-0173WO1 is about 4-fold or more. In some instances, the increase in half-life is about 5-fold or more. In some instances, the increase in half-life is about 6-fold or more. In some instances, the increase in half-life is about 7-fold or more. In some instances, the increase in half-life is about 8-fold. In some instances, the increase in half-life is about 9-fold or more. In some instances, the increase in half-life is about 10-fold or more. In some instances, the polynucleotide having a 3 UTR sequence provided inSEQ ID NO: 127, SEQ ID NO: 128, SEQ ID NO: 129, SEQ ID NO: 130, or Table 11 or a variant or fragment thereof, results in a polynucleotide with a mean half-life score of greater than 10. In some instances, the polynucleotide having a 3 UTR sequence provided inSEQ ID NO: 127, SEQ ID NO: 128, SEQ ID NO: 129, SEQ ID NO: 130, or Table 11 or a variant or fragment thereof, results in an increased level and / or activity, e.g., output, of the polypeptide encoded by the polynucleotide. In some instances, the increase is compared to an otherwise similarpolynucleotide which does not have a 3 UTR, has a different 3 UTR, or does nothave a 3 UTR of Table 11 or a variant or fragment thereof.In some instances, the polynucleotide comprises a 3 UTR sequence providedin SEQ ID NO: 127, SEQ ID NO: 128, SEQ ID NO: 129, SEQ ID NO: 130, or Table 11 or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100%identity to a 3 UTR sequence provided in SEQ ID NO: 127, SEQ ID NO: 128, SEQID NO: 129, SEQ ID NO: 130, or Table 11, or a fragment thereof. In some instances,the 3 UTR comprises a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%,98%, 99% or 100% identity to SEQ ID NO: 99, SEQ ID NO: 100, SEQ ID NO: 101, SEQ ID NO: 102, SEQ ID NO: 103, SEQ ID NO: 104, SEQ ID NO: 105, SEQ ID NO: 106, SEQ ID NO: 107, SEQ ID NO: 108, SEQ ID NO: 109, SEQ ID NO: 110, SEQ ID NO: 111, SEQ ID NO: 112, SEQ ID NO: 113, SEQ ID NO:114, SEQ ID NO:124 , SEQ ID NO: 125, SEQ ID NO: 126, SEQ ID NO: 127, SEQ ID NO: 128, SEQ ID NO: 129, or SEQ ID NO: 130. Attorney Docket No.: 45817-0173WO1 In some instances, the 3 UTR comprises the sequence of SEQ ID NO: 99, or asequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identityto SEQ ID NO: 99. In some instances, the 3 UTR comprises the sequence of SEQ IDNO: 100, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or100% identity to SEQ ID NO: 100. In some instances, the 3 UTR comprises thesequence of SEQ ID NO: 101, or a sequence with at least 80%, 85%, 90%, 95%, 96%,97%, 98%, 99% or 100% identity to SEQ ID NO: 101. In some instances, the 3 UTRcomprises the sequence of SEQ ID NO: 102, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 102. In someinstances, the 3 UTR comprises the sequence of SEQ ID NO: 103, or a sequence withat least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO:103. In some instances, the 3 UTR comprises the sequence of SEQ ID NO: 104, or asequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identityto SEQ ID NO: 104. In some instances, the 3 UTR comprises the sequence of SEQID NO: 105, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%or 100% identity to SEQ ID NO: 105. In some instances, the 3 UTR comprises thesequence of SEQ ID NO: 106, or a sequence with at least 80%, 85%, 90%, 95%, 96%,97%, 98%, 99% or 100% identity to SEQ ID NO: 106. In some instances, the 3 UTRcomprises the sequence of SEQ ID NO: 107, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 107. In someinstances, the 3 UTR comprises the sequence of SEQ ID NO: 108, or a sequence withat least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ IDNO: 108. In some instances, the 3 UTR comprises the sequence of SEQ ID NO: 109,or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100%identity to SEQ ID NO: 109. In some instances, the 3 UTR comprises the sequence ofSEQ ID NO: 110, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%,99% or 100% identity to SEQ ID NO: 110. In some instances, the 3 UTR comprisesthe sequence of SEQ ID NO: 111, or a sequence with at least 80%, 85%, 90%, 95%,96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 111. In some instances, the 3UTR comprises the sequence of SEQ ID NO: 112, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 112. In Attorney Docket No.: 45817-0173WO1 some instances, the 3 UTR comprises the sequence of SEQ ID NO: 113, or asequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 113. In some instances, the 3 UTR comprises the sequence of SEQID NO: 114, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 114. In some instances, the 3 UTR comprises thesequence of SEQ ID NO: 124, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 124. In some instances, the 3 UTRcomprises the sequence of SEQ ID NO: 125, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 125. In some instances, the 3 UTR comprises the sequence of SEQ ID NO: 126, or a sequence withat least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 126. In some instances, the 3 UTR comprises the sequence of SEQ ID NO: 127,or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 127. In some instances, the 3 UTR comprises the sequence ofSEQ ID NO: 128, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 128. In some instances, the 3 UTR comprisesthe sequence of SEQ ID NO: 129, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 129. In some instances, the 3UTR comprises the sequence of SEQ ID NO: 130, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 130. Table 11– 3’ UTR Sequences G C U Attorney Docket No.: 45817-0173WO1 U C C A C G G G C A G U U U Attorney Docket No.: 45817-0173WO1 G A G A U U A U G U In some instances, the 3 UTR comprises the sequence of SEQ ID NO: 127, ora sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 127. In some instances, the 3 UTR comprises the sequence ofSEQ ID NO: 128, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 128. In some instances, the 3 UTR comprisesthe sequence of SEQ ID NO: 129, or a sequence with at least 80%, 85%, 90%, 95%, Attorney Docket No.: 45817-0173WO196%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 129. In some instances, the 3UTR comprises the sequence of SEQ ID NO: 130, or a sequence with at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or 100% identity to SEQ ID NO: 130. Regions having a 5 CapThe disclosure also includes a polynucleotide that comprises both a 5 cap anda polynucleotide of the present disclosure (e.g., a polynucleotide comprising a nucleotide sequence encoding an Engager polypeptide to be expressed). The 5 cap structure of a natural mRNA is involved in nuclear export,increasing mRNA stability and binds the mRNA Cap Binding Protein (CBP), which is responsible for mRNA stability in the cell and translation competency through the association of CBP with poly A binding protein to form the mature cyclic mRNAspecies. The cap further assists the removal of 5 proximal introns during mRNAsplicing. Endogenous mRNA molecules can be 5 -end capped generating a 5 -ppp-5 -triphosphate linkage between a terminal guanosine cap residue and the 5 -terminaltranscribed sense nucleotide of the mRNA molecule. This 5 -guanylate cap can thenbe methylated to generate an N7-methyl-guanylate residue. The ribose sugars of theterminal and / or ante-terminal transcribed nucleotides of the 5 end of the mRNA canoptionally also be 2 -O-methylated. 5 -decapping through hydrolysis and cleavage ofthe guanylate cap structure can target a nucleic acid molecule, such as an mRNA molecule, for degradation. In some instances, the polynucleotides of the present disclosure (e.g., a polynucleotide comprising a nucleotide sequence encoding an Engager polypeptide) incorporate a cap moiety. In any of the instances disclosed herein, a 5’ terminal cap may terminate at the 3’ end with an A or G, even if not shown in the disclosure below. In some instances, polynucleotides of the present disclosure comprise a non- hydrolyzable cap structure preventing decapping and thus increasing mRNA half-life.Because cap structure hydrolysis requires cleavage of 5 -ppp-5 phosphodiester Attorney Docket No.: 45817-0173WO1 linkages, modified nucleotides can be used during the capping reaction. For example, a Vaccinia Capping Enzyme from New England Biolabs (Ipswich, MA) can be used with -thio-guanosine nucleotides according to the manufacturer's instructions tocreate a phosphorothioate linkage in the 5 -ppp-5 cap. Additional modified guanosinenucleotides can be used such as -methyl-phosphonate and seleno-phosphate nucleotides. Additional modifications include, but are not limited to, 2 -O-methylation ofthe ribose sugars of 5 -terminal and / or 5 -anteterminal nucleotides of thepolynucleotide (as mentioned above) on the 2 -hydroxyl group of the sugar ring.Multiple distinct 5 -cap structures can be used to generate the 5 -cap of a nucleic acidmolecule, such as a polynucleotide that functions as an mRNA molecule. Cap analogs, which herein are also referred to as synthetic cap analogs, chemical caps, chemical cap analogs, or structural or functional cap analogs, differ from natural (i.e.,endogenous, wild-type or physiological) 5 -caps in their chemical structure, whileretaining cap function. Cap analogs can be chemically (i.e., non-enzymatically) or enzymatically synthesized and / or linked to the polynucleotides of the present disclosure. For example, the Anti-Reverse Cap Analog (ARCA) cap contains twoguanines linked by a 5 -5 -triphosphate group, wherein one guanine contains an N7methyl group as well as a 3 -O-methyl group (i.e., N7,3 -O-dimethyl-guanosine-5 -triphosphate-5 -guanosine (m7G-3 mppp-G; which can equivalently be designated 3O-Me-m7G(5 )ppp(5 )G). The 3 -O atom of the other, unmodified, guanine becomeslinked to the 5 -terminal nucleotide of the capped polynucleotide. The N7- and 3 -O-methlyated guanine provides the terminal moiety of the capped polynucleotide. Another exemplary cap is mCAP, which is similar to ARCA but has a 2 -O-methyl group on guanosine (i.e., N7,2 -O-dimethyl-guanosine-5 -triphosphate-5 -guanosine, m7Gm-ppp-G). Another exemplary cap is m7G-ppp-Gm-A (i.e., N7,guanosine-5 -triphosphate-2 -O-dimethyl-guanosine-adenosine). Attorney Docket No.: 45817-0173WO1 In some instances, the cap is a dinucleotide cap analog. As a non-limiting example, the dinucleotide cap analog can be modified at different phosphate positions with a boranophosphate group or a phosphoroselenoate group such as the dinucleotide cap analogs described in U.S. Patent No. US 8,519,110, the contents of which are herein incorporated by reference in its entirety. In some instances, the cap is a cap analog is a N7-(4-chlorophenoxyethyl) substituted dinucleotide form of a cap analog known in the art and / or described herein. Non-limiting examples of a N7-(4-chlorophenoxyethyl) substituted dinucleotide form of a cap analog include a N7-(4-chlorophenoxyethyl)-G(5 )ppp(5 )G and a N7-(4-chlorophenoxyethyl)-m3 -OG(5 )ppp(5 )G cap analog (See,e.g., the various cap analogs and the methods of synthesizing cap analogs described in Kore et al. Bioorganic & Medicinal Chemistry 201321:4570-4574; the contents of which are herein incorporated by reference in its entirety). In some instances, a cap analog of the present disclosure is a 4-chloro / bromophenoxyethyl analog. Polynucleotides of the present disclosure can also be capped post-manufacture (whether IVT or chemical synthesis), using enzymes, in order to generate moreauthentic 5 -cap structures. As used herein, the phrase "more authentic" refers to afeature that closely mirrors or mimics, either structurally or functionally, an endogenous or wild type feature. That is, a "more authentic" feature is better representative of an endogenous, wild-type, natural or physiological cellular function and / or structure as compared to synthetic features or analogs, etc., of the prior art, or which outperforms the corresponding endogenous, wild-type, natural or physiologicalfeature in one or more respects. Non-limiting examples of more authentic 5 capstructures of the present disclosure are those that, among other things, have enhancedbinding of cap binding proteins, increased half-life, reduced susceptibility to 5endonucleases and / or reduced 5 decapping, as compared to synthetic 5 cap structuresknown in the art (or to a wild-type, natural or physiological 5 cap structure). Forexample, recombinant Vaccinia Virus Capping Enzyme and recombinant 2 -O-methyltransferase enzyme can create a canonical 5 -5 -triphosphate linkage betweenthe 5 -terminal nucleotide of a polynucleotide and a guanine cap nucleotide wherein Attorney Docket No.: 45817-0173WO1the cap guanine contains an N7 methylation and the 5 -terminal nucleotide of themRNA contains a 2 -O-methyl. Such a structure is termed the Cap1 structure. Thiscap results in a higher translational-competency and cellular stability and a reducedactivation of cellular pro-inflammatory cytokines, as compared, e.g., to other 5 capanalog structures known in the art. Cap structures include, but are not limited to,7mG(5 )ppp(5 )N1pN2p (cap 0), 7mG(5 )ppp(5 )N1mpNp (cap 1), and 7mG(5 )-ppp(5 )N1mpN2mp (cap 2).As a non-limiting example, capping chimeric polynucleotides post- manufacture can be more efficient as nearly 100% of the chimeric polynucleotides can be capped. This is in contrast to ~80% when a cap analog is linked to a chimeric polynucleotide in the course of an in vitro transcription reaction. According to the present disclosure, 5 terminal caps can include endogenouscaps or cap analogs. According to the present disclosure, a 5 terminal cap cancomprise a guanine analog. Useful guanine analogs include, but are not limited to,inosine, N1-methyl-guanosine, 2 fluoro-guanosine, 7-deaza-guanosine, 8-oxo-guanosine, 2-amino-guanosine, LNA-guanosine, and 2-azido-guanosine. Also provided herein are exemplary caps including those that can be used in co-transcriptional capping methods for ribonucleic acid (RNA) synthesis, using RNA polymerase, e.g., wild type RNA polymerase or variants thereof, e.g., such as those variants described herein. In some instances, caps can be added when RNA is produced in a “one-pot” reaction, without the need for a separate capping reaction. Thus, the methods, in some instances, comprise reacting a polynucleotide template with an RNA polymerase variant, nucleoside triphosphates, and a cap analog under in vitro transcription reaction conditions to produce RNA transcript. As used here the term “cap” includes the inverted G nucleotide and can comprise one or more additional nucleotides 3’ of the inverted G nucleotide, e.g., 1, 2, 3, or more nucleotides 3’ of the inverted G nucleotide and 5’ to the 5’ UTR, e.g., a 5’ UTR described herein. Attorney Docket No.: 45817-0173WO1 Exemplary caps comprise a sequence of GG, GA, or GGA, wherein the underlined, italicized G is an in inverted G nucleotide followed by a 5’-5’- triphosphate group. In some instances, a cap comprises a compound of Formula (C-I) a stereoisomer, tautomer or salt thereof, wherein ; ring B1 is a modified or unmodified Guanine; ring B2 and ring B3 each independently is a nucleobase or a modified nucleobase; X2 is O, S(O)p, NR24 or CR25R26 in which p is 0, 1, or 2; Y0is O or CR6R7; Y1 is O, S(O)n, CR6R7, or NR8, in which n is 0, 1 , or 2; each --- is a single bond or absent, wherein when each --- is a single bond, Yi is O, S(O)n, CR6R7, or NR8; and when each --- is absent, Y1is void; Y2is (OP(O)R4)min which m is 0, 1, or 2, or -O-(CR40R41)u-Q0-(CR42R43)v-, in which Q0is a bond, O, S(O)r, NR44, or CR45R46, r is 0, 1 , or 2, and each of u and v independently is 1, 2, 3 or 4; each R2 and R2' independently is halo, LNA, or OR3; each R3 independently is H, C1-C6 alkyl, C2-C6 alkenyl, or C2-C6 alkynyl and R3, Attorney Docket No.: 45817-0173WO1 when being C1-C6alkyl, C2-C6alkenyl, or C2-C6alkynyl, is optionally substituted with one or more of halo, OH and C1-C6alkoxyl that is optionally substituted with one or more OH or OC(O)-C1-C6alkyl; each R4and R4' independently is H, halo, C1-C6alkyl, OH, SH, SeH, or BH3-; each of R6, R7, and R8, independently, is -Q1-T1, in which Q1is a bond or C1-C3alkyl linker optionally substituted with one or more of halo, cyano, OH and C1-C6 alkoxy, and T1 is H, halo, OH, COOH, cyano, or Rs1, in which Rs1 is C1-C3 alkyl, C2-C6 alkenyl, C2-C6 alkynyl, C1- C6 alkoxyl, C(O)O-C1-C6 alkyl, C3-C8 cycloalkyl, C6-C10 aryl, NR31R32, (NR31R32R33)+, 4 to 12- membered heterocycloalkyl, or 5- or 6- membered heteroaryl, and Rs1 is optionally substituted with one or more substituents selected from the group consisting of halo, OH, oxo, C1-C6 alkyl, COOH, C(O)O-C1- C6 alkyl, cyano, C1-C6 alkoxyl, NR31R32, (NR31R32R33)+, C3-C8 cycloalkyl, C6- C10 aryl, 4 to 12-membered heterocycloalkyl, and 5- or 6-membered heteroaryl; each of R10, R11, R12, R13R14, and R15, independently, is -Q2-T2, in which Q2is a bond or C1-C3alkyl linker optionally substituted with one or more of halo, cyano, OH and C1-C6alkoxy, and T2is H, halo, OH, NH2, cyano, NO2, N3, Rs2, or ORs2, in which Rs2is C1-C6alkyl, C2-C6alkenyl, C2-C6alkynyl, C3-C8cycloalkyl, C6-C10aryl, NHC(O)- C1-C6alkyl, NR31R32, (NR31R32R33)+, 4 to 12-membered heterocycloalkyl, or 5- or 6- membered heteroaryl, and Rs2is optionally substituted with one or more substituents selected from the group consisting of halo, OH, oxo, C1-C6alkyl, COOH, C(O)O-C1- C6alkyl, cyano, C1- C6alkoxyl, NR31R32, (NR31R32R33)+, C3-C8cycloalkyl, C6- C10 aryl, 4 to 12-membered heterocycloalkyl, and 5- or 6- membered heteroaryl; or alternatively R12 together with R14 is oxo, or R13 together with R15 is oxo, each of R20, R21, R22, and R23 independently is -Q3-T3, in which Q3 is a bond or C1-C3 alkyl linker optionally substituted with one or more of halo, cyano, OH and C1-C6 alkoxy, and T3 is H, halo, OH, NH2, cyano, NO2, N3, RS3, or ORS3, in which RS3 is C1- C6 alkyl, C2-C6 alkenyl, C2-C6 alkynyl, C3-C8 cycloalkyl, C6-C10 aryl, NHC(O)-C1- C6 alkyl, mono-C1-C6 alkylamino, di-C1-C6 alkylamino, 4 to 12-membered heterocycloalkyl, or 5- or 6-membered heteroaryl, and Rs3 is optionally substituted with one or more substituents selected from the group consisting of halo, OH, oxo, C1-C6alkyl, COOH, C(O)O-C1-C6alkyl, cyano, C1-C6alkoxyl, amino, mono-C1-C6 Attorney Docket No.: 45817-0173WO1 alkylamino, di-C1-C6alkylamino, C3-C8cycloalkyl, C6-C10aryl, 4 to 12-membered heterocycloalkyl, and 5- or 6-membered heteroaryl; each of R24, R25, and R26independently is H or C1-C6alkyl; each of R27and R28independently is H or OR29; or R27and R28together form O-R30- O; each R29independently is H, C1-C6alkyl, C2-C6alkenyl, or C2-C6alkynyl and R29, when being C1-C6 alkyl, C2-C6 alkenyl, or C2-C6 alkynyl, is optionally substituted with one or more of halo, OH and C1-C6 alkoxyl that is optionally substituted with one or more OH or OC(O)-C1-C6 alkyl; R30 is C1-C6 alkylene optionally substituted with one or more of halo, OH and C1-C6 alkoxyl; each of R31, R32, and R33, independently is H, C1-C6 alkyl, C3-C8 cycloalkyl, C6-C10 aryl, 4 to 12-membered heterocycloalkyl, or 5- or 6-membered heteroaryl; each of R40, R41, R42, and R43 independently is H, halo, OH, cyano, N3, OP(O)R47R48, or C1-C6alkyl optionally substituted with one or more OP(O)R47R48, or one R41and one R43, together with the carbon atoms to which they are attached and Q0, form C4- C10cycloalkyl, 4- to 14-membered heterocycloalkyl, C6-C10aryl, or 5- to 14- membered heteroaryl, and each of the cycloalkyl, heterocycloalkyl, phenyl, or 5- to 6- membered heteroaryl is optionally substituted with one or more of OH, halo, cyano, N3, oxo, OP(O)R47R48, C1-C6alkyl, C1-C6haloalkyl, COOH, C(O)O-C1-C6alkyl, C1- C6alkoxyl, C1-C6haloalkoxyl, amino, mono-C1-C6alkylamino, and di-C1-C6alkylamino; R44 is H, C1-C6 alkyl, or an amine protecting group; each of R45 and R46 independently is H, OP(O)R47R48, or C1-C6 alkyl optionally substituted with one or more OP(O)R47R48, and each of R47 and R48, independently is H, halo, C1-C6 alkyl, OH, SH, SeH, or BH3. It should be understood that a cap analog, as provided herein, may include any of the cap analogs described in international publication WO 2017 / 066797, published on 20 April 2017, incorporated by reference herein in its entirety. In some instances, the B2middle position can be a non-ribose molecule, such as arabinose. Attorney Docket No.: 45817-0173WO1 In some instances R2is ethyl-based. Thus, in some instances, a cap comprises the following structure: (C-II). In other instances, a cap comprises the following structure: (C-III). Attorney Docket No.: 45817-0173WO1 In yet other instances, a cap comprises the following structure: (C-IV). In still other is, a cap comprises the following structure: (C-V). In some instances, R is an alkyl (e.g., C1-C6 alkyl). In some instances, R is a methyl group (e.g., C1alkyl). In some instances, R is an ethyl group (e.g., C2alkyl). Attorney Docket No.: 45817-0173WO1 In some instances, a cap comprises a sequence selected from the following sequences: GAA, GAC, GAG, GAU, GCA, GCC, GCG, GCU, GGA, GGC, GGG, GGU, GUA, GUC, GUG, and GUU. In some instances, a cap comprises GAA. In some instances, a cap comprises GAC. In some instances, a cap comprises GAG. In some instances, a cap comprises GAU. In some instances, a cap comprises GCA. In some instances, a cap comprises GCC. In some instances, a cap comprises GCG. In some instances, a cap comprises GCU. In some instances, a cap comprises GGA. In some instances, a cap comprises GGC. In some instances, a cap comprises GGG. In some instances, a cap comprises GGU. In some instances, a cap comprises GUA. In some instances, a cap comprises GUC. In some instances, a cap comprises GUG. In some instances, a cap comprises GUU. In some instances, a cap comprises a sequence selected from the following sequences: m7GpppApA, m7GpppApC, m7GpppApG, m7GpppApU, m7GpppCpA, m7GpppCpC, m7GpppCpG, m7GpppCpU, m7GpppGpA, m7GpppGpC, m7GpppGpG, m7GpppGpU, m7GpppUpA, m7GpppUpC, m7GpppUpG, and m7GpppUpU. In some instances, a cap comprises m7GpppApA. In some instances, a cap comprises m7GpppApC. In some instances, a cap comprises m7GpppApG. In some instances, a cap comprises m7GpppApU. In some instances, a cap comprises m7GpppCpA. In some instances, a cap comprises m7GpppCpC. In some instances, a cap comprises m7GpppCpG. In some instances, a cap comprises m7GpppCpU. In some instances, a cap comprises m7GpppGpA. In some instances, a cap comprises m7GpppGpC. In some instances, a cap comprises m7GpppGpG. In some instances, a cap comprises m7GpppGpU. In some instances, a cap comprises m7GpppUpA. In some instances, a cap comprises m7GpppUpC. In some instances, a cap comprises m7GpppUpG. In some instances, a cap comprises m7GpppUpU. A cap, in some instances, comprises a sequence selected from the following sequences: m7G3 OMepppApA, m7G3 OMepppApC, m7G3 OMepppApG, m7G3 OMepppApU, m7G3 OMepppCpA, m7G3 OMepppCpC, m7G3 OMepppCpG, m7G3 OMepppCpU, m7G3 OMepppGpA, m7G3 OMepppGpC, m7G3 OMepppGpG, Attorney Docket No.: 45817-0173WO1 m7G3 OMepppGpU, m7G3 OMepppUpA, m7G3 OMepppUpC, m7G3 OMepppUpG, and m7G3 OMepppUpU. In some instances, a cap comprises m7G3 OMepppApA. In some instances, a cap comprises m7G3 OMepppApC. In some instances, a cap comprises m7G3 OMepppApG. In some instances, a cap comprises m7G3 OMepppApU. In some instances, a cap comprises m7G3 OMepppCpA. In some instances, a cap comprises m7G3 OMepppCpC. In some instances, a cap comprises m7G3 OMepppCpG. In some instances, a cap comprises m7G3 OMepppCpU. In some instances, a cap comprises m7G3 OMepppGpA. In some instances, a cap comprises m7G3 OMepppGpC. In some instances, a cap comprises m7G3 OMepppGpG. In some instances, a cap comprises m7G3 OMepppGpU. In some instances, a cap comprises m7G3 OMepppUpA. In some instances, a cap comprises m7G3 OMepppUpC. In some instances, a cap comprises m7G3 OMepppUpG. In some instances, a cap comprises m7G3 OMepppUpU. In some instances, a cap comprises a sequence selected from the following sequences: m7G3 OMepppA2 OMepA, m7G3 OMepppA2 OMepC, m7G3 OMepppA2 OMepG, m7G3 OMepppA2 OMepU, m7G3 OMepppC2 OMepA, m7G3 OMepppC2 OMepC, m7G3 OMepppC2 OMepG, m7G3 OMepppC2 OMepU, m7G3 OMepppG2 OMepA, m7G3 OMepppG2 OMepC, m7G3 OMepppG2 OMepG, m7G3 OMepppG2 OMepU, m7G3 OMepppU2 OMepA, m7G3 OMepppU2 OMepC, m7G3 OMepppU2 OMepG, and m7G3 OMepppU2 OMepU. In some instances, a cap comprises m7G3 OMepppA2 OMepA. In some instances, a cap comprises m7G3 OMepppA2 OMepC. In some instances, a cap comprises m7G3 OMepppA2 OMepG. In some instances, a cap comprises m7G3 OMepppA2 OMepU. In some instances, a cap comprises m7G3 OMepppC2 OMepA. In some instances, a cap comprises m7G3 OMepppC2 OMepC. In some instances, a cap comprises m7G3 OMepppC2 OMepG. In some instances, a cap comprises m7G3 OMepppC2 OMepU. In some instances, a cap comprises m7G3 OMepppG2 OMepA. In some instances, a cap comprises m7G3 OMepppG2 OMepC. In some instances, a cap comprises Attorney Docket No.: 45817-0173WO1 m7G3 OMepppG2 OMepG. In some instances, a cap comprises m7G3 OMepppG2 OMepU. In some instances, a cap comprises m7G3 OMepppU2 OMepA. In some instances, a cap comprises m7G3 OMepppU2 OMepC. In some instances, a cap comprises m7G3 OMepppU2 OMepG. In some instances, a cap comprises m7G3 OMepppU2 OMepU. A cap, in still other instances, comprises a sequence selected from the following sequences: m7GpppA2 OMepA, m7GpppA2 OMepC, m7GpppA2 OMepG, m7GpppA2 OMepU, m7GpppC2 OMepA, m7GpppC2 OMepC, m7GpppC2 OMepG, m7GpppC2 OMepU, m7GpppG2 OMepA, m7GpppG2 OMepC, m7GpppG2 OMepG, m7GpppG2 OMepU, m7GpppU2 OMepA, m7GpppU2 OMepC, m7GpppU2 OMepG, and m7GpppU2 OMepU. In some instances, a cap comprises m7GpppA2 OMepA. In some instances, a cap comprises m7GpppA2 OMepC. In some instances, a cap comprises m7GpppA2 OMepG. In some instances, a cap comprises m7GpppA2 OMepU. In some instances, a cap comprises m7GpppC2 OMepA. In some instances, a cap comprises m7GpppC2 OMepC. In some instances, a cap comprises m7GpppC2 OMepG. In some instances, a trinucleotide cap comprises m7GpppC2 OMepU. In some instances, a cap comprises m7GpppG2 OMepA. In some instances, a cap comprises m7GpppG2 OMepC. In some instances, a cap comprises m7GpppG2 OMepG. In some instances, a cap comprises m7GpppG2 OMepU. In some instances, a cap comprises m7GpppU2 OMepA. In some instances, a cap comprises m7GpppU2 OMepC. In some instances, a cap comprises m7GpppU2 OMepG. In some instances, a cap comprises m7GpppU2 OMepU. In some instances, a cap comprises m7Gpppm6A2’OmepG. In some instances, a cap comprises m7Gpppe6A2’OmepG. In some instances, a cap comprises GAG. In some instances, a cap comprises GCG. In some instances, a cap comprises GUG. In some instances, a cap comprises GGG. In some instances, a cap comprises any one of the following structures: Attorney Docket No.: 45817-0173WO1 or In some instances, the cap comprisesm7GpppN1N2N3, where N1, N2, and N3are optional (i.e., can be absent or one or more can be present) and are independently a natural, a modified, or an unnatural nucleoside base. In some instances,m7G is further methylated, e.g., at the 3’ position. In some instances, them7G comprises an O-methyl at the 3’ position. In some instances N1, N2, and N3if present, optionally, are independently an adenine, a uracil, a guanidine, a thymine, or a cytosine. In some instances, one or more (or all) of N1, N2, and N3, if present, are methylated, e.g., at the 2’ position. In some instances, one or more (or all) of N1, N2, and N3, if present have an O-methyl at the 2’ position. Attorney Docket No.: 45817-0173WO1 In some instances, the cap comprises the following structure: wherein B1, B2, and B3are independently a natural, a modified, or an unnatural nucleoside based; and R1, R2, R3, and R4are independently OH or O-methyl. In some , R3is O-methyl and R4is OH. In some instances, R3and R4are O-methyl. In some instances, R4is O-methyl. In some instances, R1is OH, R2is OH, R3is O-methyl, and R4 is OH. In some instances, R1 is OH, R2 is OH, R3 is O-methyl, and R4 is O- methyl. In some instances, at least one of R1 and R2 is O-methyl, R3 is O-methyl, and R4 is OH. In some instances, at least one of R1 and R2 is O-methyl, R3 is O-methyl, and R4 is O-methyl. In some instances, B1, B3, and B3 are natural nucleoside bases. In some instances, at least one of B1, B2, and B3 is a modified or unnatural base. In some instances, at least one of B1, B2, and B3 is N6-methyladenine. In some instances, B1 is adenine, cytosine, thymine, or uracil. In some instances, B1 is adenine, B2 is uracil, and B3is adenine. In some instances, R1and R2are OH, R3and R4are O-methyl, B1is adenine, B2is uracil, and B3is adenine. In some instances the cap comprises a sequence selected from the following sequences: GAAA, GACA, GAGA, GAUA, GCAA, GCCA, GCGA, GCUA, GGAA, GGCA, GGGA, GGUA, GUCA, and GUUA. In some instances the cap comprises a sequence selected from the following sequences: GAAG, GACG, GAGG, GAUG, GCAG, GCCG, GCGG, GCUG, GGAG, GGCG, GGGG, GGUG, GUCG, GUGG, Attorney Docket No.: 45817-0173WO1 and GUUG. In some instances the cap comprises a sequence selected from the following sequences: GAAU, GACU, GAGU, GAUU, GCAU, GCCU, GCGU, GCUU, GGAU, GGCU, GGGU, GGUU, GUAU, GUCU, GUGU, and GUUU. In some instances the cap comprises a sequence selected from the following sequences: GAAC, GACC, GAGC, GAUC, GCAC, GCCC, GCGC, GCUC, GGAC, GGCC, GGGC, GGUC, GUAC, GUCC, GUGC, and GUUC. A cap, in some instances, comprises a sequence selected from the following sequences: m7G3 OMepppApApN, m7G3 OMepppApCpN, m7G3 OMepppApGpN, m7G3 OMepppApUpN, m7G3 OMepppCpApN, m7G3 OMepppCpCpN, m7G3 OMepppCpGpN, m7G3 OMepppCpUpN, m7G3 OMepppGpApN, m7G3 OMepppGpCpN, m7G3 OMepppGpGpN, m7G3 OMepppGpUpN, m7G3 OMepppUpApN, m7G3 OMepppUpCpN, m7G3 OMepppUpGpN, and m7G3 OMepppUpUpN, where N is a natural, a modified, or an unnatural nucleoside base. A cap, in some instances, comprises a sequence selected from the following sequences: m7G3 OMepppA2 OMepApN, m7G3 OMepppA2 OMepCpN, m7G3 OMepppA2 OMepGpN, m7G3 OMepppA2 OMepUpN, m7G3 OMepppC2 OMepApN, m7G3 OMepppC2 OMepCpN, m7G3 OMepppC2 OMepGpN, m7G3 OMepppC2 OMepUpN, m7G3 OMepppG2 OMepApN, m7G3 OMepppG2 OMepCpN, m7G3 OMepppG2 OMepGpN, m7G3 OMepppG2 OMepUpN, m7G3 OMepppU2 OMepApN, m7G3 OMepppU2 OMepCpN, m7G3 OMepppU2 OMepGpN, and m7G3 OMepppU2 OMepUpN, where N is a natural, a modified, or an unnatural nucleoside base. A cap, in some instances, comprises a sequence selected from the following sequences: m7GpppA2 OMepApN, m7GpppA2 OMepCpN, m7GpppA2 OMepGpN, m7GpppA2 OMepUpN, m7GpppC2 OMepApN, m7GpppC2 OMepCpN, m7GpppC2 OMepGpN, m7GpppC2 OMepUpN, m7GpppG2 OMepApN, m7GpppG2 OMepCpN, m7GpppG2 OMepGpN, m7GpppG2 OMepUpN, m7GpppU2 OMepApN, m7GpppU2 OMepCpN, m7GpppU2 OMepGpN, and Attorney Docket No.: 45817-0173WO1 m7GpppU2 OMepUpN, where N is a natural, a modified, or an unnatural nucleoside base. A cap, in some instances, comprises a sequence selected from the following sequences: m7G3 OMepppA2 OMepA2 OMepN, m7G3 OMepppA2 OMepC2 OMepN, m7G3 OMepppA2 OMepG2 OMepN, m7G3 OMepppA2 OMepU2 OMepN, m7G3 OMepppC2 OMepA2 OMepN, m7G3 OMepppC2 OMepC2 OMepN, m7G3 OMepppC2 OMepG2 OMepN, m7G3 OMepppC2 OMepU2 OMepN, m7G3 OMepppG2 OMepA2 OMepN, m7G3 OMepppG2 OMepC2 OMepN, m7G3 OMepppG2 OMepG2 OMepN, m7G3 OMepppG2 OMepU2 OMepN, m7G3 OMepppU2 OMepA2 OMepN, m7G3 OMepppU2 OMepC2 OMepN, m7G3 OMepppU2 OMepG2 OMepN, and m7G3 OMepppU2 OMepU2 OMepN, where N is a natural, a modified, or an unnatural nucleoside base. A cap, in some instances, comprises a sequence selected from the following sequences: m7GpppA2 OMepA2 OMepN, m7GpppA2 OMepC2 OMepN, m7GpppA2 OMepG2 OMepN, m7GpppA2 OMepU2 OMepN, m7GpppC2 OMepA2 OMepN, m7GpppC2 OMepC2 OMepN, m7GpppC2 OMepG2 OMepN, m7GpppC2 OMepU2 OMepN, m7GpppG2 OMepA2 OMepN, m7GpppG2 OMepC2 OMepN, m7GpppG2 OMepG2 OMepN, m7GpppG2 OMepU2 OMepN, m7GpppU2 OMepA2 OMepN, m7GpppU2 OMepC2 OMepN, m7GpppU2 OMepG2 OMepN, and m7GpppU2 OMepU2 OMepN, where N is a natural, a modified, or an unnatural nucleoside base. In some instances, a cap comprises GGAG. In some instances, a cap comprises the following structure:

[0002] Attorney Docket No.: 45817-0173WO1 (C-X). In some instances, the mRNA comprises a m7GpppGm, m7GpppGmA, or m7GpppGmAG cap. Poly A Tails In some instances, the polynucleotides of the present disclosure (e.g., a polynucleotide comprising a nucleotide sequence encoding an Engager polypeptide) further comprise a poly A tail. In some instances, terminal groups on the poly A tailcan be incorporated for stabilization. In some instances, a poly A tail comprises des-3hydroxyl tails. During RNA processing, a long chain of adenine nucleotides (poly A tail) can be added to a polynucleotide (e.g., an mRNA molecule) in order to increase stability.Immediately after transcription, the 3 end of the transcript can be cleaved to free a 3hydroxyl. Then poly A polymerase adds a chain of adenine nucleotides to the RNA. The process, called polyadenylation, adds a poly A tail that can be between, for example, approximately 80 to approximately 250 residues long, including approximately 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240 or 250 residues long. In some instances, the poly A tail is 100 nucleotides in length (SEQ ID NO: 132). Poly A tails can also be added after the construct is exported from the nucleus. Attorney Docket No.: 45817-0173WO1 According to the present disclosure, terminal groups on the poly A tail can be incorporated for stabilization. Polynucleotides of the present disclosure can includedes-3 hydroxyl tails. They can also include structural moieties or 2'-O-methylmodifications as taught by Junjie Li, et al. (Current Biology, vol.15, 1501–1507, August 23, 2005), the contents of which are incorporated herein by reference in its entirety). The polynucleotides of the present disclosure can be designed to encode transcripts with alternative poly A tail structures including histone mRNA. According to Norbury, "Terminal uridylation has also been detected on human replication- dependent histone mRNAs. The turnover of these mRNAs is thought to be important for the prevention of potentially toxic histone accumulation following the completion or inhibition of chromosomal DNA replication. These mRNAs are distinguished bytheir lack of a 3 poly A tail, the function of which is instead assumed by a stablestem–loop structure and its cognate stem–loop binding protein (SLBP); the latter carries out the same functions as those of PABP on polyadenylated mRNAs" (Norbury, "Cytoplasmic RNA: a case of the tail wagging the dog," Nature Reviews Molecular Cell Biology; AOP, published online 29 August 2013; doi:10.1038 / nrm3645), the contents of which are incorporated herein by reference in its entirety. Unique poly A tail lengths provide certain advantages to the polynucleotides of the present disclosure. Generally, the length of a poly A tail, when present, is greater than 30 nucleotides in length (SEQ ID NO: 221). In some instances, the poly A tail is greater than 35 nucleotides in length (SEQ ID NO: 218) (e.g., at least or greater than about 35, 40, 45, 50, 55, 60, 70, 80, 90, 100, 120, 140, 160, 180, 200, 250, 300, 350, 400, 450, 500, 600, 700, 800, 900, 1,000, 1,100, 1,200, 1,300, 1,400, 1,500, 1,600, 1,700, 1,800, 1,900, 2,000, 2,500, and 3,000 nucleotides). In some instances, the polynucleotide or region thereof includes from about 30 to about 3,000 nucleotides (e.g., from 30 to 50, from 30 to 100, from 30 to 250, from 30 to 500, from 30 to 750, from 30 to 1,000, from 30 to 1,500, from 30 to 2,000, from Attorney Docket No.: 45817-0173WO1 30 to 2,500, from 50 to 100, from 50 to 250, from 50 to 500, from 50 to 750, from 50 to 1,000, from 50 to 1,500, from 50 to 2,000, from 50 to 2,500, from 50 to 3,000, from 100 to 500, from 100 to 750, from 100 to 1,000, from 100 to 1,500, from 100 to 2,000, from 100 to 2,500, from 100 to 3,000, from 500 to 750, from 500 to 1,000, from 500 to 1,500, from 500 to 2,000, from 500 to 2,500, from 500 to 3,000, from 1,000 to 1,500, from 1,000 to 2,000, from 1,000 to 2,500, from 1,000 to 3,000, from 1,500 to 2,000, from 1,500 to 2,500, from 1,500 to 3,000, from 2,000 to 3,000, from 2,000 to 2,500, and from 2,500 to 3,000). In some instances, the poly A tail is designed relative to the length of the overall polynucleotide or the length of a particular region of the polynucleotide. This design can be based on the length of a coding region, the length of a particular feature or region or based on the length of the ultimate product expressed from the polynucleotides. In this context, the poly A tail can be 10, 20, 30, 40, 50, 60, 70, 80, 90, or 100% greater in length than the polynucleotide or feature thereof. The poly A tail can also be designed as a fraction of the polynucleotides to which it belongs. In this context, the poly A tail can be 10, 20, 30, 40, 50, 60, 70, 80, or 90% or more of the total length of the construct, a construct region or the total length of the construct minus the poly A tail. Further, engineered binding sites and conjugation of polynucleotides for Poly A binding protein can enhance expression. Additionally, multiple distinct polynucleotides can be linked together via thePABP (Poly A binding protein) through the 3 -end using modified nucleotides at the3 -terminus of the poly A tail. Transfection experiments can be conducted in relevantcell lines at and protein production can be assayed by ELISA at 12hr, 24hr, 48hr, 72hr and day 7 post-transfection. In some instances, the polynucleotides of the present disclosure are designed to include a poly A-G Quartet region. The G-quartet is a cyclic hydrogen bonded array of four guanine nucleotides that can be formed by G-rich sequences in both DNA and RNA. In some instances, the G-quartet is incorporated at the end of the poly Attorney Docket No.: 45817-0173WO1 A tail. The resultant polynucleotide is assayed for stability, protein production and other parameters including half-life at various time points. It has been discovered that the poly A-G quartet results in protein production from an mRNA equivalent to at least 75% of that seen using a poly A tail of 120 nucleotides alone (SEQ ID NO: 133). In some instances, the poly A tail comprises an alternative nucleoside, e.g., inverted thymidine. Poly A tails comprising an alternative nucleoside, e.g., inverted thymidine, may be generated as described herein. For instance, mRNA constructs may be modified by ligation to stabilize the poly A tail. Ligation may be performedusing 0.5-1.5 mg / mL mRNA (5 Cap1, 3 A100), 50 mM Tris-HCl pH 7.5, 10 mMMgCl2, 1 mM TCEP, 1000 units / mL T4 RNA Ligase 1, 1 mM ATP, 20% w / v polyethylene glycol 8000, and 5:1 molar ratio of modifying oligo to mRNA. Modifying oligo has a sequence of 5’-phosphate-AAAAAAAAAAAAAAAAAAAA- (inverted deoxythymidine (idT) (SEQ ID NO:134)) (see below). Ligation reactions are mixed and incubated at room temperature (~22°C) for, e.g., 4 hours. Stable tail mRNA are purified by, e.g., dT purification, reverse phase purification, hydroxyapatite purification, ultrafiltration into water, and sterile filtration. The resulting stable tail-containing mRNAs contain the following structure at the 3’end, starting with the poly A region: A100-UCUAGAAAAAAAAAAAAAAAAAAAA- inverted deoxythymidine (SEQ ID NO: 59). Modifying oligo to stabilize tail (5’-phosphate-AAAAAAAAAAAAAAAAAAAA- (inverted deoxythymidine) (SEQ ID NO: 134)):

[0003] Attorney Docket No.: 45817-0173WO1 In some instances, the poly A tail comprises A100-UCUAG-A20-inverted deoxy- thymidine (SEQ ID NO: 59). In some instances, the poly A tail consists of A100- UCUAG-A20-inverted deoxy-thymidine (SEQ ID NO: 59). Start codon region The disclosure also includes a polynucleotide that comprises both a start codon region and the polynucleotide described herein (e.g., a polynucleotide comprising a nucleotide sequence encoding an Engager polypeptide). In some instances, the polynucleotides of the present disclosure can have regions that are analogous to or function like a start codon region. In some instances, the translation of a polynucleotide can initiate on a codon that is not the start codon AUG. Translation of the polynucleotide can initiate on an alternative start codon such as, but not limited to, ACG, AGG, AAG, CTG / CUG, GTG / GUG, ATA / AUA, ATT / AUU, TTG / UUG (see Touriol et al. Biology of the Cell 95 (2003) 169-178 and Matsuda and Mauro PLoS ONE, 20105:11; the contents of each of which are herein incorporated by reference in its entirety). As a non-limiting example, the translation of a polynucleotide begins on the alternative start codon ACG. As another non-limiting example, polynucleotide translation begins on the alternative start codon CTG or CUG. As yet another non- Attorney Docket No.: 45817-0173WO1 limiting example, the translation of a polynucleotide begins on the alternative start codon GTG or GUG. Nucleotides flanking a codon that initiates translation such as, but not limited to, a start codon or an alternative start codon, are known to affect the translation efficiency, the length and / or the structure of the polynucleotide. (See, e.g., Matsuda and Mauro PLoS ONE, 20105:11; the contents of which are herein incorporated by reference in its entirety). Masking any of the nucleotides flanking a codon that initiates translation can be used to alter the position of translation initiation, translation efficiency, length and / or structure of a polynucleotide. In some instances, a masking agent can be used near the start codon or alternative start codon in order to mask or hide the codon to reduce the probability of translation initiation at the masked start codon or alternative start codon. Non-limiting examples of masking agents include antisense locked nucleic acids (LNA) polynucleotides and exon-junction complexes (EJCs) (See, e.g., Matsuda and Mauro describing masking agents LNA polynucleotides and EJCs (PLoS ONE, 20105:11); the contents of which are herein incorporated by reference in its entirety). In some instances, a masking agent can be used to mask a start codon of a polynucleotide in order to increase the likelihood that translation will initiate on an alternative start codon. In some instances, a masking agent can be used to mask a first start codon or alternative start codon in order to increase the chance that translation will initiate on a start codon or alternative start codon downstream to the masked start codon or alternative start codon. In some instances, a start codon or alternative start codon can be located within a perfect complement for a miRNA binding site. The perfect complement of a miRNA binding site can help control the translation, length and / or structure of the polynucleotide similar to a masking agent. As a non-limiting example, the start codon or alternative start codon can be located in the middle of a perfect complement for a miRNA binding site. The start codon or alternative start codon can be located after the first nucleotide, second nucleotide, third nucleotide, fourth nucleotide, fifth Attorney Docket No.: 45817-0173WO1 nucleotide, sixth nucleotide, seventh nucleotide, eighth nucleotide, ninth nucleotide, tenth nucleotide, eleventh nucleotide, twelfth nucleotide, thirteenth nucleotide, fourteenth nucleotide, fifteenth nucleotide, sixteenth nucleotide, seventeenth nucleotide, eighteenth nucleotide, nineteenth nucleotide, twentieth nucleotide or twenty-first nucleotide. In some instances, the start codon of a polynucleotide can be removed from the polynucleotide sequence in order to have the translation of the polynucleotide begin on a codon that is not the start codon. Translation of the polynucleotide can begin on the codon following the removed start codon or on a downstream start codon or an alternative start codon. In a non-limiting example, the start codon ATG or AUG is removed as the first 3 nucleotides of the polynucleotide sequence in order to have translation initiate on a downstream start codon or alternative start codon. The polynucleotide sequence where the start codon was removed can further comprise at least one masking agent for the downstream start codon and / or alternative start codons in order to control or attempt to control the initiation of translation, the length of the polynucleotide and / or the structure of the polynucleotide. In some instances, the poly A tail may be 80 nucleotides, 120 nucleotides, or 160 nucleotides in length (SEQ ID NO: 219). In some instances, the poly A tail may be 20, 40, 80, 100, 120, 140 or 160 nucleotides in length (SEQ ID NO: 220). In some instances, the mRNA comprises a 100 nucleotide poly A tail (SEQ ID NO: 132). Stop Codon Region The present disclosure also includes a polynucleotide that comprises both a stop codon region and the polynucleotide described herein (e.g., a polynucleotide comprising a nucleotide sequence encoding an Engager polypeptide). In some instances, the polynucleotides of the present disclosure can include at least two stopcodons before the 3 untranslated region (UTR). The stop codon can be selected fromTGA, TAA and TAG in the case of DNA, or from UGA, UAA and UAG in the case of RNA. In some instances, the polynucleotides of the present disclosure include the stop codon TGA in the case of DNA, or the stop codon UGA in the case of RNA, and Attorney Docket No.: 45817-0173WO1 one additional stop codon. In a further embodiment the additional stop codon can be TAA or UAA. In some instances, the polynucleotides of the present disclosure include three consecutive stop codons, four stop codons, or more. Combination of mRNA elements Any of the polynucleotides disclosed herein can comprise one, two, three, or all of the following elements: (a) a 5’-UTR, e.g., as described herein; (b) a coding region comprising a stop element (e.g., as described herein); (c) a 3’-UTR (e.g., as described herein) and; optionally (d) a 3’ stabilizing region, e.g., as described herein. Also disclosed herein are LNP compositions comprising the same. In some instances, a polynucleotide of the disclosure comprises (a) a 5’ UTR described in Table 10 or a variant or fragment thereof and (b) a coding region comprising a stop element provided herein. In some instances, the polynucleotide further comprises a cap structure, e.g., as described herein, or a poly A tail, e.g., as described herein. In some instances, the polynucleotide further comprises a 3’ stabilizing region, e.g., as described herein. In some instances, a polynucleotide of the disclosure comprises (a) a 5’ UTR described in Table 10 or a variant or fragment thereof and (c) a 3’ UTR described in Table 11 or a variant or fragment thereof. In some instances, the polynucleotide further comprises a cap structure, e.g., as described herein, or a poly A tail, e.g., as described herein. In some instances, the polynucleotide further comprises a 3’ stabilizing region, e.g., as described herein. In some instances, a polynucleotide of the disclosure comprises (c) a 3’ UTR described in Table 11 or a variant or fragment thereof and (b) a coding region comprising a stop element provided herein. In some instances, the polynucleotide comprises a sequence provided in Table 12. In some instances, the polynucleotide further comprises a cap structure, e.g., as described herein, or a poly A tail, e.g., as described herein. In some instances, the polynucleotide further comprises a 3’ stabilizing region, e.g., as described herein. Attorney Docket No.: 45817-0173WO1 In some instances, a polynucleotide of the disclosure comprises (a) a 5’ UTR described in Table 10 or a variant or fragment thereof; (b) a coding region comprising a stop element provided herein; and (c) a 3’ UTR described in Table 11 or a variant or fragment thereof. In some instances, the polynucleotide further comprises a cap structure, e.g., as described herein, or a poly A tail, e.g., as described herein. In some instances, the polynucleotide further comprises a 3’ stabilizing region, e.g., as described herein. Table 12 – Exemplary 3’ UTR and stop element sequences A A A A A A A A A G C Attorney Docket No.: 45817-0173WO1 C Identification and Ratio Determination (IDR) Sequences In some aspects, a polynucleotide of this disclosure (e.g., an mRNA or mRNAs) comprises an Identification and Ratio Determination (IDR) sequence. An IDR sequence is a sequence of a biological molecule (e.g., nucleic acid or protein) that, when combined with the sequence of a target biological molecule, serves to identify the target biological molecule. Typically, an IDR sequence is a heterologous sequence that is incorporated within or appended to a sequence of a target biological molecule and can be used as a reference to identify the target molecule. Thus, in some cases, a nucleic acid (e.g., mRNA or mRNAs) comprises (i) a target sequence of interest (e.g., a coding sequence encoding a therapeutic and / or antigenic peptide or protein); and (ii) a unique IDR sequence. An RNA species (e.g., RNA having a given coding sequence) may comprise an IDR sequence that differs from the IDR sequence of other RNA species (e.g., RNA(s) having different coding sequence(s)). Each IDR sequence thus identifies a particular RNA species, and so the abundance of IDR sequences may be measured to determine the abundance of each RNA species in a composition. Use of distinct IDR sequences to identify RNA species allows for analysis of multivalent RNA compositions (e.g., containing multiple RNA species) containing RNA species with similar coding sequences and / or lengths, which could otherwise be difficult to distinguish using PCR- or chromatography-based analysis of full-length RNAs. Each RNA species in a multivalent RNA composition may comprise an IDR sequence that is not a sequence isomer of an IDR sequence of another RNA species in a multivalent RNA composition (e.g., the IDR sequence does not have the same number of adenosine nucleotides, the same number of cytosine nucleotides, the same number of guanine nucleotides, and the same number of uracil nucleotides, as another Attorney Docket No.: 45817-0173WO1 IDR sequence in the composition, even if those sequences have different sequences). Having identical nucleotide compositions causes sequence isomers to have the same mass, presenting a challenge to distinguishing sequence isomers using mass-based identification methods (e.g., mass spectrometry). Each RNA species in a multivalent RNA composition may comprise an IDR sequence having a mass that differs from the mass of IDR sequences of each other RNA species in a multivalent RNA composition. For example, the mass of each IDR sequence may differ from the mass of other IDR sequences by at least 9 Da, at least 25 Da, at least 25 Da, or at least 50 Da. Use of IDR sequences with distinct masses allows RNA fragments comprising different IDR sequences to be distinguished using mass-based analysis methods (e.g., mass spectrometry), which do not require reverse transcription, amplification, or sequencing of RNAs. Each RNA species in an RNA composition may comprises an IDR sequence with a different length. For example, each IDR sequence may have a length independently selected from 0 to 25 nucleotides. The length of a nucleic acid influences the rate at which the nucleic acid traverses a chromatography column, and so the use of IDR sequences of different lengths on different RNA species allows RNA fragments having different IDR sequences to be distinguished using chromatography-based methods (e.g., LC-UV). IDR sequences may be chosen such that no IDR sequence comprises a start codon, ‘AUG’. Lack of a start codon in an IDR sequence prevents undesired translation of nucleotide sequences within and / or downstream from the IDR sequence. IDR sequences may be chosen such that no IDR sequence comprises a recognition site for a restriction enzyme. In one example, no IDR sequence comprises a recognition site for XbaI, ‘UCUAG’. Lack of a recognition site for a restriction enzyme (e.g., XbaI recognition site ‘UCUAG’) allows the restriction enzyme to be used in generating and modifying a DNA template for in vitro transcription, without affecting the IDR sequence or sequence of the transcribed RNA. In some cases, the IDR sequence may be inserted in a 3’UTR and / or a poly A tail. Attorney Docket No.: 45817-0173WO1 In some instances, the IDR sequence is inserted in a 3’UTR. In one case, the IDR sequence consists of 15 nucleotides (e.g., AGAAAUAAAUUAAUU (SEQ ID NO:173)). In another case, the IDR sequence consists of 9 to 15 nucleotides, wherein no IDR sequence comprises a recognition site for a restriction enzyme. In one instance, the 3’UTR with an IDR is shown below: UAAAGCUCCCCGGGGCAAACACCAUUGUCACACUCCAGCCUCGGUGGC CUAGCCAAACACCAUUGUCACACUCCAUUCUUGCCCCUUGGGCCCAAAC ACCAUUGUCACACUCCAUCCCCCCAGCCCCUCCUCCCCUUCCUGCA(X)nG UGGUCUUUGAAUAAAGUCUGAGUGGGCGGC (SEQ ID NO:174), wherein n = 9 to 15 and wherein each X is independently an A, U, C, or G. Polynucleotide Comprising an mRNA Encoding an Engager polypeptide In some instances, a polynucleotide of the present disclosure, for example a polynucleotide comprising an mRNA nucleotide sequence encoding an Engagerpolypeptide, comprises from 5 to 3 end:(i) a 5 cap such as provided above;(ii) a 5 UTR, such as the sequences provided above;(iii) an ORF encoding a human Engager polypeptide; (iv) at least one stop codon;(v) a 3 UTR, such as the sequences provided above; and(vi) a poly A tail provided above. Methods of Making Polynucleotides The present disclosure also provides methods for making a polynucleotide of the present disclosure (e.g., a polynucleotide comprising a nucleotide sequence encoding an Engager polypeptide) or a complement thereof. In some aspects, a polynucleotide (e.g., a RNA, e.g., an mRNA) disclosed herein, and encoding an Engager polypeptide, can be constructed using in vitro transcription (IVT). In other aspects, a polynucleotide (e.g., a RNA, e.g., an mRNA) disclosed herein, and encoding an Engager polypeptide, can be constructed by chemical synthesis using an oligonucleotide synthesizer. Attorney Docket No.: 45817-0173WO1 In other aspects, a polynucleotide (e.g., a RNA, e.g., an mRNA) disclosed herein, and encoding an Engager polypeptide is made by using a host cell. In certain aspects, a polynucleotide (e.g., a RNA, e.g., an mRNA) disclosed herein, and encoding an Engager polypeptide is made by one or more combination of the IVT, chemical synthesis, host cell expression, or any other methods known in the art. Naturally occurring nucleosides, non-naturally occurring nucleosides, or combinations thereof, can totally or partially naturally replace occurring nucleosides present in the candidate nucleotide sequence and can be incorporated into a sequence- optimized nucleotide sequence (e.g., a RNA, e.g., an mRNA) encoding an Engager polypeptide. The resultant polynucleotides, e.g., mRNAs, can then be examined for their ability to produce protein and / or produce a therapeutic outcome. In Vitro Transcription / Enzymatic Synthesis The present disclosure also provides methods for making a polynucleotide disclosed herein or a complement thereof. In some aspects, a polynucleotide (e.g., an mRNA) disclosed herein can be constructed using in vitro transcription. In other aspects, a polynucleotide (e.g., an mRNA) disclosed herein can be constructed by chemical synthesis using an oligonucleotide synthesizer. In other aspects, a polynucleotide (e.g., an mRNA) disclosed herein is made by using a host cell. In certain aspects, a polynucleotide (e.g., an mRNA) disclosed herein is made by one or more combination of the IVT, chemical synthesis, host cell expression, or any other methods known in the art. Naturally occurring nucleosides, non-naturally occurring nucleosides, or combinations thereof, can totally or partially naturally replace occurring nucleosides present in the candidate nucleotide sequence and can be incorporated into a sequence- optimized nucleotide sequence (e.g., an mRNA) encoding an engager polypeptide. The resultant mRNAs can then be examined for their ability to produce a therapeutic outcome. Attorney Docket No.: 45817-0173WO1 While RNA can be made synthetically using methods well known in the art, In some instances an RNA transcript (e.g., mRNA transcript) is synthesized by contacting a DNA template with a RNA polymerase (e.g., a T7 RNA polymerase or a T7 RNA polymerase variant) under conditions that result in the production of RNA transcript. In some aspects, the present disclosure provides methods of performing an IVT (in vitro transcription) reaction, comprising contacting a DNA template with the RNA polymerase (e.g., a T7 RNA polymerase, such as a T7 RNA polymerase variant) in the presence of nucleoside triphosphates and buffer under conditions that result in the production of RNA transcripts. Other aspects of the present disclosure provide capping methods, e.g., co- transcriptional capping methods or other methods known in the art. In some instances, a capping method comprises reacting a polynucleotide template with a T7 RNA polymerase variant, nucleoside triphosphates, and a cap analog under in vitro transcription reaction conditions to produce RNA transcript. IVT conditions typically require a purified linear DNA template containing a promoter, nucleoside triphosphates, a buffer system that includes dithiothreitol (DTT) and magnesium ions, and a RNA polymerase. The exact conditions used in the transcription reaction depend on the amount of RNA needed for a specific application. Typical IVT reactions are performed by incubating a DNA template with a RNA polymerase and nucleoside triphosphates, including GTP, ATP, CTP, and UTP (ornucleotide analogs) in a transcription buffer. A RNA transcript having a 5 terminalguanosine triphosphate is produced from this reaction. A deoxyribonucleic acid (DNA) is simply a nucleic acid template for RNA polymerase. A DNA template may include a polynucleotide encoding an Engager polypeptide. A DNA template, in some instances, includes a RNA polymerase promoter (e.g., a T7 RNA polymerase promoter) located 5' from and operably linked to polynucleotide encoding an Engager polypeptide. A DNA template may also Attorney Docket No.: 45817-0173WO1 include a nucleotide sequence encoding a polyadenylation (poly A) tail located at the 3' end of the gene of interest. Polypeptides of interest include, but are not limited to, biologics, antibodies, antigens (vaccines), and therapeutic proteins. The term “protein” encompasses peptides. A RNA transcript, in some instances, is the product of an IVT reaction and, as will be understood by one of ordinary skill in the art, the DNA template for making an RNA molecule is known based on base complementarity. A RNA transcript, in some instances, is a messenger RNA (mRNA) that includes a nucleotide sequence encoding a polypeptide of interest linked to a poly A tail. In some instances, the mRNA is modified mRNA (mmRNA), which includes at least one modified nucleotide. A nucleotide includes a nitrogenous base, a five-carbon sugar (ribose or deoxyribose), and at least one phosphate group. Nucleotides include nucleoside monophosphates, nucleoside diphosphates, and nucleoside triphosphates. A nucleoside monophosphate (NMP) includes a nucleobase linked to a ribose and a single phosphate; a nucleoside diphosphate (NDP) includes a nucleobase linked to a ribose and two phosphates; and a nucleoside triphosphate (NTP) includes a nucleobase linked to a ribose and three phosphates. Nucleotide analogs are compounds that have the general structure of a nucleotide or are structurally similar to a nucleotide. Nucleotide analogs, for example, include an analog of the nucleobase, an analog of the sugar and / or an analog of the phosphate group(s) of a nucleotide. A nucleoside includes a nitrogenous base and a 5-carbon sugar. Thus, a nucleoside plus a phosphate group yields a nucleotide. Nucleoside analogs are compounds that have the general structure of a nucleoside or are structurally similar to a nucleoside. Nucleoside analogs, for example, include an analog of the nucleobase and / or an analog of the sugar of a nucleoside. It should be understood that the term “nucleotide” includes naturally-occurring nucleotides, synthetic nucleotides and modified nucleotides, unless indicated Attorney Docket No.: 45817-0173WO1 otherwise. Examples of naturally-occurring nucleotides used for the production of RNA, e.g., in an IVT reaction, as provided herein include adenosine triphosphate (ATP), guanosine triphosphate (GTP), cytidine triphosphate (CTP), uridine triphosphate (UTP), and 5-methyluridine triphosphate (m5UTP). In some instances, adenosine diphosphate (ADP), guanosine diphosphate (GDP), cytidine diphosphate (CDP), and / or uridine diphosphate (UDP) are used. Examples of nucleotide analogs include, but are not limited to, antiviral nucleotide analogs, phosphate analogs (soluble or immobilized, hydrolyzable or non- hydrolyzable), dinucleotide, trinucleotide, e.g., a cap analog, or a precursor / substrate for enzymatic capping (vaccinia or ligase), a nucleotide labeled with a functionalgroup to facilitate ligation / conjugation of cap or 5 moiety (IRES), a nucleotidelabeled with a 5 PO4 to facilitate ligation of cap or 5 moiety, or a nucleotide labeledwith a functional group / protecting group that can be chemically or enzymatically cleaved. Examples of antiviral nucleotide / nucleoside analogs include, but are not limited, to Ganciclovir, Entecavir, Telbivudine, Vidarabine and Cidofovir. Modified nucleotides may include modified nucleobases. For example, a RNA transcript (e.g., mRNA transcript) of the present disclosure may include a modifiednucleobase selected from pseudouridine ( ), 1-methylpseudouridine (m1 ), 1-ethylpseudouridine, 2-thiouridine, 4’-thiouridine, 2-thio-1-methyl-1-deaza- pseudouridine, 2-thio-1-methyl-pseudouridine, 2-thio-5-aza-uridine , 2-thio- dihydropseudouridine, 2-thio-dihydrouridine, 2-thio-pseudouridine, 4-methoxy-2- thio-pseudouridine, 4-methoxy-pseudouridine, 4-thio-1-methyl-pseudouridine, 4-thio- pseudouridine, 5-aza-uridine, dihydropseudouridine, 5-methyluridine, 5- methoxyuridine (mo5U) and 2’-O-methyl uridine. In some instances, a RNA transcript (e.g., mRNA transcript) includes a combination of at least two (e.g., 2, 3, 4 or more) of the foregoing modified nucleobases. The nucleoside triphosphates (NTPs) as provided herein may comprise unmodified or modified ATP, modified or unmodified UTP, modified or unmodified GTP, and / or modified or unmodified CTP. In some instances, NTPs of an IVT Attorney Docket No.: 45817-0173WO1 reaction comprise unmodified ATP. In some instances, NTPs of an IVT reaction comprise modified ATP. In some instances, NTPs of an IVT reaction comprise unmodified UTP. In some instances, NTPs of an IVT reaction comprise modified UTP. In some instances, NTPs of an IVT reaction comprise unmodified GTP. In some instances, NTPs of an IVT reaction comprise modified GTP. In some instances, NTPs of an IVT reaction comprise unmodified CTP. In some instances, NTPs of an IVT reaction comprise modified CTP. The concentration of nucleoside triphosphates and cap analog present in an IVT reaction may vary. In some instances, NTPs and cap analog are present in the reaction at equimolar concentrations. In some instances, the molar ratio of cap analog (e.g., trinucleotide cap) to nucleoside triphosphates in the reaction is greater than 1:1. For example, the molar ratio of cap analog to nucleoside triphosphates in the reaction may be 2:1, 3:1, 4:1, 5:1, 6:1, 7:1, 8:1, 9:1, 10:1, 15:1, 20:1, 25:1, 50:1, or 100:1. In some instances, the molar ratio of cap analog (e.g., trinucleotide cap) to nucleoside triphosphates in the reaction is less than 1:1. For example, the molar ratio of cap analog (e.g., trinucleotide cap) to nucleoside triphosphates in the reaction may be 1:2, 1:3, 1:4, 1:5, 1:6, 1:7, 1:8, 1:9, 1:10, 1:15, 1:20, 1:25, 1:50, or 1:100. The composition of NTPs in an IVT reaction may also vary. For example, ATP may be used in excess of GTP, CTP and UTP. As a non-limiting example, an IVT reaction may include 7.5 millimolar GTP, 7.5 millimolar CTP, 7.5 millimolar UTP, and 3.75 millimolar ATP. The same IVT reaction may include 3.75 millimolar cap analog (e.g., trinucleotide cap). In some instances, the molar ratio of G:C:U:A:cap is 1:1:1:0.5:0.5. In some instances, the molar ratio of G:C:U:A:cap is 1:1:0.5:1:0.5. In some instances, the molar ratio of G:C:U:A:cap is 1:0.5:1:1:0.5. In some instances, the molar ratio of G:C:U:A:cap is 0.5:1:1:1:0.5. In some instances, a RNA transcript (e.g., mRNA transcript) includes amodified nucleobase selected from pseudouridine ( ), 1-methylpseudouridine (m1 ),5-methoxyuridine (mo5U), 5-methylcytidine (m5C), -thio-guanosine and -thio- adenosine. In some instances, a RNA transcript (e.g., mRNA transcript) includes a Attorney Docket No.: 45817-0173WO1 combination of at least two (e.g., 2, 3, 4 or more) of the foregoing modified nucleobases. In some instances, a RNA transcript (e.g., mRNA transcript) includespseudouridine ( ). In some instances, a RNA transcript (e.g., mRNA transcript)includes 1-methylpseudouridine (m1). In some instances, a RNA transcript (e.g., mRNA transcript) includes 5-methoxyuridine (mo5U). In some instances, a RNA transcript (e.g., mRNA transcript) includes 5-methylcytidine (m5C). In some instances, a RNA transcript (e.g., mRNA transcript) includes -thio-guanosine. In some instances, a RNA transcript (e.g., mRNA transcript) includes -thio-adenosine. In some instances, the polynucleotide (e.g., RNA polynucleotide, such as mRNA polynucleotide) is uniformly modified (e.g., fully modified, modified throughout the entire sequence) for a particular modification. For example, a polynucleotide can be uniformly modified with 1-methylpseudouridine (m1), meaning that all uridine residues in the mRNA sequence are replaced with 1- methylpseudouridine (m1). Similarly, a polynucleotide can be uniformly modified for any type of nucleoside residue present in the sequence by replacement with a modified residue such as any of those set forth above. Alternatively, the polynucleotide (e.g., RNA polynucleotide, such as mRNA polynucleotide) may not be uniformly modified (e.g., partially modified, part of the sequence is modified). Each possibility represents a separate embodiment of the present disclosure. In some instances, the buffer system contains tris. The concentration of tris used in an IVT reaction, for example, may be at least 10 mM, at least 20 mM, at least 30 mM, at least 40 mM, at least 50 mM, at least 60 mM, at least 70 mM, at least 80 mM, at least 90 mM, at least 100 mM or at least 110 mM phosphate. In some instances, the concentration of phosphate is 20-60 mM or 10-100 mM. In some instances, the buffer system contains dithiothreitol (DTT). The concentration of DTT used in an IVT reaction, for example, may be at least 1 mM, at least 5 mM, or at least 50 mM. In some instances, the concentration of DTT used in Attorney Docket No.: 45817-0173WO1 an IVT reaction is 1-50 mM or 5-50 mM. In some instances, the concentration of DTT used in an IVT reaction is 5 mM. In some instances, the buffer system contains magnesium. In some instances, the molar ratio of NTP to magnesium ions (Mg2+; e.g., MgCl2) present in an IVT reaction is 1:1 to 1:5. For example, the molar ratio of NTP to magnesium ions may be 1:1, 1:2, 1:3, 1:4 or 1:5. In some instances, the molar ratio of NTP plus cap analog (e.g., trinucleotide cap, such as GAG) to magnesium ions (Mg2+; e.g., MgCl2) present in an IVT reaction is 1:1 to 1:5. For example, the molar ratio of NTP+trinucleotide cap (e.g., GAG) to magnesium ions may be 1:1, 1:2, 1:3, 1:4 or 1:5. In some instances, the buffer system contains Tris-HCl, spermidine (e.g., at a concentration of 1-30 mM), TRITON®X-100 (polyethylene glycol p-(1,1,3,3- tetramethylbutyl)-phenyl ether) and / or polyethylene glycol (PEG). The addition of nucleoside triphosphates (NTPs) to the 3 end of a growingRNA strand is catalyzed by a polymerase, such as T7 RNA polymerase, for example, any one or more of the T7 RNA polymerase variants (e.g., G47A) of the present disclosure. In some instances, the RNA polymerase (e.g., T7 RNA polymerase variant) is present in a reaction (e.g., an IVT reaction) at a concentration of 0.01 mg / ml to 1 mg / ml. For example, the RNA polymerase may be present in a reaction at a concentration of 0.01 mg / mL, 0.05 mg / ml, 0.1 mg / ml, 0.5 mg / ml or 1.0 mg / ml. In some instances, the polynucleotide of the present disclosure is an IVT polynucleotide. Traditionally, the basic components of an mRNA molecule include atleast a coding region, a 5 UTR, a 3 UTR, a 5 cap and a poly A tail. The IVTpolynucleotides of the present disclosure can function as mRNA but are distinguished from wild-type mRNA in their functional and / or structural design features which serve, e.g., to overcome existing problems of effective polypeptide production using nucleic-acid based therapeutics. Attorney Docket No.: 45817-0173WO1 The primary construct of an IVT polynucleotide comprises a first region of linked nucleotides that is flanked by a first flanking region and a second flaking region. This first region can include, but is not limited to, the encoded Engager polypeptide. The first flanking region can include a sequence of linked nucleosides which function as a 5’ untranslated region (UTR) such as the 5’ UTR of any of the nucleic acids encoding the native 5’ UTR of the polypeptide or a non-native 5’UTR such as, but not limited to, a heterologous 5’ UTR or a synthetic 5’ UTR. The IVT encoding an Engager polypeptide can comprise at its 5 terminus a signal sequence region encoding one or more signal sequences. The flanking region can comprise aregion of linked nucleotides comprising one or more complete or incomplete 5 UTRssequences. The flanking region can also comprise a 5 terminal cap. The secondflanking region can comprise a region of linked nucleotides comprising one or morecomplete or incomplete 3 UTRs which can encode the native 3’ UTR of an Engagerpolypeptide, or a non-native 3’ UTR such as, but not limited to, a heterologous 3’UTR or a synthetic 3’ UTR. The flanking region can also comprise a 3 tailingsequence. The 3’ tailing sequence can be, but is not limited to, a poly A tail, a poly A- G quartet and / or a stem loop sequence. Additional and exemplary features of IVT polynucleotide architecture and methods of making a polynucleotide are disclosed in PCT International application WO 2017 / 201325, filed on 18 May 2017, the entire contents of which are hereby incorporated by reference. Chemical synthesis Standard methods can be applied to synthesize an isolated polynucleotide sequence encoding an isolated polypeptide of interest, such as a polynucleotide of the present disclosure (e.g., a polynucleotide comprising a nucleotide sequence encoding an Engager polypeptide). For example, a single DNA or RNA oligomer containing a codon-optimized nucleotide sequence coding for the particular isolated polypeptide can be synthesized. In other aspects, several small oligonucleotides coding for portions of the desired polypeptide can be synthesized and then ligated. In some Attorney Docket No.: 45817-0173WO1aspects, the individual oligonucleotides typically contain 5 or 3 overhangs forcomplementary assembly. A polynucleotide disclosed herein (e.g., a RNA, e.g., an mRNA) can be chemically synthesized using chemical synthesis methods and potential nucleobase substitutions known in the art. See, for example, International Publication Nos. WO2014093924, WO2013052523; WO2013039857, WO2012135805, WO2013151671; U.S. Publ. No. US20130115272; or U.S. Pat. Nos. US8999380 or US8710200, all of which are herein incorporated by reference in their entireties. Pharmaceutical Compositions Pharmaceutical compositions containing a T cell engager as described herein or nucleic acid encoding the same can be prepared using methods known in the art. Pharmaceutical compositions described herein may contain a T cell engager or nucleic acid encoding the same in combination with one or more pharmaceutically acceptable excipients. For instance, pharmaceutical compositions described herein can be prepared using physiologically acceptable carriers, excipients, or stabilizers (Remington's Pharmaceutical Sciences (19th ed., 1995), incorporated herein by reference), and in a desired form, e.g., in the form of lyophilized formulations or aqueous solutions. The compositions can also be prepared so as to contain the active agent (e.g., T cell engager or nucleic acid encoding the same) at a desired concentration. For example, a pharmaceutical composition described herein may contain at least 10% (e.g., 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95%, 97%, 98%, 99%, 99.5%, 99.9%, or 100%) active agent by weight (w / w). Additionally, an active agent that can be incorporated into a pharmaceutical formulation can itself have a desired level of purity. For example, a polypeptide or nucleic acid described herein may be characterized by a certain degree of purity after isolating it from cell culture media or after chemical synthesis Pharmaceutical compositions can be prepared for storage as lyophilized formulations or aqueous solutions by mixing the active agent having the desired Attorney Docket No.: 45817-0173WO1 degree of purity with optional pharmaceutically acceptable carriers, excipients or stabilizers typically employed in the art, e.g., buffering agents, stabilizing agents, preservatives, isotonifiers, non-ionic detergents, antioxidants, and other miscellaneous additives. See, e.g., Remington's Pharmaceutical Sciences (19th ed., 1995), incorporated herein by reference). Such additives must be nontoxic to the recipients at the dosages and concentrations employed. Buffering agents Buffering agents help to maintain the pH in the range which approximates physiological conditions. Suitable buffering agents for use with the pharmaceutical compositions of the disclosure include both organic and inorganic acids and salts thereof, such as citrate buffers (e.g., monosodium citrate-disodium citrate mixture, citric acid-trisodium citrate mixture, citric acid-monosodium citrate mixture, etc.), succinate buffers (e.g., succinic acid- monosodium succinate mixture, succinic acid- sodium hydroxide mixture, succinic acid- disodium succinate mixture, etc.), tartrate buffers (e.g., tartaric acid-sodium tartrate mixture, tartaric acid-potassium tartrate mixture, tartaric acid-sodium hydroxide mixture, etc.), fumarate buffers (e.g., fumaric acid-monosodium fumarate mixture, fumaric acid- disodium fumarate mixture, monosodium fumarate-disodium fumarate mixture, etc.), gluconate buffers (e.g., gluconic acid-sodium gluconate mixture, gluconic acid-sodium hydroxide mixture, gluconic acid-potassium gluconate mixture, etc.), oxalate buffer (e.g., oxalic acid- sodium oxalate mixture, oxalic acid-sodium hydroxide mixture, oxalic acid-potassium oxalate mixture, etc.), lactate buffers (e.g., lactic acid-sodium lactate mixture, lactic acid-sodium hydroxide mixture, lactic acid-potassium lactate mixture, etc.), and acetate buffers (e.g., acetic acid-sodium acetate mixture, acetic acid-sodium hydroxide mixture, etc.). Additionally, phosphate buffers, histidine buffers, and trimethylamine salts such as Tris can be used. Preservatives Preservatives can be added to a composition described herein, for example, to inhibit microbial growth. Suitable preservatives for use with the pharmaceutical Attorney Docket No.: 45817-0173WO1 compositions of the disclosure include phenol, benzyl alcohol, meta-cresol, methyl paraben, propyl paraben, octadecyldimethylbenzyl ammonium chloride, benzalconium halides (e.g., chloride, bromide, and iodide), hexamethonium chloride, and alkyl parabens such as methyl or propyl paraben, catechol, resorcinol, cyclohexanol, and 3-pentanol. Isotonifiers, also known as “stabilizers,” can be added to ensure isotonicity of liquid compositions described herein and include polyhydric sugar alcohols, for example trihydric or higher sugar alcohols, such as glycerin, arabitol, xylitol, sorbitol, and mannitol. Stabilizers refer to a broad category of excipients which can range in function from a bulking agent to an additive which solubilizes the therapeutic agent or helps to prevent denaturation or adherence to the container wall. Typical stabilizers can be polyhydric sugar alcohols; amino acids such as arginine, lysine, glycine, glutamine, asparagine, histidine, alanine, ornithine, L- leucine, 2-phenylalanine, glutamic acid, threonine, etc.; organic sugars or sugar alcohols, such as lactose, trehalose, stachyose, mannitol, sorbitol, xylitol, ribitol, myoinisitol, galactitol, glycerol and the like, including cyclitols such as inositol; polyethylene glycol; amino acid polymers; sulfur containing reducing agents, such as urea, glutathione, thioctic acid, sodium thioglycolate, thioglycerol, a- monothioglycerol and sodium thio sulfate; low molecular weight polypeptides (e.g., peptides of 10 residues or fewer); proteins such as HAS, BSA, MSA, gelatin, or immunoglobulins; hydrophilic polymers, such as polyvinylpyrrolidone monosaccharides, such as xylose, mannose, fructose, glucose; disaccharides such as lactose, maltose, sucrose and trisaccharides such as raffinose; and polysaccharides such as dextran. Detergents In some instances, non-ionic surfactants or detergents (also known as “wetting agents”) are added to the pharmaceutical composition, for example, to help solubilize the therapeutic agent as well as to protect the therapeutic agent against agitation- induced aggregation, which also permits the formulation to be exposed to shear surface stressed without causing denaturation of the protein. Suitable non-ionic surfactants include, for example and without limitation, polysorbates (20, 80, etc.), Attorney Docket No.: 45817-0173WO1 polyoxamers (184, 188 etc.), Pluronic polyols, polyoxyethylene sorbitan monoethers (TWEEN®-20, TWEEN®-80, etc.). Other pharmaceutical carriers Alternative pharmaceutically acceptable carriers that can be incorporated into a pharmaceutical composition described herein may include dextrose, sucrose, sorbitol, mannitol, starch, rubber arable, potassium phosphate, arginate, gelatin, potassium silicate, microcrystalline cellulose, polyvinylpyrrolidone, cellulose, water, syrups, methyl cellulose, methylhydroxy benzoate, propylhydroxy benzoate, talc, magnesium stearate, and mineral oils, but not limited to. A pharmaceutical composition described herein may further include a lubricant, a humectant, a sweetener, a flavoring agent, an emulsifier, a suspending agent, and a preservative. Details of suitable pharmaceutically acceptable carriers and formulations can be found in Remington's Pharmaceutical Sciences (19th ed., 1995), which is incorporated herein by reference. Lipid Nanoparticle (LNP) Compositions The present disclosure provides LNP compositions with advantageous properties. The lipid nanoparticle compositions described herein may be used for the delivery of therapeutic and / or prophylactic agents, e.g., nucleic acids such as mRNAs, to mammalian cells or organs. For example, the lipid nanoparticles described herein have little or no immunogenicity. For example, the lipid compounds disclosed herein have a lower immunogenicity as compared to a reference lipid (e.g., MC3, KC2, or DLinDMA). For example, a formulation comprising a lipid disclosed herein and a therapeutic or prophylactic agent, e.g., mRNA, has an increased therapeutic index as compared to a corresponding formulation which comprises a reference lipid (e.g., MC3, KC2, or DLinDMA) and the same therapeutic or prophylactic agent. In some instances, the present application provides pharmaceutical compositions comprising: (a) a delivery agent comprising a lipid nanoparticle; and (b) Attorney Docket No.: 45817-0173WO1 polynucleotides (e.g., mRNAs) comprising nucleotide sequences encoding one or more (1, 2, 3) of the T cell engager(s) of the disclosure. Lipid Nanoparticles In some instances, polynucleotides of the present disclosure (e.g., mRNA) are included in a lipid nanoparticle (LNP). Lipid nanoparticles according to the present disclosure may comprise: (i) an ionizable amino lipid; (ii) a sterol or other structural lipid; (iii) a non-cationic helper lipid or phospholipid; and (iv) a PEG-modified lipid. In some instances, polynucleotides (e.g., mRNA) encoding one or more (1, 2, 3) of the T cell engager(s) of the disclosure are formulated in a delivery vehicle such as a nanoparticle (e.g., LNP). The lipid nanoparticles according to the present disclosure can be generated using components, compositions, and methods as are generally known in the art, see, for example PCT / US2016 / 052352; PCT / US2016 / 068300; PCT / US2017 / 037551; PCT / US2015 / 027400; PCT / US2016 / 047406; PCT / US2016000129; PCT / US2016 / 014280; PCT / US2016 / 014280; PCT / US2017 / 038426; PCT / US2014 / 027077; PCT / US2014 / 055394; PCT / US2016 / 52117; PCT / US2012 / 069610; PCT / US2017 / 027492; PCT / US2016 / 059575 and PCT / US2016 / 069491 all of which are incorporated by reference herein in their entirety. In some instances, the lipid nanoparticle comprises an ionizable cationic lipid (e.g., an ionizable amino lipid) at a content of 20-60 mole ratio%, 25-60 mole ratio%, 30-60 mole ratio%, 35-60 mole ratio%, 40-60 mole ratio%, 45-60 mole ratio%, 20-55 mole ratio%, 25-55 mole ratio%, 30-55 mole ratio%, 35-55 mole ratio%, 40-55 mole ratio%, 45-55 mole ratio%, 20-50 mole ratio%, 25-50 mole ratio%, 30-50 mole ratio%, 35-50 mole ratio%, or 40-50 mole ratio%. For example, the lipid nanoparticle may comprise an ionizable cationic lipid (e.g., an ionizable amino lipid) at a content of 40-50 mole ratio%, 45-50 mole ratio%, 45-46 mole ratio%, 46-47 mole ratio%, 47- 48 mole ratio%, 48-49 mole ratio%, or 49-50 mole ratio%, for example about 45 mole ratio%, about 45.5 mole ratio%, about 46 mole ratio%, about 46.5 mole ratio%, about Attorney Docket No.: 45817-0173WO1 47 mole ratio%, about 47.5 mole ratio%, about 47.8 mole ratio%, about 48 mole ratio%, about 48.5 mole ratio%, about 49 mole ratio%, or about 49.5 mole ratio% ionizable cationic lipid (e.g., an ionizable amino lipid). In one instance, the lipid nanoparticle comprises an ionizable amino lipid (e.g., Compound 2) at a content of about 47.8 mole ratio%. In another instance, the lipid nanoparticle comprises an ionizable amino lipid (e.g., Compound 2) at a content of 47.8 mole ratio%. In some instances, the lipid nanoparticle comprises a non-cationic helper lipid or phospholipid at a content of 5-25 mole ratio%. For example, the lipid nanoparticle may comprise a non-cationic helper lipid or phospholipid at a content of molar ratio of 5-25 mole ratio%, 5-20 mole ratio%, 5-15 mole ratio%, 10-25 mole ratio%, 10-20 mole ratio%, 10-15 mole ratio%, 5-6 mole ratio%, 6-7 mole ratio%, 7-8 mole ratio%, 8-9 mole ratio%, 9-10 mole ratio%, 10-11 mole ratio%, 11-12 mole ratio%, 12-13 mole ratio%, 13-14 mole ratio%, 14-15 mole ratio%, 10-14 mole ratio%, 10-13 mole ratio%, 10-12 mole ratio%, 10-11 mole ratio%, 9-15 mole ratio%, 9-14 mole ratio%, 9-13 mole ratio%, 9-12 mole ratio%, or 9-11 mole ratio% non-cationic lipid. In one instance, the lipid nanoparticle comprises a phospholipid (e.g., DSPC) at a content of about 10.9 mole ratio%. In another instance, the lipid nanoparticle comprises a phospholipid (e.g., DSPC) at a content of 10.9 mole ratio%. In some instances, the lipid nanoparticle comprises a sterol or other structural lipid at a content molar ratio of 25-55 mole ratio%, 25-50 mole ratio%, 25-45 mole ratio%, 25-40 mole ratio%, 25-35 mole ratio%, 30-55 mole ratio%, 30-50 mole ratio%, 30-45 mole ratio%, 30-40 mole ratio%, 30-35 mole ratio%, 35-55 mole ratio%, 35-50 mole ratio%, 35-45 mole ratio%, 35-40 mole ratio%, 25-30 mole ratio%, 30-35 mole ratio%, 25-28 mole ratio%, 28-30 mole ratio%, 30-33 mole ratio%, 35-38 mole ratio%, 38-40 mole ratio%, 36-40 mole ratio%, 37-40 mole ratio%, 38-40 mole ratio%, 38-39 mole ratio%, 36-40 mole ratio%, 37-40 mole ratio%, 36-39 mole ratio%, or 37-39 mole ratio%. For example, the lipid nanoparticle may comprise a sterol or other structural lipid at a content of about 30 mole ratio%, about 30.5 mole ratio%, about 31.0 mole ratio%, about 31.5 mole ratio%, about 32.0 mole ratio%, about 32.5 mole ratio%, about 33.0 mole ratio%, about 33.5 mole Attorney Docket No.: 45817-0173WO1 ratio%, about 34.0 mole ratio%, about 34.5 mole ratio%, about 35.0 mole ratio%, about 35.5 mole ratio%, about 36.0 mole ratio%, about 36.5 mole ratio%, about 37.0 mole ratio%, about 37.5 mole ratio%, about 38.0 mole ratio%, about 38.5 mole ratio%, about 39.0 mole ratio%, about 39.5 mole ratio%, about 40.0 mole ratio%, about 40.5 mole ratio%, about 41.0 mole ratio%, about 41.5 mole ratio%, about 42.0 mole ratio%, about 42.5 mole ratio%, about 43.0 mole ratio%, about 43.5 mole ratio%, about 44.0 mole ratio%, about 44.5 mole ratio%, or about 45.0 mole ratio%. In one instance, the lipid nanoparticle comprises a structural lipid (e.g., cholesterol) at a content of about 38.3 mole ratio%. In another instance, the lipid nanoparticle comprises a structural lipid (e.g., cholesterol) at a content of 38.3 mole ratio%. In some instances, the lipid nanoparticle comprises a PEG-modified lipid at a content of 0.5-15 mole ratio%, 1.0-15 mole ratio%, 1.5-15 mole ratio%, 2.0-15 mole ratio%, 2.5-15 mole ratio%, 3.0-15 mole ratio%, 3.5-15 mole ratio%, 4.0-15 mole ratio%, 4.5-15 mole ratio%, 5.0-15 mole ratio%, 10-15 mole ratio%, 0.5-10 mole ratio%, 0.5-5 mole ratio%, 0.5-4.5 mole ratio%, 0.5-4.0 mole ratio%, 0.5-3.5 mole ratio%, 0.5-3.0 mole ratio%, 0.5-2.5 mole ratio%, 0.5-2.0 mole ratio%, 0.5-1.5 mole ratio%, 0.5-1.0 mole ratio%, 1.0-10 mole ratio%, 1.0-5 mole ratio%, 1.0-4.5 mole ratio%, 1.0-4.0 mole ratio%, 1.0-3.5 mole ratio%, 1.0-3.0 mole ratio%, 1.0-2.5 mole ratio%, 1.0-2.0 mole ratio%, 1.0-1.5 mole ratio%, 1.5-5.0 mole ratio%, 1.5-4.5 mole ratio%, 1.5-4.0 mole ratio%, 1.5-3.5 mole ratio%, 1.5-3.0 mole ratio%, 1.5-2.5 mole ratio%, 1.5-2.0 mole ratio%, 2.0-5.0 mole ratio%, 2.0-4.5 mole ratio%, 2.0-4.0 mole ratio%, 2.0-3.5 mole ratio%, 2.0-3.0 mole ratio%, or 2.0-2.5 mole ratio%. For example, the lipid nanoparticle may comprise a PEG-modified lipid at a content of a about 0.5 mole ratio%, about 1.0 mole ratio%, about 1.5 mole ratio%, about 2.0 mole ratio%, about 2.5 mole ratio%, about 3.0 mole ratio%, about 3.5 mole ratio%, about 4.0 mole ratio%, about 4.5 mole ratio%, about 5.0 mole ratio%, about 6.0 mole ratio%, about 7.0 mole ratio%, about 8.0 mole ratio%, about 9.0 mole ratio%, about 10.0 mole ratio%, or about 15.0 mole ratio%. In one instance, the lipid nanoparticle comprises a PEG-lipid (e.g., Compound I) at a content of about 3 mole ratio%. In another instance, the lipid nanoparticle comprises a PEG-lipid (e.g., Compound I) at a content of 3 mole ratio%. Attorney Docket No.: 45817-0173WO1 In some instances, the lipid nanoparticle comprises: (i) 20 to 60 mole ratio% ionizable cationic lipid (e.g., ionizable amino lipid such as Compound 2), (ii) 25 to 55 mole ratio% sterol or other structural lipid (e.g., cholesterol), (iii) 5 to 25 mole ratio% non-cationic lipid (e.g., phospholipid such as DSPC), and (iv) 0.5 to 15 mole ratio% PEG-modified lipid (e.g., Compound I). In some instances, the lipid nanoparticle comprises: (i) 40 to 50 mole ratio% ionizable cationic lipid (e.g., ionizable amino lipid such as Compound 2), (ii) 30 to 45 mole ratio% sterol or other structural lipid (e.g., cholesterol), (iii) 5 to 15 mole ratio% non-cationic lipid (e.g., phospholipid such as DSPC), and (iv) 1 to 5 mole ratio% PEG-modified lipid (e.g., Compound I). In some instances, the lipid nanoparticle comprises: (i) 45 to 50 mole ratio% ionizable cationic lipid (e.g., ionizable amino lipid such as Compound 2), (ii) 35 to 45 mole ratio% sterol or other structural lipid (e.g., cholesterol), (iii) 8 to 12 mole ratio% non-cationic lipid (e.g., phospholipid such as DSPC), and (iv) 1.5 to 3.5 mole ratio% PEG-modified lipid (e.g., Compound I). In some instances, the lipid nanoparticle comprises: (i) about 47.5 mole ratio% ionizable cationic lipid (e.g., ionizable amino lipid such as Compound 2), (ii) about 39 mole ratio% sterol or other structural lipid (e.g., cholesterol), (iii) about 10.5 mole ratio% non-cationic lipid (e.g., phospholipid such as DSPC), and (iv) about 3 mole ratio% PEG-modified lipid (e.g., Compound I). In one instance, the lipid nanoparticle comprises: (i) 47.5 mole ratio% ionizable cationic lipid (e.g., ionizable amino lipid such as Compound 2), (ii) 39 mole ratio% sterol or other structural lipid (e.g., cholesterol), (iii) 10.5 mole ratio% non- cationic lipid (e.g., phospholipid such as DSPC), and (iv) 3 mole ratio% PEG- modified lipid (e.g., Compound I). Attorney Docket No.: 45817-0173WO1 Ionizable Amino Lipids In some instances, the lipid nanoparticle of the present disclosure comprises an ionizable cationic lipid (e.g., an ionizable amino lipid) that is a compound of Formula (I): or its N-oxide, or a salt or isomer thereof, wherein R’ais R’branched; wherein denotes a point of attachment; wherein Ra, Ra, Ra, and Raare each independently selected from the group consisting of H, C2-12 alkyl, and C2-12 alkenyl; R2and R3are each independently selected from the group consisting of C1-14 alkyl and C2-14 alkenyl; R4is selected from the group consisting of -(CH2)nOH, wherein n is selected from the group consisting of 1, 2, 3, 4, and 5, , denotes a point of attachment; wherein R10is N(R)2; each R is independently selected from the group consisting of C1-6 alkyl, C2-3 alkenyl, and H; and n2 is selected from the group consisting of 1, 2, 3, 4, 5, 6, 7, 8, 9, and 10; each R5is independently selected from the group consisting of C1-3 alkyl, C2-3 alkenyl, and H; each R6is independently selected from the group consisting of C1-3 alkyl, C2-3alkenyl, and H; Attorney Docket No.: 45817-0173WO1 M and M’ are each independently selected fro...

Claims

Attorney Docket No.: 45817-0173WO1 WHAT IS CLAIMED IS:

1. A lipid nanoparticle comprising a first mRNA, a second mRNA, a third mRNA, and a fourth mRNA, wherein: the first mRNA comprises a nucleic acid sequence encoding a first polypeptide with the structure VH-CH1-Linker 1-VHH1a-Linker 2-VHH1b; the second mRNA comprises a nucleic acid sequence encoding a second polypeptide with the structure VH-CH1-Linker 1-VHH2a -Linker 2-VHH2b; the third mRNA comprises a nucleic acid sequence encoding a third polypeptide with the structure VH-CH1-Linker 1-VHH3a -Linker 2-VHH3b; and the fourth mRNA comprises a nucleic acid sequence encoding a common polypeptide with the structure VL-CL-Linker 1-VHH4; wherein the VH-CH1 of the first, second, and third polypeptides are from an Fab that specifically binds to human CD3, and wherein the VL-CL of the fourth polypeptide is from Fab that specifically binds to human CD3; optionally wherein the human CD3 is human CD3E; and wherein the first polypeptide associates with the common polypeptide, the second polypeptide associates with the common polypeptide, and the third polypeptide associates with the common polypeptide; wherein VHH1aand VHH1bare single domain antibodies that specifically bind to a first tumor associated-antigen, optionally wherein VHH1aand VHH1bhave the same amino acid sequence; wherein VHH2aand VHH2bare single domain antibodies that specifically bind to a second tumor associated-antigen, optionally wherein VHH2a and VHH2b have the same amino acid sequence; wherein VHH3a and VHH3b are single domain antibodies that specifically bind to a third tumor associated-antigen, optionally wherein VHH3a and VHH3b have the same amino acid sequence; wherein VHH4 is a single domain antibody that specifically binds to human serum albumin; wherein Linker 1 is a peptide linker, optionally a glycine serine linker, and further optionally comprising the amino acid sequence set forth in SEQ ID NO:4; andAttorney Docket No.: 45817-0173WO1 wherein Linker 2 is a peptide linker, optionally a glycine serine linker, and further optionally comprising the amino acid sequence set forth in SEQ ID NO:5; also optionally the CH1 of the first, second, and third polypeptides are identical.

2. The lipid nanoparticle of claim 1, wherein the tumor associated-antigen s are multiple myeloma associated antigens, optionally wherein the first tumor associated- antigen is FCRH5, the second tumor associated-antigen is GPRC5D, and the third tumor associated-antigen is BCMA; or wherein the first tumor associated-antigen is CD19, the second tumor associated-antigen is CD20, and the third tumor associated- antigen is CD22.

3. The lipid nanoparticle of claim 1 or claim 2, wherein the first mRNA, the second mRNA, the third mRNA, and the fourth mRNA are modified mRNAs, optionally wherein all the uracils in the mRNAs are N1-methylpseudouracils.

4. The lipid nanoparticle of any one of claims 1 to 3, wherein the first, second, third and fourth mRNAs, further comprise a 5’UTR and a 3’UTR, optionally wherein the 3’UTR comprises one or more miR binding sites and / or an IDR.

5. The lipid nanoparticle of claim 4, wherein the first, second, third and fourth mRNAs further comprise a poly A tail, optionally wherein the poly A tail is about 100 nucleotides in length.

6. The lipid nanoparticle of claim 4 or claim 5, wherein the first, second, third and fourth mRNAs further comprise a 5’ terminal cap.

7. The lipid nanoparticle of any one of claims 1 to 3, wherein the first, second, third and fourth mRNAs, further comprise: (i) a 5’ terminal cap, optionally comprising m7GpppGm; (ii) a 5’UTR, optionally comprising the sequence of SEQ ID NO:64;Attorney Docket No.: 45817-0173WO1 (iii) a signal sequence if not present in the first, second, third and fourth mRNAs; (iv) a 3’UTR, optionally wherein the 3’UTR comprises one or more miR binding sites and / or an IDR, and further optionally comprising the sequence of any one of SEQ ID NOs:127 to 130; and (v) a poly A tail, optionally wherein the poly A tail is about 100 nucleotides in length, optionally SEQ ID NO:

132.

8. The lipid nanoparticle of any one of claims 1 to 7, wherein: (i) the first mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:55, wherein the first mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to the N-terminus of the first VHH, the C- terminus of which in turn is linked to the N-terminus of the second VHH, wherein the first and second VHH bind to human FCRH5; (ii) the second mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:56, wherein the second mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the third VHH, the C-terminus of which in turn is linked to the N-terminus of the fourth VHH, wherein the third and fourth VHH bind to human GPRC5D; (iii) the third mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:57, wherein the third mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the fifthAttorney Docket No.: 45817-0173WO1 VHH the C-terminus of which in turn is linked to the N-terminus of the sixth VHH, wherein the fifth and sixth VHH bind to human BCMA; and (iv) the fourth mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:58, wherein the fourth mRNA encodes a VL-CL chain of a Fab that binds to human CD3, wherein the C-terminus of the CL is linked to the N-terminus of the VHH that binds to human HSA, optionally wherein all the uracils in the four mRNAs are N1- methylpseudouracils, or the uridines of the mRNA are N1-methylpseudouridines, further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is about 2: about 4:about 1: about 4.7, respectively, and yet further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is 2: 4:1: 4.7, respectively.

9. The lipid nanoparticle of any one of claims 1 to 8, wherein: (i) the first mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:60, wherein the first mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to the N-terminus of the first VHH, the C-terminus of which in turn is linked to the N-terminus of the second VHH, wherein the first and second VHH bind to human FCRH5; (ii) the second mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:61, wherein the second mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the third VHH, the C-terminus ofAttorney Docket No.: 45817-0173WO1 which in turn is linked to the N-terminus of the fourth VHH, wherein the third and fourth VHH bind to human GPRC5D; (iii) the third mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:62, wherein the third mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the fifth VHH the C-terminus of which in turn is linked to the N-terminus of the sixth VHH, wherein the fifth and sixth VHH bind to human BCMA; and (iv) the fourth mRNA comprises a sequence that that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:63, wherein the fourth mRNA encodes a VL-CL chain of a Fab that binds to human CD3, wherein the C-terminus of the CL is linked to the N-terminus of the VHH that binds to human HSA, optionally wherein all the uracils in the four mRNAs are N1- methylpseudouracils, or the uridines of the mRNA are N1-methylpseudouridines, further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is about 2: about 4:about 1: about 4.7, respectively, and yet further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is 2: 4:1: 4.7, respectively.

10. The lipid nanoparticle of any one of claims 1 to 9, wherein the lipid nanoparticle comprises an ionizable amino lipid, a structural lipid, a phospholipid, and a polyethylene glycol (PEG)-modified lipid, optionally wherein the ionizable amino lipid is present at about 40 to 50 mole ratio%, the structural lipid is present at 35 to 45 mole ratio%, the phospholipid is present at 5 to 15 mole ratio%, and the PEG- modified lipid is present at 1.5 to 5 mole ratio%, and further optionally wherein the ionizable amino lipid is present at about 47.5 mole ratio%, the structural lipid isAttorney Docket No.: 45817-0173WO1 present at about 39 mole ratio%, the phospholipid is present at about 10.5 mole ratio%, and the PEG-modified lipid is present at about 3 mole ratio%.

11. The lipid nanoparticle of claim 10, wherein the ionizable amino lipid is Compound 2.

12. The lipid nanoparticle of claim 10 or 11, wherein the structural lipid is cholesterol.

13. The lipid nanoparticle of any one of claims 10 to 12, wherein the phospholipid is DSPC.

14. The lipid nanoparticle of any one of claims 10 to 13, wherein the PEG-modified lipid is Compound I.

15. The lipid nanoparticle of any one of claims 10 to 14, wherein the ionizable amino lipid is Compound 2, the structural lipid is cholesterol, the phospholipid is DSPC, and the PEG-modified lipid is Compound I.

16. The lipid nanoparticle of any one of claims 10 to 15, wherein the ionizable amino lipid is Compound 2 and is present at about 47.5 mole ratio%, the structural lipid is cholesterol and is present at about 39 mole ratio%, the phospholipid is DSPC and is present at about 10.5 mole ratio%, and the PEG-modified lipid is Compound I and is present at about 3 mole ratio%.

17. A pharmaceutical composition comprising the lipid nanoparticle of any one of claims 1 to 16, and a pharmaceutically acceptable carrier.

18. A method of treating a cancer in a human subject in need thereof, the method comprising administering to the human subject a therapeutically effective amount of the lipid nanoparticle of any one of claims 1 to 16 or the pharmaceutical composition of claim 17, optionally wherein the cancer is a FCRH5+, a GPRC5D+, a BCMA+, aAttorney Docket No.: 45817-0173WO1 FCRH5+ and GPRC5D+, a FCRH5+ and BCMA+, a GPRC5D+ and BCMA+, or a FCRH5+, GPRC5D+, and BCMA+ cancer; optionally wherein the cancer is a hematological cancer optionally multiple myeloma, and further optionally wherein the multiple myeloma is relapsed multiple myeloma, refractory multiple myeloma, or relapsed refractory multiple myeloma, and even further optionally wherein the treatment is a second, third, or later line treatment, and further optionally wherein the therapeutically effective amount is 0.002 mg / kg administered intravenously once weekly or twice weekly, also further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is about 2: about 4:about 1: about 4.7, respectively, and yet further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is 2: 4:1: 4.7, respectively.

19. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a lipid nanoparticle comprising a first mRNA, a second mRNA, a third mRNA, and a fourth mRNA, wherein: the first mRNA comprises a nucleic acid sequence encoding a first polypeptide with the structure VH-CH1-Linker 1-VHH1a -Linker 2-VHH1b; the second mRNA comprises a nucleic acid sequence encoding a second polypeptide with the structure VH-CH1-Linker 1-VHH2a -Linker 2-VHH2b; the third mRNA comprises a nucleic acid sequence encoding a third polypeptide with the structure VH-CH1-Linker 1-VHH3a -Linker 2-VHH3b; and the fourth mRNA comprises a nucleic acid sequence encoding a common polypeptide with the structure VL-CL-Linker 1-VHH4; wherein the VH-CH1 of the first, second, and third polypeptides are from an Fab that specifically binds to human CD3, and wherein the VL-CL of the fourth polypeptide is from Fab that specifically binds to human CD3; optionally wherein the human CD3 is human CD3E; and wherein the first polypeptide associates with the common polypeptide, the second polypeptide associates with the common polypeptide, and the third polypeptide associates with the common polypeptide; wherein VHH1aand VHH1bare single domain antibodies that specifically binds to a first tumor associated-antigen, optionally wherein VHH1aand VHH1bhave the same amino acid sequence;Attorney Docket No.: 45817-0173WO1 wherein VHH2aand VHH2bare single domain antibodies that specifically binds to a second tumor associated-antigen, optionally wherein VHH2aand VHH2bhave the same amino acid sequence; wherein VHH3aand VHH3bare single domain antibodies that specifically binds to a third tumor associated-antigen, optionally wherein VHH3aand VHH3bhave the same amino acid sequence; wherein VHH4 is a single domain antibody that specifically binds to human serum albumin; wherein Linker 1 is a peptide linker, optionally a glycine serine linker, and further optionally comprising the amino acid sequence set forth in SEQ ID NO:4; and wherein Linker 2 is a peptide linker, optionally a glycine serine linker, and further optionally comprising the amino acid sequence set forth in SEQ ID NO:5; also optionally the CH1 of the first, second, and third polypeptides are identical.

20. The pharmaceutical composition of claim 19, wherein the tumor associated- antigen s are multiple myeloma associated antigens., optionally wherein the first tumor associated-antigen is FCRH5, the second tumor associated-antigen is GPRC5D, and the third tumor associated-antigen is BCMA; or wherein the first tumor associated-antigen is CD19, the second tumor associated-antigen is CD20, and the third tumor associated-antigen is CD22.

21. The pharmaceutical composition of claim 19 or claim 20, wherein the first mRNA, the second mRNA, the third mRNA, and the fourth mRNA are modified mRNAs, optionally wherein all the uracils in the mRNAs are N1- methylpseudouracils.

22. The pharmaceutical composition of any one of claims 19 to 21, wherein the first, second, third and fourth mRNAs, further comprise a 5’UTR and a 3’UTR, optionally wherein the 3’UTR comprises one or more miR binding sites and / or an IDR.Attorney Docket No.: 45817-0173WO1 23. The pharmaceutical composition of claim 22, wherein the first, second, third and fourth mRNAs further comprise a poly A tail, optionally wherein the poly A tail is about 100 nucleotides in length.

24. The pharmaceutical composition of claim 22 or claim 23, wherein the first, second, third and fourth mRNAs further comprise a 5’ terminal cap.

25. The pharmaceutical composition of any one of claims 19 to 21, wherein the first, second, third and fourth mRNAs, further comprise: (i) a 5’ terminal cap, optionally comprising m7GpppGm; (ii) a 5’UTR, optionally comprising the sequence of SEQ ID NO:64; (iii) a signal sequence if not present in the mRNAs; (iv) a 3’UTR, optionally wherein the 3’UTR comprises one or more miR binding sites and / or an IDR, and further optionally comprising the sequence of any one of SEQ ID NOs:127 to 130; and (v) a poly A tail, optionally wherein the poly A tail is about 100 nucleotides in length, optionally SEQ ID NO:

132.

26. The pharmaceutical composition of any one of claims 19 to 25, wherein: (i) the first mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:55, wherein the first mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to the N-terminus of the first VHH, the C- terminus of which in turn is linked to the N-terminus of the second VHH, wherein the first and second VHH bind to human FCRH5; (ii) the second mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:56,Attorney Docket No.: 45817-0173WO1 wherein the second mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the third VHH, the C-terminus of which in turn is linked to the N-terminus of the fourth VHH, wherein the third and fourth VHH bind to human GPRC5D; (iii) the third mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:57, wherein the third mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the fifth VHH the C-terminus of which in turn is linked to the N-terminus of the sixth VHH, wherein the fifth and sixth VHH bind to human BCMA; and (iv) the fourth mRNA comprises a sequence that encodes an amino acid sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the sequence set forth in SEQ ID NO:58, wherein the fourth mRNA encodes a VL-CL chain of a Fab that binds to human CD3, wherein the C-terminus of the CL is linked to the N-terminus of the VHH that binds to human HSA, optionally wherein all the uracils in the four mRNAs are N1- methylpseudouracils, or the uridines of the mRNA are N1-methylpseudouridines, further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is about 2: about 4:about 1: about 4.7, respectively, and yet further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is 2: 4:1: 4.7, respectively.

27. The pharmaceutical composition of any one of claims 19 to 26, wherein: (i) the first mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:60, wherein the first mRNA encodes aAttorney Docket No.: 45817-0173WO1 VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to the N-terminus of the first VHH, the C-terminus of which in turn is linked to the N-terminus of the second VHH, wherein the first and second VHH bind to human FCRH5; (ii) the second mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:61, wherein the second mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the third VHH, the C-terminus of which in turn is linked to the N-terminus of the fourth VHH, wherein the third and fourth VHH bind to human GPRC5D; (iii) the third mRNA comprises a sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:62, wherein the third mRNA encodes a VH-CH1 chain of a Fab that binds to human CD3, wherein the C-terminus of the CH1 is linked to linked to the N-terminus of the fifth VHH the C-terminus of which in turn is linked to the N-terminus of the sixth VHH, wherein the fifth and sixth VHH bind to human BCMA; and (iv) the fourth mRNA comprises a sequence that that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the nucleic acid sequence set forth in SEQ ID NO:63, wherein the fourth mRNA encodes a VL-CL chain of a Fab that binds to human CD3, wherein the C-terminus of the CL is linked to the N-terminus of the VHH that binds to human HSA, optionally wherein all the uracils in the four mRNAs are N1- methylpseudouracils, or the uridines of the mRNA are N1-methylpseudouridines, further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is about 2: about 4:about 1: about 4.7, respectively, and yet further optionallyAttorney Docket No.: 45817-0173WO1 wherein the mass ratio of the first, second, third, and fourth mRNAs is 2: 4:1: 4.7, respectively.

28. The pharmaceutical composition of any one of claims 19 to 27, wherein the lipid nanoparticle comprises an ionizable amino lipid, a structural lipid, a phospholipid, and a polyethylene glycol (PEG)-modified lipid, optionally wherein the ionizable amino lipid is present at about 40 to 50 mole ratio%, the structural lipid is present at 35 to 45 mole ratio%, the phospholipid is present at 5 to 15 mole ratio%, and the PEG- modified lipid is present at 1.5 to 5 mole ratio%, and further optionally wherein the ionizable amino lipid is present at about 47.5 mole ratio%, the structural lipid is present at about 39 mole ratio%, the phospholipid is present at about 10.5 mole ratio%, and the PEG-modified lipid is present at about 3 mole ratio%.

29. The pharmaceutical composition of claim 28, wherein the ionizable amino lipid is Compound 2.

30. The pharmaceutical composition of claim 28 or 29, wherein the structural lipid is cholesterol.

31. The pharmaceutical composition of any one of claims 28 to 30, wherein the phospholipid is DSPC.

32. The pharmaceutical composition of any one of claims 28 to 31, wherein the PEG- modified lipid is Compound I.

33. The pharmaceutical composition of any one of claims 28 to 32, wherein the ionizable amino lipid is Compound 2, the structural lipid is cholesterol, the phospholipid is DSPC, and the PEG-modified lipid is Compound I.

34. The pharmaceutical composition of any one of claims 28 to 33, wherein the ionizable amino lipid is Compound 2 and is present at about 47.5 mole ratio%, theAttorney Docket No.: 45817-0173WO1 structural lipid is cholesterol and is present at about 39 mole ratio%, the phospholipid is DSPC and is present at about 10.5 mole ratio%, and the PEG-modified lipid is Compound I and is present at about 3 mole ratio%.

35. A method of treating a cancer in a human subject in need thereof, the method comprising administering to the human subject a therapeutically effective amount of the pharmaceutical composition of any one of claims 19 to 34, optionally wherein the cancer is FCRH5+, GPRC5D+, BCMA+, FCRH5+ and GPRC5D+, FCRH5+ and BCMA+, GPRC5D+ and BCMA+, or FCRH5+, GPRC5D+, and BCMA+; optionally wherein the cancer is a hematological cancer optionally multiple myeloma, and further optionally wherein the multiple myeloma is relapsed multiple myeloma, refractory multiple myeloma, or relapsed refractory multiple myeloma, and even further optionally wherein the treatment is a second, third, or later line treatment, and further optionally wherein the therapeutically effective amount is 0.002 mg / kg administered intravenously once weekly or twice weekly, also further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is about 2: about 4:about 1: about 4.7, respectively, and yet further optionally wherein the mass ratio of the first, second, third, and fourth mRNAs is 2: 4:1: 4.7, respectively. .

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