GPRC5D CHIMERIC ANTIGEN RECEPTORS AND CELLS THAT EXPRESS THEM

Abstract

The present description provides chimeric antigen receptors (CARs) that specifically target a G protein-coupled receptor, group 5 family C member D (GPRC5D) of the G protein-coupled receptor, and immune-sensitive cells comprising such CARs, for the treatment of cancer.

Description

RECEPTORS FOR CHIMERIC GPRC5D ANTIGENS AND CELLS THAT EXPRESS THEM LIST OF SEQUENCES This application contains a sequence listing that is presented electronically in ASCII format and is incorporated herein by reference in its entirety. Such an ASCII copy, created on January 9, 2020, is named JBI6043WOPCTl_SL.txt and its size is 150,002 bytes. FIELD OF THE INVENTION The invention relates to GPRC5D-targeting chimeric antigen receptors (CARs) comprising GPRC5D single-chain variable fragments and engineered GPRC5D-targeting immune cells expressing the CARs. Also provided are nucleic acids and expression vectors encoding CARs, recombinant cells containing the vectors, and compositions comprising engineered immune cells expressing CARs that target GPRC5D. Also provided are methods of making CARs, and engineered immune cells, and methods of using the engineered immune cells to treat conditions including cancer. BACKGROUND OF THE INVENTION T-cell therapy uses isolated T cells that have been genetically modified to improve their specificity for a specific tumor-associated antigen. Genetic modification may involve the expression of a chimeric antigen receptor (CAR) or an exogenous T cell receptor to provide a novel antigen specificity on the T cell. T cells expressing chimeric antigen receptors (CAR-T cells) can induce tumor immunoreactivity. There is a need for better cancer therapies that use CAR-T cells. BRIEF DESCRIPTION OF THE INVENTION In the present description chimeric antigen receptors (CAR) are described, e.g. e.g., CARs targeting a coupled receptor family C group 5 (GPRC5D) member D MA / t / ZUZI / U / 4400 to G protein, cells comprising CARs, vectors encoding CARs, e.g. eg, recombinant expression vectors, and nucleic acid molecules encoding CARs, methods of making CARs, compositions, polypeptides, proteins, nucleic acids, host cells, cell populations, and methods of treating disorders, e.g. eg, cancer, using the described CARs. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 66, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 67, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 68; a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 58, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 60; a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 39, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40 and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 41; a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 43 and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 44; or a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 45, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and a heavy chain CDR3 having the amino acid sequence from SEQ ID NO: 47; wherein the extracellular antigen binding domain binds the antigen of GPRC5D. In a mode: the extracellular antigen-binding domain comprises heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 66, heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 67, and CDR3 of heavy chain having the amino acid sequence of SEQ ID NO: 68, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 69, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 70, and a light chain CDR3 having the amino acid sequence MA / t / ZUZI / U / 4400 of SEQ ID NO: 71; the extracellular antigen-binding domain comprises heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 58, heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and CDR3 of heavy chain having the amino acid sequence of SEQ ID NO: 60, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 61, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 62 and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 63 the extracellular antigen binding domain comprises the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 39, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40, and the heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 41, and further comprising a light chain CDR1 having has the amino acid sequence of SEQ ID NO: 48, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 49, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 50 ; the extracellular antigen-binding domain comprises heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 43, and CDR3 of heavy chain having the amino acid sequence of SEQ ID NO: 44, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 51, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 52 and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 53; or the extracellular antigen-binding domain comprises heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 45, heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and CDR3 heavy chain having the amino acid sequence of SEQ ID NO: 47, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 54, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 55 and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 56. In one embodiment, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 73, 65, 1, 3 and 5, or a heavy chain variable region (HCVR) comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 72, 64, 2, 4 and 6, or a combination of an LCVR comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 73, 65, 1, 3 and 5, and an HCVR comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 72, 64, 2, 4 and 6. In one embodiment, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 73 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 72; a light chain variable region comprising an amino acid sequence of SEQ ID NO: 65 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 64; a light chain variable region comprising an amino acid sequence of SEQ ID NO: 1 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 2; a light chain variable region comprising an amino acid sequence of SEQ ID NO: 3 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 4; or a light chain variable region comprising an amino acid sequence of SEQ ID NO: 5 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 6. In one embodiment, the extracellular antigen binding domain comprises a single chain variable fragment (scFv). In some embodiments, the scFv comprises a polypeptide linker between the light chain variable region and the heavy chain variable region. In one embodiment, the linker polypeptide comprises an amino acid sequence of SEQ ID NO: 7. In one embodiment, the scFv comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 78, 77, 75, 76, 8, 9, 10, 24, 25 and 26. In one embodiment, the extracellular antigen-binding domain comprises a signal polypeptide. In some embodiments, the signal polypeptide comprises an amino acid sequence of SEQ ID NO: 11. In one embodiment, the intracellular signaling domain comprises a polypeptide component selected from the group consisting of a component of TNF receptor superfamily member 9 (CD137), a component of the surface glycoprotein CD3 zeta chain (CD3z) T-cell, a component of the differentiation cluster (CD27), a component of the differentiation cluster superfamily (such as, e.g., CD28 or inducible T-cell costimulator (ICOS)) and a combination of IVIA / I / U / 4400 these. In some embodiments, the CD137 component comprises an amino acid sequence of SEQ ID NO: 12. In some embodiments, the CD3z component comprises an amino acid sequence of SEQ ID NO: 13. In one embodiment, the intracellular signaling domain comprises the amino acid sequence of SEQ ID NO: 14. In one embodiment, the transmembrane domain comprises a CD8a transmembrane region (CD8a-TM) polypeptide. In some embodiments, the CD8a-TM polypeptide comprises an amino acid sequence of SEQ ID NO: 15. In one embodiment, the CAR further comprises a hinge region linking the transmembrane domain to the extracellular antigen-binding domain. In some embodiments, the hinge region is a CD8a hinge region. In some embodiments, the CD8a hinge region comprises an amino acid sequence of SEQ ID NO: 16. In one embodiment, the extracellular antigen-binding domain comprises an amino acid sequence selected from the group consisting of SEQ ID NOs: 82, 81, 80, 79, 17, 18, 19, 20, 21, and 22. In one embodiment, a CAR of the present disclosure comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 86, 85, 83, 84, 27, 28, 29, 30, 31, and 32. In one aspect, the disclosure provides isolated lymphocytes that express the CARs as described herein. In some embodiments, the lymphocyte is a T lymphocyte. In some embodiments, the T lymphocyte is a naive T cell. In some embodiments, the T lymphocyte is a memory stem T cell. In some embodiments, the T lymphocyte is a central memory T cell. In some embodiments, the T cell is CD4+. In some embodiments, the T cell is CD8+. In some embodiments, the T cell is CD4+ and CD8+. In one aspect, the disclosure provides isolated nucleic acid molecules that encode any of the CARs described herein. In some embodiments, the nucleic acid molecule comprises a nucleic acid sequence selected from the group consisting of SEQ ID NO: 90, 89, 87, 88, 33, 34, 35, 36, 37, and 38. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to a nucleotide sequence of SEQ ID NO: 90, 89, 87, 88, 33, 34, 35 , 36, 37, or 38. In one embodiment, the present disclosure provides a vector comprising the nucleic acid molecule. In one embodiment, the present ΜΛ / t / ZUZ I / U / 4400 disclosure provides a cell expressing the nucleic acid molecule. In one aspect, the present disclosure provides compositions, e.g. eg, pharmaceutical compositions, comprising an effective amount of the lymphocyte expressing one or more of the described CARs and a pharmaceutically acceptable excipient. In one aspect, the present disclosure provides a CAR in accordance with the present disclosure for use in a method of therapy. In one aspect, the present disclosure provides a lymphocyte in accordance with the present disclosure for use in a method of therapy. In one aspect, the present disclosure provides a composition, e.g. eg, a pharmaceutical composition, according to the present disclosure for use in a method of therapy. In one aspect, the present disclosure provides a CAR in accordance with the present disclosure for use in a method of treating cancer. In one aspect, the present disclosure provides a lymphocyte in accordance with the present disclosure for use in a method of treating cancer. In one aspect, the present disclosure provides a composition, e.g. eg, a pharmaceutical composition, according to the present disclosure for use in a method of treating cancer. In one embodiment, the cancer is selected from the group consisting of bladder cancer, metastatic bladder cancer, esophageal cancer, non-small cell lung adenocarcinoma, non-small cell lung squamous cell carcinoma, prostate cancer, urothelial carcinoma, small cell lung cancer, endometrial cancer, cholangiocarcinoma, hepatocellular carcinoma, sarcomas, solid tumors of squamous origin, lung cancer, gastric cancer, colon cancer , hepatocellular carcinoma, renal cell carcinoma, bladder urothelial carcinoma, metastatic melanoma, breast cancer, ovarian cancer, cervical cancer, head and neck cancer, pancreatic cancer, glioma, glioblastoma, non-Hodgkin lymphoma (NHL), acute lymphocytic leukemia (ALL), chronic lymphocytic leukemia (CLL), chronic myelogenous leukemia ( CML), smoldering multiple myeloma (SMM), multiple myeloma (MM), acute myeloid leukemia (AML), and combinations of these. In one embodiment, the cancer being treated is multiple myeloma. In one aspect, the present disclosure provides methods of treating a subject having cancer, the methods comprising administering a therapeutically effective amount of a lymphocyte expressing one or more of the described CARs to a subject in need thereof, whereby the lymphocyte induces the destruction of cancer cells in the subject. In one embodiment, the cancer is selected from the group consisting of bladder cancer, bladder cancer, MA / t / ZUZI / U / 4400 metastatic bladder, esophageal cancer, non-small cell lung adenocarcinoma, non-small cell lung squamous cell carcinoma, prostate cancer, urothelial carcinoma, lung cancer small cell lung cancer, endometrial cancer, cholangiocarcinoma, hepatocellular carcinoma, sarcomas, solid tumors of squamous origin, lung cancer, gastric cancer, colon cancer, hepatocellular carcinoma, renal cell carcinoma, bladder urothelial carcinoma, metastatic melanoma, breast cancer, ovarian cancer, cervical cancer, head and neck cancer, pancreatic cancer, glioma, glioblastoma, non-Hodgkin lymphoma (NHL), acute lymphocytic leukemia (ALL), chronic lymphocytic leukemia (CLL), chronic myelogenous leukemia (CML), smoldering multiple myeloma (SMM), multiple myeloma (MM), acute myeloid leukemia (AML), and combinations thereof. In one embodiment, the cancer being treated in a subject is multiple myeloma. In one aspect, a method for targeted killing of a cancer cell is disclosed, the method comprising contacting the cancer cell with a lymphocyte expressing one or more of the described CARs, whereby the lymphocyte induces killing of the cell. cancerous. In some embodiments, the cancer cell is selected from the group consisting of a lung cancer cell, a gastric cancer cell, a colon cancer cell, a hepatocellular carcinoma cell, a renal cell carcinoma cell, a urothelial carcinoma cell cell, metastatic melanoma cell, breast cancer cell, ovarian cancer cell, cervical cancer cell, head and neck cancer cell, pancreatic cancer cell, glioma cell, glioblastoma, and one non-Hodgkin lymphoma (NHL) cell, one acute lymphocytic leukemia (ALL) cell, one chronic lymphocytic leukemia (CLL) cell, one chronic myelogenous leukemia (CML) cell, one smoldering multiple myeloma cell (SMM), a multiple myeloma (MM) cell, an acute myeloid leukemia (AML) cell, and combinations thereof. In one embodiment, the cancer cell is a multiple myeloma cell. BRIEF DESCRIPTION OF THE FIGURES The foregoing will become apparent from the following more particular description of illustrative embodiments, as illustrated in the attached figures. Figure 1 shows flow cytometric analyzes of electroporated primary human pan T cells with no mRNA (mock) or 10 pg mRNA expressing either a Q-GPRC5D scFv CAR or an isotype control CAR. 24 hours after electroporation, CAR surface expression was measured by flow cytometry after staining with biotinylated protein L and conjugated PE. ΜΛ / t / ZUZ I / U / 4400 of streptavidin. The open histogram is simulated, the gray filled histogram is the CAR-T population. Figure 2 shows flow cytometric analyzes of transiently transfected pan T cells cocultured with a multiple myeloma cell line. Twenty-four hours after transient transfection, primary pan T cells were labeled with Cell Trace Violet (CTV) fluorescent proliferation dye and then cocultured with a multiple myeloma cell line, H929. Four days after cocultivation, cells were pregated in the CD8+CD4- population and the surface expression of the activation markers CD25 and CD71 on CAR-T were compared to T cells cultured alone or in the presence of aCD3 / microspheres. CD28. Figure 3 shows an analysis of the cytokine profile for primary pan T cells transiently transfected with CAR-expressing mRNA and cocultured with various myeloma cell lines. Primary pan T cells transiently transfected 24 hours earlier with CAR-expressing mRNA were cocultured in a 1:1 ratio with various myeloma cell lines expressing the target antigen, GPRC5D, at high (+++), medium ( ++), low (+) or negative (-). Sixteen hours after coculture, supernatants were collected and cytokine profile analysis was performed using the Meso Scale Discovery (MSD) method of the coculture supernatants. Figure 4 shows an analysis of the cytokine profile for primary pan T cells transiently transfected with CAR-expressing mRNA and cocultured with autologous peripheral blood mononuclear cells (PBMCs) and a multiple myeloma cell line. Twenty-four hours after transient transfection with CAR-expressing mRNA, primary pan T cells were cocultured (in a 1:1:1 ratio) with autologous PBMC and the multiple myeloma cell line, H929. Sixteen hours after cocultivation, the supernatants were collected. MSD cytokine profile analysis of supernatants from cocultures containing all three populations (CAR-T, H929, autologous PBMCs) were compared to control cocultures lacking CAR-T cells, PBMCs, or H929, with each population of cells grown in isolation. Figure 5 shows flow cytometric analyzes of the cytotoxic potential of CAR-T cells in myeloma cells expressing GPRC5D. Primary pan T cells (transiently expressing one of the three CARs as described above) were cocultured in the indicated effector:target (E:T) ratios with fluorescently labeled myeloma cell lines, MM1R, H929, and K562, for eight hours. , at which time the cocultures were stained with viability dye. Percent kill is the ratio of the absolute number of live target (CTV positive) (viability dye negative) cells remaining in the coculture relative to the number of live targets cultured without CAR-T cells. Figure 6 shows flow cytometric analyzes of cytotoxic potential of the ΜΛ / t / ZUZ I / U / 4400 CAR-T cells in myeloma cells expressing GPRC5D. Primary T cells from patients with multiple myeloma (transiently expressing one of two CARs as described above) in the indicated effector:target (E:T) ratios were cocultured with the fluorescently labeled myeloma cell line MM.1S or negative cell line. of GPRC5d KG-1 control for 48 hours, at which time the co-cultures were stained with viability stain. Percent cytotoxicity was determined as the percentage of fluorescently labeled cells that stained positive for the viability dye, indicating cell death. Figure 7 shows the results of flow cytometric analyzes of the proliferative capacity of O-GPRC5D CAR-T cells. Fluorescently labeled pan T cells (transiently expressing an O-GPRC5D CAR or isotype CAR control) were cocultured at an E:T ratio of 1 with H929 for four days. Proliferation was measured as the absolute number of live CAR-T (viability dye negative) cells that had diluted fluorescent tracer (CTV). Proliferation in response to H929 was compared to CAR-T proliferation after four days of stimulation of O-CD3 / CD28 microspheres and cultured CAR-T alone (no stimulation control). Figure 8 shows a bar graph depicting the percent CAR expression of GPRC5D in T cells from healthy donors, as measured by flow cytometry. Gray shaded bars represent background CAR detection in non-transduced (mock) cells. Black bars show GPRC5D GC5B680-N68S-LH in transduced CAR-T cells. The values ​​shown represent the mean ± SD with 6 healthy donors. Figures 9A-9F depict data showing expression of CD4, CD8, and memory markers in GPRC5D CAR-T cells. Figures 9A-9C show bar graphs, with the data collectively showing that the CAR of GPRC5D GC5B680-N68S-LH was detected by flow cytometry in both CD4 and CD8 T cells, and that the CD4 / CD8 ratio was not much different from a non-transduced population. Figure 9A shows the percentage of a simulated (non-transduced) cell population comprised of each CD8+ and CD4+ cells. Figures 9B-9C each, respectively, show the percentage of CAR' cells (transduced cells that do not express GPRC5D CAR) comprised by each of the CD8+ and CD4+ cells and the percentage of CAR+ cells (transduced cells that do not express GPRC5D CAR). expressing CARs of GPRC5D) comprised by each of CD8+ and CD4+ cells. Figure 9D illustrates a flow cytogram prepared from a donor illustrating a labeling strategy for selection of different indicated memory populations in a CAR-T population using surface markers (CD45RA and CD62L). Figures 9E and 9F represent bar graphs showing that GPRC5D GC5B680-N68S-LH was more highly expressed in Tn / scm and Tcm, which has been shown to have higher capacity. IVIA / I / U / 4400 proliferative, survival and therapeutic efficacy. The values ​​shown in Figures 9A-9C and 9E9F represent the mean ± SD with 6 healthy donors. Figures 10A-10B show scatter plots showing the CAR-T toxicity of GPRC5D. GPRC5D GC5B680-N68S-LH or non-transduced (mock) T cells were added at various E:T ratios to GPRC5D+ MM.1S cells or GPRC5D K562 cells containing a luciferase transgene. CAR-Ts were drawn from six healthy donors. Values ​​are expressed as the mean ± SD over 6 hours (Figure 1OA) or 24 hours (Figure 1OB). Percent specific lysis was calculated (i) by measuring the luciferase signal in tumor cells in the presence of CAR-Ts at 6 or 24 hours divided by the luciferase signal in tumor cells alone at the same time points and multiplied by 100 and (ii) by subtracting that number from 100. The equation is: 100[(CAR-T + tumor luminescence / average tumor luminescence alone)xl00]. The dotted line represents a percentage of specific lysis equal to zero. Negative lysis is indicative of cell growth. Figures 11A-11F illustrate scatter plots showing that the cytotoxicity of GPRC5D CAR-T cells spiked at the indicated E:T ratios was assessed using GPRC5D+ H929, MM.1S, MM.1R, MOLP-2 cells. and EJM or K562 cells from GPRC5D. GPRC5D CAR-T cells showed cytotoxicity against all GPRC5D+ cell lines. Figure 12 shows a bar graph depicting CD25 surface expression levels (%CD25) by GC5B680-N68S-LH cells either (mock) or non-transduced in the presence of K562 cells at an E:T ratio of 3. :1. CAR-Ts were drawn from six healthy donors. Data are expressed as the mean ± SD. Figure 13 illustrates flow cytograms showing that GC5B680-N68S-LH specifically proliferates in the presence of GPRC5D+ target cells (H929 or MM.1S) or a positive control (agonist CD3 / CD28 beads) and not in the absence of target cells or in the presence of GPRC5D (K562) cells. Cell proliferation was measured by using CELLTRACE Violet (CTV) (X-axis). CAR+ events were detected using an anti-idiotype antibody (Y-axis). Figure 14 shows a bar graph showing that the 3 / 7 levels of cleaved caspase in CAR-T cells (GC5B680-N68S-LH) incubated with the GPRC5D+ cell line H929 for 24 hours remain unchanged compared to the GPRC5D+ cell line. controls (staurosporine, GPRC5D K562 cells, or alone). A 1:2 E:T ratio was used for H929 and K562 cells. CAR- represents transduced cells that do not express the CAR of GPRC5D. CAR+ represents transduced cells expressing the CAR of GPRC5D. Figure 15 shows a graph showing the effect of CAR-T cells targeting GPRC5D on human MM MM.1S xenografts established in NSG-B2M mice according to the MA / t / ZUZI / U / 4400 Example 15. CAR-T Targeting GC5B680-N68S-LH, GC5B680-N68S-HL, GC5B83-N24T-N31S-LH, and GC5B83-N24T-N31S-HL, GPRC5D, Mock, Non-Transduced CAR-T, PBS, Solution phosphate-regulated saline, NSG, severe combined gamma immunodeficiency in nonobese diabetics, B2M, Beta-2 microglobulin, MM, multiple myeloma. Group tumor volumes are plotted as the mean ± SEM. Tumor cells were implanted on day 0.1 x 106 CAR+ T cells were implanted on day 13. Symbol indicates significant difference at day 26 vs. the PBS control (p<0.05, n=10 / group). Figure 16 shows a graph demonstrating the effect of GC5B680-N68S-LH on the survival of NSG mice bearing human MM H929 xenografts disseminated according to Example 16. CAR-T targeting GC5B680-N68S-LH, GC5B680 -N68S-HL, GC5B83-N24TN31S-LH, and GC5B83-N24T-N31S-HL, GPRC5D, Mock, non-transduced CAR-T, PBS, phosphate-buffered saline, NSG, severe combined gamma immunodeficiency in nonobese diabetics, MM , multiple myeloma. Tumor cells were implanted on day 0; 1 x 106 CAR+ T cells were implanted on day 9. The symbol indicates a significant difference at day 111 vs. the PBS control. DETAILED DESCRIPTION OF THE INVENTION The following is a description of illustrative embodiments. The present disclosure provides chimeric antigen receptors (CARs) that target a G-protein-coupled receptor family group 5 C (GPRC5D) member D, the cells comprising such CARs, and methods of treating cancer (e.g., g ., hematological malignancies and solid tumors) using the CARs described herein. The CARs of the invention have antigen specificity for GPRC5D (eg, a human GPRC5D polypeptide having the amino acid sequence of SEQ ID NO: 57, or fragments thereof). The phrases having antigen specificity and eliciting an antigen-specific response, as used herein, mean that the CAR can specifically bind to and immunologically recognize an antigen such that binding of the CAR to the GPRC5D antigen elicits a response. immune. Methods for evaluating CARs for antigen specificity and for the ability to recognize target cells are known in the art. The disclosure also provides related nucleic acids, recombinant expression vectors, host cells, cell populations, antibodies or antigen-binding portions thereof, and pharmaceutical compositions that are related to the CARs of the invention. Various aspects of the invention are described below, with reference to examples / U / 4400 only for illustrative purposes. It is to be understood that numerous specific details, relationships, and methods are set forth to provide a full understanding of the invention. However, one skilled in the relevant art will readily recognize that the invention can be practiced without one or more of the specific details or practiced with other methods, protocols, reagents, cell lines, and animals. The present invention is not limited by the illustrated order of acts or events, as some acts may occur in different orders and / or simultaneously with other acts or events. Furthermore, not all of the illustrated acts, steps or events are required to implement a methodology in accordance with the present invention. Many of the techniques and procedures described, or referred to herein, are well understood and commonly used using conventional methodology by those skilled in the art. Unless otherwise defined, all terms of art, notations, and other terms or scientific terminology used herein are intended to have the meanings commonly understood by those skilled in the art to which this invention pertains. In some cases, terms with commonly understood meanings are defined in this description for clarity and / or for quick reference, and the inclusion of such definitions in this description should not necessarily be construed to represent a material difference from what is generally understood. in technique. It will further be understood that terms, such as those defined in commonly used dictionaries, are to be construed as having a meaning that is consistent with their meaning in the context of the relevant art and / or as otherwise defined herein. . The terminology used in the present description is for the purpose of describing only particular embodiments and is not intended to be limiting. As used herein, the indefinite articles one, an, and the are to be understood to include plural references unless the context clearly indicates otherwise. Chimeric antagonist receptors The present invention relates generally to the use of genetically modified T cells to stably express a desired chimeric antigen receptor. A chimeric antigen receptor (CAR) is an artificially constructed hybrid protein or polypeptide that contains the antigen-binding domains of an antibody (scFv) linked to T-cell signaling domains. Characteristics of CARs can include their ability to redirect the specificity and reactivity of T cells towards a selected target in a non-MHC-restricted manner, thus exploiting the antigen-binding properties of monoclonal antibodies. Non-MHC-restricted antigen recognition gives CAR-expressing T cells the ability to recognize antigens independent of antigen processing, thus avoiding a major mechanism of tumor evasion. Furthermore, when expressed in T cells, the MA / t / ZUZI / U / 4400 CARs advantageously do not dimerize with the endogenous T cell receptor (TCR) alpha and beta chains. The CARs described herein provide recombinant polypeptide constructs comprising at least one extracellular antigen-binding domain, one transmembrane domain, and one intracellular signaling domain (also referred to herein as cytoplasmic signaling domain) comprising a functional signaling derived from a stimulatory molecule as defined below. T cells expressing a CAR are referred to herein as CAR T cells, CAR-T cells, or CAR-modified T cells, and these terms are used interchangeably herein. The cell can be genetically engineered to stably express an antibody-binding domain on its surface, conferring a novel antigen specificity that is independent of MHC. In some cases, the T cell is genetically engineered to stably express a CAR that combines an antigen recognition domain of a specific antibody with an intracellular domain of the CD3-zeta chain or FcyRI protein into a single chimeric protein. In one embodiment, the stimulatory molecule is the zeta chain associated with the T cell receptor complex. An intracellular signaling domain, as the term is used herein, refers to an intracellular portion of a molecule. It is the functional portion of the protein that acts by transmitting information within the cell to regulate cellular activity through defined signaling pathways by generating second messengers or by functioning as effectors by responding to such messengers. The intracellular signaling domain generates a signal that promotes an immune effector function of the CAR-containing cell, e.g. eg, a CAR-T cell. Examples of immune effector function, e.g. eg, in a CAR-T cell, they include cytolytic activity and auxiliary activity, which includes cytokine secretion. In one embodiment, the intracellular signaling domain may comprise a primary intracellular signaling domain. Illustrative primary intracellular signaling domains include those derived from the molecules responsible for primary stimulation, or antigen-dependent simulation. In one embodiment, the intracellular signaling domain may comprise a costimulatory intracellular domain. Illustrative costimulatory intracellular signaling domains include those derived from the molecules responsible for costimulatory signals, or antigen-independent simulation. For example, in the case of a CAR-T, a primary intracellular signaling domain may comprise a cytoplasmic sequence of a T cell receptor, and a costimulatory intracellular signaling domain may comprise the cytoplasmic sequence of the coreceptor or costimulatory molecule. A primary intracellular signaling domain may comprise a motif of ΜΛ / t / ZUZ I / U / 4400 signaling is known as a tyrosine-based immunoreceptor activation motif or ITAM. Examples of ΓΤΑΜ that contain primary cytoplasmic signaling sequences include, but are not limited to, those derived from CD3-zeta, FcR gamma, FcR beta, CD3 gamma, CD3 delta, CD3 epsilon, CD5, CD22, CD79a, CD79b, and CD66d DAP10 and DAP12. The primary intracellular signaling domain can be derived from the signaling domains of, for example, CD3-zeta, CD3 epsilon, CD22, CD79a, CD66d, CD39 DAP10, DAP12, Fe receptor I epsilon gamma chain (FCER1G), FcR beta , CD3 delta, CD3 gamma, CD5, CD226 or CD79B. The term zeta or alternatively zeta chain, CD3-zeta or TCR-zeta is defined as the protein given as GenBank accession number BAG36664.1, or the equivalent residues from a non-human species, e.g. g., murine, rabbit, primate, mouse, rodent, monkey, ape and the like, and a zeta-stimulatory domain or alternatively a CD3-zeta-stimulatory domain or a TCR-zeta-stimulatory domain is defined as the amino acid residues of the zeta chain cytoplasmic domain that are sufficient to functionally transmit an initial signal necessary for T cell activation. In one aspect, the zeta cytoplasmic domain comprises residues 52 to 164 of GenBank accession number BAG36664.1 or those equivalent residues from a non-human species, e.g. eg, mouse, rodent, monkey, ape, and the like, which are functional orthologs thereof. In a preferred embodiment, the intracellular signaling domain comprises a CD3-zeta stimulatory domain. In one aspect, the zeta-stimulatory domain or a CD3-zeta-stimulatory domain is the sequence provided as SEQ ID NO: 13. The term "costimulatory molecule" refers to the analogous binding partner on a T cell that specifically binds to a costimulatory ligand, thereby mediating a costimulatory response by the T cell, such as, but not limited to, proliferation. Costimulatory molecules are cell surface molecules other than antigen receptors or their ligands that are required for an effective immune response. Costimulatory molecules include, but are not limited to, an MHC class 1 molecule, BTLA, and a Toll ligand receptor, as well as 0X40, CD2, CD27, CD28, CDS, ICAM-1, LFA-1 (CDlla / CD18 ), 41BB (CD137), CD30, CD40, CD54 (ICAM), CD83, CD134 (OX40), CD150 (SLAMF1), CD152 (CTLA4), CD223 (LAG3), CD270 (HVEM), CD278 (ICOS), DAP10, LAT, NKD2C SLP76, TRIM, BTLA, GITR, CD226, HVEM, and ZAP70. A costimulatory intracellular signaling domain may be the intracellular portion of a costimulatory molecule. A costimulatory molecule can be represented by the following families of proteins: TNF receptor proteins, immunoglobulin-like proteins, cytokine receptors, integrins, lymphocyte activation signaling molecules (SLAM proteins), and NK cell activation receptors. Examples of such IVIA / I / U / 4400 molecules include CD27, CD28, 4-1BB (CD137), 0X40, GITR, CD30, CD40, ICOS, BAFFR, HVEM, lymphocyte function-associated antigen-1 (LFA-1), CD2, CD7, LIGHT, NKG2C, SLAMF7, NKp80, CD160, B7-H3, and a ligand that specifically binds CD83 and the like. The intracellular signaling domain may comprise the entire intracellular portion, or the entire native intracellular signaling domain, of the molecule from which it is derived, or a functional fragment thereof. The term 4-1BB refers to a member of the TNFR superfamily with an amino acid sequence given as GenBank accession number AAA62478.2, or the equivalent residues from a non-human species, e.g. eg, mouse, rodent, monkey, ape and the like; and a 4-1BB costimulatory domain is defined as amino acid residues 214-255 of GenBank accession no. AAA62478.2, or the equivalent residues from a non-human species, e.g. eg, mouse, rodent, monkey, ape and the like. In one aspect, the 4-1BB costimulatory domain is the sequence provided as SEQ ID NO: 12 or the equivalent residues from a non-human species, e.g. eg, mouse, rodent, monkey, ape and the like. In some embodiments, the cytoplasmic signaling domain further comprises one or more functional signaling domains derived from at least one costimulatory molecule as defined herein. In one embodiment, the costimulatory molecule is selected from 4-1BB (ie, CD137), CD27, CD3-zeta, and / or CD28. CD28 is an important T cell marker in T cell costimulation. CD27 is a member of the tumor necrosis factor receptor superfamily and acts as a costimulatory immune control molecule. 4-1BB transmits a strong costimulatory signal to T cells, which promotes differentiation and improves long-term survival of T cells. CD3-zeta associates with TCRs to produce a signal and contains immunoreceptor-based activation motifs. in tyrosine (ΓΓΑΜ, for its acronym in English). In a preferred embodiment, the intracellular signaling domain comprises a costimulatory intracellular signaling domain, wherein the costimulatory intracellular signaling domain is a 4-1BB costimulatory domain. In a preferred embodiment, the 4-1BB costimulatory domain is the sequence provided as SEQ ID NO: 12. In one embodiment, a transmembrane domain that naturally associates with one of the domains in the CAR is used. In another embodiment, the transmembrane domain can be selected or modified by amino acid substitution to avoid binding of such domains to the transmembrane domains of the same or different surface membrane proteins to minimize interactions with other members of the receptor complex. In an illustrative embodiment, the transmembrane domain is the CD8a transmembrane domain. MA / t / ZUZI / U / 4400 In one embodiment, the CAR comprises a hinge domain that comprises a CD8a hinge domain. In one embodiment, the CAR comprises a CD8a hinge domain and a CD8a transmembrane domain. In one embodiment, the CAR comprises a hinge domain comprising a CD8a hinge domain and an intracellular signaling domain comprising CD28, 4-1BB and CD3-zeta. The CARs described herein provide recombinant polypeptide constructs comprising at least one extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain (also referred to herein as cytoplasmic signaling domain) comprising, e.g. eg, a functional signaling domain derived from a stimulatory molecule as defined below. In one embodiment, the CAR comprises a chimeric fusion protein comprising an extracellular antigen recognition domain, a transmembrane domain, and an intracellular signaling domain comprising a functional signaling domain derived from a stimulatory molecule. In one embodiment, the CAR comprises a chimeric fusion protein comprising an extracellular antigen recognition domain, a transmembrane domain, and an intracellular signaling domain comprising a costimulatory molecule-derived functional signaling domain and a derived functional signaling domain. of a stimulatory molecule. In one embodiment, the CAR comprises a chimeric fusion protein comprising an extracellular antigen recognition domain, a transmembrane domain, and an intracellular signaling domain comprising at least two functional signaling domains derived from one or more costimulatory molecule(s). and a functional signaling domain derived from a stimulatory molecule. The CARs of the invention can be designed to comprise the CD28 and / or 4-1BB signaling domain by itself or combined with any other desired cytoplasmic domain useful in the context of the CARs of the invention. In one embodiment, the cytoplasmic domain of CAR may further comprise the signaling domain of CD3zeta. For example, the cytoplasmic domain of CAR can include, but is not limited to, CD3-zeta, 4-1BB, and CD28 signaling modules and combinations of these. In a preferred embodiment, the CAR comprises a CD8a hinge domain, a CD8a transmembrane domain, and an intracellular signaling domain comprising the CD3-zeta signaling domain. In a preferred embodiment, the CAR comprises a CD8a hinge domain, a CD8a transmembrane domain, and an intracellular signaling domain comprising the MA / t / ZUZI / U / 4400 Cd3-zeta signaling domain and a 4-1BB costimulatory domain. Accordingly, the invention provides CAR T cells and methods for their use in adoptive therapy. The description further provides variants, e.g. eg, functional variants of the CARs, nucleic acids, polypeptides and proteins described herein. "Variant" refers to a polypeptide or polynucleotide that differs from a reference polypeptide or reference polynucleotide by one or more modifications, eg, substitutions, insertions, or deletions. The term functional variant, as used herein, refers to a CAR, polypeptide, or protein that has substantial or significant sequence identity or similarity to a parent CAR, polypeptide, or protein, which functional variant retains the biological activity of the parent CAR, polypeptide, or protein. CAR, polypeptide or protein for which it is a variant. Functional variants encompass e.g. those variants of the CAR, polypeptide, or protein described herein (the parent CAR, polypeptide, or protein) that retain the ability to recognize target cells to a similar extent, the same extent, or to a greater extent, as the CAR, parent polypeptide or protein. Referring to the parent CAR, polypeptide or protein, the functional variant can be, for example, at least about 30%, about 40%, about 50%, about 60%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99% or more identical in amino acid sequence to the CAR, polypeptide, or original protein. In the present disclosure, the structure of polypeptides is found at defined locations on the basis of % sequence identity to a reference sequence mentioned (with a determined seq. id. no.). In this context, the % sequence identity between two amino acid sequences can be determined by comparing these two optimally aligned sequences, and in which the amino acid sequence to be compared can comprise additions or deletions with respect to the reference sequence. for optimal alignment between these two sequences. Percent identity is calculated by determining the number of identical positions for which the amino acid residue is identical between the two sequences, dividing this number of identical positions by the total number of positions in the comparison window, and multiplying the result obtained by 100 to obtain the percent identity between these two sequences. Typically, the comparison window corresponds to the full length of the sequence being compared. For example, it is possible to use the BLAST program, BLAST 2 sequences (Tatusova et al, Blast 2 sequences - a new tool for comparing protein and nucleotide sequences, FEMS Microbiol Lett. 174:247-250) MA / t / ZUZI / U / 4400 available at the site http: / / www.ncbi.nlm.nih.gov / gorf / bl2.html, the parameters used are those determined by default (particularly for the gap penalty parameters). open: 5 and penalty for extension gaps: 2; the chosen matrix which is, for example, the BLOSUM 62 matrix proposed by the program), the percentage of identity between the two sequences to be compared is calculated directly by the program. Determining the sequence identity of a query sequence to a reference sequence is within the ability of the skilled artisan and can be performed using commercially available analysis software such as BLAST™. A functional variant can comprise, for example, the amino acid sequence of the original CAR, polypeptide or protein with at least one conservative amino acid substitution. In another embodiment, functional variants may comprise the original CAR, polypeptide, or protein amino acid sequence with at least one conservative amino acid substitution. In this case, the non-conservative amino acid substitution may not interfere with or inhibit the biological activity of the functional variant. Non-conservative amino acid substitution can enhance the biological activity of the functional variant such that the biological activity of the functional variant is increased compared to the parent CAR, polypeptide or protein. The amino acid substitutions of the CARs of the invention may be conservative amino acid substitutions. Conservative amino acid substitutions are known in the art and include amino acid substitutions in which an amino acid having certain physical and / or chemical properties is exchanged for another amino acid having the same chemical or similar physical properties. For example, the conservative amino acid substitution can be an acidic amino acid substituted for another acidic amino acid (eg, Asp or Glu), an amino acid with a nonpolar side chain substituted for another amino acid with a nonpolar side chain (eg. g., Ala, Gly, Val, lie, Leu, Met, Phe, Pro, Trp, Val, etc.), a basic amino acid substituted by another basic amino acid (Lys, Arg, etc.), an amino acid with a side chain polar substituted by another amino acid with a polar side chain (Asn, Cys, Gln, Ser, Thr, Tyr, etc.), etc. The CAR, polypeptide or protein may consist essentially of the specified amino acid sequence(s) described herein, such that other components e.g. eg, other amino acids, do not materially change the biological activity of the functional variant. The CARs, polypeptides, and proteins of the embodiments of the disclosure (including functional portions and functional variants) may be of any length, that is, they may comprise any number of amino acids, as long as the CARs, polypeptides, or proteins (or portions functional or functional variants thereof) retain their activity MA / t / ZUZI / U / 4400 biological, p. eg, the ability to specifically bind to an antigen, detect diseased cells (eg, cancer cells) in a host, or treat or prevent disease in a host, etc. For example, the polypeptide can be from about 50 to about 5000 amino acids long, such as about 50, about 70, about 75, MA / t / ZUZI / U / 4400 about 100, about 200, about 300, about 400, about 500, about 600, about 700, about 800, about 900, about 125, about 225, about 325, about 425, about 525 , about 625, about 725, about 825, about 925, about 150, about 250, about 350, about 450, about 550, about 650, about 750, about 850, about 950, about 175, about 275, about 375 about 475 , about 575, about 675. about 775, about 875, about 975 about 1000 or more amino acids in length. Polypeptides of the invention also include oligopeptides. The CARs, polypeptides, and proteins of embodiments of the invention (including functional portions and functional variants of the invention) may comprise synthetic amino acids instead of one or more naturally occurring amino acids. Such synthetic amino acids are known in the art and include, for example, aminocyclohexane carboxylic acid, norleucine, α-amino n-decanoic acid, homoserine, S-acetylaminomethyl-cysteine, trans-3- and trans-4-hydroxyproline, 4-aminophenylalanine, 4 -nitrophenylalanine, a-(2-amino-2-norbornane)-carboxylic acid, α,γ-diaminobutyric acid, α,β-diaminopropionic acid, homophenylalanine, 4-chlorophenylalanine, 4-carboxyphenylalanine, β-phenylserine β-hydroxyphenylalanine, phenylglycine, a Naphthylalanine, Cyclohexylalanine, Cyclohexylglycine, N'-benzyl-N'-methyl-lysine, Ν',Ν'-dibenzyl-lysine, 6-hydroxylysine, ornithine, α-aminocyclopentane carboxylic acid, α-aminocyclohexane carboxylic acid, α-aminocycloheptane carboxylic acid, indoline-2-carboxylic acid, 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid, aminomalonic acid, aminomalonic acid monoamide and d-tert-butylglycine. CARs, polypeptides and proteins of embodiments of the invention (including functional portions and functional variants) may be subject to post-translational modifications. These can be glycosylated, esterified, N-acylated, amidated, carboxylated, phosphorylated, esterified, cyclized via, e.g. eg, a disulfide bridge, or converted to an acid addition salt. In some embodiments, these are dimerized or polymerized, or conjugated. CARs, polypeptides and / or proteins of embodiments of the invention (including functional portions and functional variants thereof) can be obtained by methods known in the art. Suitable methods for synthesizing de novo polypeptides and proteins are described in references such as Chan et al., Fmoc So / id Phase Peptide Synthesis, Oxford University Press, Oxford, United Kingdom, 2000; Peptide and Protein Drug Analysis, ed. Reid, R., Marcel Dekker, Inc., 2000; and Epitope Mapping, ed. Westwood et al., Oxford University Press, Oxford, United Kingdom, 2001. Also, polypeptides and proteins can be produced recombinantly using the nucleic acids described herein using standard recombinant methods. See, for example, Sambrook et al., Molecular Cioning: A Laboratory Manual, 3rd ed., Cold Spring Harbor Press, Cold Spring Harbor, N.Y. 2001; and Ausubel et al., Current Protoco / s in Molecular Bio / ogy, Greene Publishing Associates and John Wiley & Sons, NY, 1994. In addition, some of the CARs, polypeptides, and proteins of the invention (including functional portions and functional variants of these) can be isolated and / or purified from a source, such as a plant, a bacterium, an insect, a mammal, etc. Isolation and purification methods are known in the art. Alternatively, the CARs, polypeptides and / or proteins described herein (including functional portions and functional variants thereof) can be commercially synthesized. In this sense, CARs, polypeptides and proteins can be synthetic, recombinant, isolated and / or purified. Examples of modified nucleotides that can be used to generate the recombinant nucleic acids used to produce the polypeptides described herein include, but are not limited to, 5-fluorouracil, 5-bromouracil, 5-chlorouracil, 5-iodouracil, hypoxanthine, xanthine, 4-acetylcytosine, 5-(carboxyhydroxymethyl)uracil, carboxymethylaminomethyl-2-thiouridine, 5-carboxymethylaminomethyluracil, dihydrouracil, N6-substituted adenine, 7-methylguanine, 5-methylaminomethyluracil, 5-methoxyaminomethyl-2-thiouracil, beta-D-mannosylkeosine , 5-methoxycarboxymethyluracil, 5-methoxyuracil, 2-methylthio-N6-isopentenyladenine, uracil-5-oxyacetic acid (v), wibutoxyosin, pseudouracil, cheosin, beta-D-galactosylkeosine, inosine, N6-isopentenyladenin, 1-methylguanine, 1- methylinosine, 2,2-dimethylguanine, 2-methyladenine, 2-methylguanine, 3-methylcytosine, 5-methylcytosine, 2-thiocytosine, 5-methyl-2-thiouracil, 2-thiouracil, 4-thiouracil, 5-methyluracil, ester uracil-5-oxyacetic acid methyl, 3-(3-amino-3-N-2-carboxypropyl) uracil and 2,6-diaminopurine. The nucleic acid may comprise any isolated or purified nucleotide sequence that encodes any of the CARs, polypeptides, or proteins, or functional portions or functional variants thereof. Alternatively, the nucleotide sequence may comprise a nucleotide sequence that is redundant in any of the sequences or a combination of degenerate sequences. Some embodiments of the invention also provide an isolated or purified nucleic acid comprising a nucleotide sequence that is complementary to the nucleotide sequence of any of the nucleic acids described herein. IVIA / I / U / 4400 or a nucleotide sequence that hybridizes under stringent conditions to the nucleotide sequence of any of the nucleic acids described herein. Nucleotide sequence that hybridizes under stringent conditions can hybridize under high stringency conditions. By high stringency conditions it is meant that the nucleotide sequence specifically hybridizes to a target sequence (the nucleotide sequence of any of the nucleic acids described herein) in an amount that is detectably stronger than non-specific hybridization. . High stringency conditions include conditions that would distinguish a polynucleotide with an exactly complementary sequence, or one containing only a few scattered mismatches, from a random sequence that just happened to have a few small regions (eg, 3-12 bases) that matched the nucleotide sequence. Such small regions of complementarity fuse more easily than a full length complement of 14-17 or more bases, and high stringency hybridization makes them readily distinguishable. Relatively high stringency conditions would include, for example, low-salt and / or high-temperature conditions, such as those provided by approximately 0.02-0.1 M NaCl or the equivalent, at temperatures of approximately 50-70°C. Such high stringency conditions tolerate little, if any, nucleotide sequence mismatch and template or target strand, and are particularly well suited for detecting expression of any of the CARs described herein. It is generally appreciated that conditions can be made more stringent by the addition of increasing amounts of formamide. In one embodiment, the nucleic acids of the invention can be incorporated into a recombinant expression vector. The present disclosure provides recombinant expression vectors comprising any of the nucleic acids of the invention. As used herein, the term "recombinant expression vector" means a genetically modified oligonucleotide or polynucleotide construct that allows expression of an mRNA, protein, polypeptide, or peptide by a host cell, when the construct comprises a nucleotide sequence that encodes the mRNA, protein, polypeptide, or peptide, and the vector is contacted with the cell under conditions sufficient for the mRNA, protein, polypeptide, or peptide to be expressed within the cell. The vectors described in the present description are not of natural origin as a whole; however, parts of the vectors may be naturally occurring. The described recombinant expression vectors may comprise any type of nucleotides, including, but not limited to, DNA and RNA, which may be single-stranded or double-stranded, synthesized or obtained in part from natural sources, and which may contain natural, non-natural nucleotides. natural or altered. Recombinant expression vectors may comprise naturally occurring or artificially occurring internucleotide linkages, or both types of linkages. The nucleotide or internucleotide bonds of artificial or altered origin do not IVIA / t / ZUZ I / U / 4400 prevent transcription or replication of the vector. In one embodiment, the recombinant expression vector of the invention can be any suitable recombinant expression vector, and can be used to transform or transfect any suitable host. Suitable vectors include those designed for propagation and expansion or for expression or both, such as plasmids and viruses. The vector can be selected from the group consisting of the pUC series (Fermentas Life Sciences, Glen Burnie, Md.), the pBluescript series (Stratagene, LaJolla, Calif.), the pET series (Novagen, Madison, Wis.), the pGEX (Pharmacia Biotech, Uppsala, Sweden) and the pEX series (Clontech, Palo Alto, Calif.). Bacteriophage vectors can be used, such as AGTIO, AGTll, ÁEMBL4, and ÁNM1149, AZapII (Stratagene). Examples of plant expression vectors include pBIO1, pBI01.2, pBI121, pBI101.3 and pBIN19 (Clontech). Examples of animal expression vectors include pEUK-CI, pMAM, and pMAMneo (Clontech). The recombinant expression vector can be a viral vector, e.g. eg, a retroviral vector, e.g. eg, a gamma retroviral vector. In one embodiment, the recombinant expression vectors of the invention are prepared using standard recombinant DNA techniques described in, for example, Sambrook et al., supra, and Ausubel et al., supra. Expression vector constructs, which are circular or linear, can be prepared to contain a replication system functional in a prokaryotic or eukaryotic host cell. Replication systems can be derived, e.g. eg, from ColEl, SV40, 2 μ plasmid, λ, bovine papillomavirus, and the like. The recombinant expression vector may comprise regulatory sequences, such as transcription and translation initiation and termination codons, that are specific to the type of host (eg, bacteria, plant, fungus, or animal) in which it is to be introducing the vector, as appropriate, and taking into account whether the vector is based on DNA or RNA. The recombinant expression vector can include one or more marker genes, which allow selection of transformed or transfected hosts. Marker genes include biocide resistance, e.g. eg, resistance to antibiotics, heavy metals, etc., complementation in an auxotrophic host to provide prototrophy, and the like. Suitable marker genes for the disclosed expression vectors include, for example, neomycin / G418 resistance genes, histidinol X resistance genes, histidinol resistance genes, tetracycline resistance genes, and ampicillin resistance genes. . The recombinant expression vector may comprise a native or regulatory promoter operably linked to the nucleotide sequence encoding the CAR, polypeptide, or protein (including functional portions and functional variants thereof) or to the nucleotide sequence that is complementary to or hybridizes to. the nucleotide sequence encoding the CAR, polypeptide or protein. The selection of promoters, p. g., strong, weak, specific to the IVIA / t / ZUZI / U / 4400 tissue, inducible and developmentally specific, are within the skill of the skilled man. Similarly, the combination of a nucleotide sequence with a promoter is also within the skill of the skilled person. The promoter can be a non-viral promoter or a viral promoter, e.g. eg, a cytomegalovirus (CMV) promoter, an RSV promoter, an SV40 promoter, or a promoter discovered in the long terminal repeat of murine stem cell virus. Recombinant expression vectors can be designed for either transient expression, stable expression, or both. Furthermore, recombinant expression vectors can be created for constitutive expression or for inducible expression. Additionally, recombinant expression vectors can be created to include a suicide gene. As used herein, suicide gene refers to a gene that causes the cell expressing the suicide gene to die. The suicide gene may be a gene that confers sensitivity to an agent, e.g. eg, a drug, after the cell in which the gene is expressed, and causes the cell to die when the cell comes in contact with or is exposed to the agent. Suicide genes are known in the art and include, for example, the herpes simplex virus (HSV) thymidine kinase (TK) gene, cytosine deaminase, purine nucleoside phosphorylase, and nitroreductase. Included within the scope of the invention are conjugates, e.g. Bioconjugates, comprising any of CARs, polypeptides or proteins (including any functional portions or variants thereof), host cells, nucleic acids, recombinant expression vectors, host cell populations, or antibodies or portions of binding to their antigen. Conjugates, as well as methods for synthesizing conjugates in general, are known in the art (see, for example, Hudecz, F., Methods Mol. Bio!. 298: 209-223 (2005) and Kirin et al., Inorg Chem. 44(15): 5405-5415 (2005)). An embodiment of the invention further provides an antibody, or antigen-binding portion thereof, that binds, e.g. eg, it specifically binds to an epitope of the CARs of the invention. The antibody can be any type of immunoglobulin that is known in the art. Immunoglobulins can be assigned to five main classes: IgA, IgD, IgE, IgG, and IgM. IgA and IgG are further subclassified as the isotypes IgAl, IgA2, IgGl, IgG2, IgG3, and IgG4. Antibody light chains from vertebrate species can be assigned to one of two types, kappa (k) and lambda (λ), based on the amino acid sequences of their constant domains. The antibody can be of any class or isotype. Antibodies include immunoglobulin molecules including monoclonal antibodies including murine, human, humanized and chimeric monoclonal antibodies, antigen-binding fragments, polyclonal, bispecific or multispecific antibodies, monomeric, dimeric, tetrameric or multimeric antibodies, antibodies of MA / t / ZUZI / U / 4400 single chain, domain antibodies and any other modified configuration of the immunoglobulin molecule comprising an antigen binding site of the required specificity. The antibody can be a naturally occurring antibody, e.g. eg, an antibody isolated and / or purified from a mammal, e.g. eg, murine, primate, mouse, rabbit, goat, horse, chicken, hamster, human, etc. Alternatively, the antibody can be an engineered (eg, engineered) antibody. "Human antibody" refers to an antibody that is optimized to have a minimal immune response when administered to a human subject. Human antibody variable regions are derived from human immunoglobulin sequences. If the human antibody contains a constant region or a constant region portion, the constant region is also derived from human immunoglobulin sequences. The human antibody comprises heavy and light chain variable regions that are derived from sequences of human origin if the human antibody variable regions are derived from a system using human germline immunoglobulin or rearranged immunoglobulin genes. Illustrative such systems are phage-displayed human immunoglobulin gene libraries and non-human transgenic animals, such as mice or rats carrying human immunoglobulin loci. Human antibody typically contains amino acid differences compared to human-expressed immunoglobulins due to differences between the systems used to obtain the human antibody and human immunoglobulin loci, the introduction of somatic mutations, or the intentional introduction of substitutions in the human antibody. the frames or the CDRs, or both. Typically, the human antibody is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%. , 94%, 95%, 96%, 97%, 98%, or 99% identical in amino acid sequence to an amino acid sequence encoded by human germline immunoglobulin or rearranged immunoglobulin genes. In some cases, the human antibody may contain consensus framework sequences derived from analysis of human framework sequences, eg, as described in Knappiket al., (2000) J Mol Biol 296:57-86, or a synthetic HCDR3 incorporated into phage-displayed human immunoglobulin gene libraries, eg, as described in Shi et al., (2010) J Mol Biol 397:385-96, and in International Patent Publication No. WO2009 / 085462. Antibodies in which at least one CDR is derived from a non-human species are not included in the definition of a human antibody. "Humanized antibodies" refers to an antibody in which at least one CDR is derived from a non-human species and at least one framework is derived from human immunoglobulin sequences. The humanized antibody may include in-frame substitutions such that the frames may not be exact copies of the expressed human immunoglobulin or human immunoglobulin germline gene sequences. / U / 4400 Typically humanized antibodies have antigen binding sites derived from the non-human species and the variable region frameworks are derived from human immunoglobulin sequences. Human antibodies have heavy and light chain variable regions in which both the framework and the antigen-binding site are derived from sequences of human origin. Also, the antibody can have any level of affinity or avidity for the functional portion of the CAR. In some embodiments, the antibody can bind to the GPRC5D antigen with a range of affinities (Kd). In an embodiment according to the invention, and in some embodiments of each and every one of the numbered embodiments indicated below, the antibody binds to the GPRC5D antigen with high affinity, for example, with a Kd equal to or less than about ΙΟ' 7M, such as, but not limited to, 1-9.9 (or any interval or value therein, such as 1, 2, 3, 4, 5, 6, 7, 8, or 9)xl0'8Μ, ΙΟ'9Μ , ΙΟ'10Μ, ΙΟ'11Μ, ΙΟ'12Μ, ΙΟ'13Μ, 10'14M, ΙΟ'15M, or any interval or value therein, as determined by surface plasmon resonance or the Kinexa method, as practiced the subject matter experts. An illustrative affinity is equal to or less than lxlO'8M. Another illustrative affinity is equal to or less than lxl O'9M. Methods for evaluating antibodies for the ability to bind to any functional portion of CARs are known in the art and include any antibody-antigen binding assay, such as, for example, radioimmunoassay (RIA). , Western blot, enzyme-linked immunosorbent assay (ELISA), immunoprecipitation, and competitive inhibition assays. Suitable methods for making antibodies are known in the art. For example, standard hybridoma methods are described in, p. eg, Kohler and Milstein, Eur. J. Immunol., 5, 511-519 (1976), Harlow and Lane (eds.), Antibodies: A Laboratory Manual, CSH Press (1988), and C. A. Janeway et al. (eds.), Immunobiology, 5th Ed., Garland Publishing, New York, N.Y. 2001)). Alternatively, other methods, such as the EBV hybridoma methods (Haskard and Archer, 1 Immunol. Methods, 74(2), 361-67 (1984), and Roder et al., Methods EnzymoL, 121, 140-67 ( 1986)), and bacteriophage vector expression systems (see, eg, Huse et al., Science, 246, 1275-81 (1989)) are known in the art. In addition, methods for producing antibodies in non-human animals are described in, p. eg, US Pat. Nos. 5,545,806, 5,569,825, and 5,714,352, and in US Patent Application Publication No. 2002 / 0197266 Al). Phage display can also be used to generate an antibody. In this regard, phage libraries encoding antigen-binding variable (V) domains of antibodies can be generated using standard molecular biology and recombinant DNA techniques. MA / t / ZUZI / U / 4400 (see, eg, Sambrook et al., supra, and Ausubel et al., supra). Phage encoding a variable region with the desired specificity are selected for specific binding to the desired antigen (ie, GPRC5D), and a complete or partial antibody comprising the selected variable domain is reconstituted. The nucleic acid sequences encoding the reconstituted antibody are introduced into a suitable cell line, such as a myeloma cell used for hybridoma production, such that antibodies having the characteristics of monoclonal antibodies are secreted by the cell. (see, eg, Janeway et al., supra, Huse et al., supra, and US Patent No. 6,265,150). Antibodies can be produced by transgenic mice that are transgenic for specific heavy and light chain immunoglobulin genes. Such methods are known in the art and are described in, for example, US Pat. 5,545,806 and 5,569,825, and Janeway et al., supra. Methods for generating humanized antibodies are known in the art and are described in, for example, Janeway et al., supra, US Pat. 5,225,539, 5,585,089 and 5,693,761, European patent no. 0239400 Bl, and UK patent no. 2,188,638. Humanized antibodies can also be generated using the antibody coating technology described in US Pat. 5,639,641 and Pedersen et al, J. Mol. Bel., 235, 959-973 (1994). Antibodies, as used herein, can be intact or multichain or single chain immunoglobulins, and can be derived from natural sources or from recombinant sources. Antibodies can be tetramers of immunoglobulin molecules. In some embodiments, the antibody is a bispecific antibody. Bispecific refers to a molecule (such as an antibody) that specifically binds to two different antigens or two different epitopes within the same antigen. The bispecific molecule may cross-react with other related antigens, for example with the same antigen from other (homologous) species, such as human or monkey, for example Macaca fascicularis(cwomo\Q\js} or Pan trog / odytes, or may bind to an epitope that is shared between two or more distinct antigens The VL and / or VH regions of existing antibodies or de novo identified VL and VH regions as described herein may be engineered into full-length bispecific antibodies Such bispecific antibodies can be made by modulating CH3 interactions in the Fe of the antibody to form bispecific antibodies using technologies such as those described in US Patent No. 7,695,936; International Patent No. WO04 / 111233, US Patent Publication No. U52010 / 0015133, US Patent Publication No. US2007 / 0287170; international patent publication no. WO2008 / 119353; US patent publication no. ΜΛ / t / ZUZ I / U / 4400 US2009 / 0182127; US patent publication no. US52010 / 0286374; US patent publication no. US2011 / 0123532; international patent publication no. WO2011 / 131746; international patent publication no. WO2011 / 143545; or US Patent Publication No. US2012 / 0149876. For example, the bispecific antibodies of the invention can be generated in vitro in a cell-free environment by introducing asymmetric mutations into the CH3 regions of two monospecific homodimeric antibodies and forming the bispecific heterodimeric antibody from two original monospecific homodimeric antibodies in reducing conditions to allow isomerization of disulfide bonds according to the methods described in international patent publication no. WO2011 / 131746. In the methods, the first monospecific bivalent antibody and the second monospecific bivalent antibody are engineered to have certain substitutions in the CH3 domain that promote heterodimer stability; The antibodies are incubated together under reducing conditions sufficient to allow the cysteines in the hinge region to undergo disulfide bond isomerization; thus generating the bispecific antibody by Fab arm swapping. Incubation conditions can be optimally restored to non-reducers. Illustrative reducing agents that can be used are 2-mercaptoethylamine (2-MEA), dithiothreitol (DTT), dithioerythritol (DTE), glutathione, tris(2-carboxyethyl)phosphine (TCEP), L-cysteine, and beta- mercaptoethanol, preferably a reducing agent selected from the group consisting of: 2-mercaptoethylamine, dithiothreitol and tris(2-carboxyethyl)phosphine. For example, incubation for at least 90 min at a temperature of at least 20 °C in the presence of at least 25 mM 2-MEA or in the presence of at least 0.5 mM dithiothreitol at pH 5-8 can be used. eg at a pH of 7.0 or at a pH of 7.4. The term "antibody fragment" refers to at least a portion of an intact antibody, or recombinant variants thereof, that retains the antigen-binding properties of the parent full-length antibody. Refers to, for example, the antigen-binding domain, e.g. eg, an antigenic determining variable region of an intact antibody, which is sufficient to confer recognition and binding, e.g. eg, specific binding of the antibody fragment to a target, such as an antigen. "Antigen-binding fragment" refers to a portion of an immunoglobulin molecule. Examples of antibody fragments include, but are not limited to, Fab, Fab', F(ab')z and Fv fragments, single chain antibodies (scFv), linear antibodies, single domain antibodies such as sdAb (either VL or VH), camelid VHH domains, and multispecific antibodies formed from antibody fragments. The term scFv refers to a protein comprising at least one antibody fragment comprising a light chain variable region and at least one antibody fragment comprising a heavy chain variable region. In some embodiments, the heavy and light chain variable regions are contiguously linked via ΜΛ / t / ZUZ I / U / 4400 of a short flexible polypeptide linker, and are capable of expression as a single chain polypeptide, and wherein the scFv retains the specificity of the intact antibody from which it is derived. Unless specified, as used herein, an scFv may have the VL and VH variable regions in any order, e.g. eg, with respect to the N-terminus and C-terminus of the polypeptide, the scFv may comprise the VL-linker-VH or may comprise the VH-linker-VL. An embodiment of the invention also provides antigen-binding portions of any of the antibodies described herein. The antigen binding moiety can be any moiety having at least one antigen binding site, such as Fab, F(ab')2, dsFv, sFv, diabodies and triabodies. In some embodiments, the antigen-binding fragments are heavy chain complementarity determining regions (HCDRs) 1, 2 and / or 3, light chain complementarity determining regions (LCDRs) 1, 2 and / or 3, a heavy chain variable region (VH), or a light chain variable region (VL), Fd and Fv fragments, and domain antibodies (dAbs) that comprise (eg, consisting of) either a VH domain or a VL domain. The VH and VL domains may be linked to each other via a linker, e.g. eg, a synthetic linker. Complementarity determining regions (CDRs) are the antigen binding sites on an antibody. CDRs can be defined using several terms: (i) The complementarity determining regions (CDRs), three in the VH (HCDR1, HCDR2, HCDR3), and three in the VL (LCDR1, LCDR2, LCDR3), are based on variability. of the sequence (Wu and Kabat, J Exp Med 132:211-50, 1970; Kabat et al, Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md., 1991 ). (ii) Hypervariable regions, HVR or HV, three in the VH (H1, H2, H3) and three in the VL (L1, L2, L3), refers to the variable domain regions of an antibody whose structure is hypervariable, as defined by Chothia and Lesk (Chothia and Lesk, Mol Biol 196:901-17, 1987). The International ImMunoGeneTics (IMGT) database (http: / / www_imgt_org) presents a standardized numbering and definition of antigen binding sites. The correspondence between the designations of CDR, HV and IMGT is described in Lefranc et al., Dev Comparat Immunol 27:5577, 2003. The term CDR, HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3, as used in the present description , includes CDRs defined by any of the methods described above, Kabat, Chothia, or IMGT, unless otherwise explicitly mentioned in the specification. Also, the antibody, or antigen-binding portion thereof, can be modified to comprise a detectable marker, such as, for example, a radioisotope, a fluorophore, or a fluorophore. ΜΛ / t / ZUZ I / U / 4400 (eg, fluorescein isothiocyanate (FUC), phycoerythrin (PE)), an enzyme (eg, alkaline phosphatase, horseradish peroxidase) and elementary particles (eg, gold particles). The present disclosure also provides a nucleic acid comprising a nucleotide sequence encoding any of the CARs, polypeptides, or proteins described herein (including functional portions and functional variants thereof). The portion of the CAR that comprises an antibody or antibody fragment thereof can exist in a variety of forms where the antigen-binding domain is expressed as part of a contiguous polypeptide chain including, for example, a single-domain antibody fragment. (sdAb), an scFv, and a chimeric or humanized human antibody (Harlow et al., 1999, In: Using Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press, N.Y.; Harlow et al., 1989, In: Antibodies: A Laboratory Manual, Cold Spring Harbor, N.Y.; Houston et al., 1988, Proc. Nati. Acad. Sci. USA 85:5879-5883; Bird et al., 1988, Science 242:423-426) . In one aspect, the antigen binding domain of a CAR composition of the invention comprises an antibody fragment. In one aspect, the CAR comprises an antibody fragment that comprises an scFv. The term "recombinant antibody" refers to an antibody that is generated using recombinant DNA technology, such as, for example, an antibody expressed by a bacteriophage or yeast expression system. The term is also to be construed as an antibody that has been generated by the synthesis of a DNA molecule encoding the antibody and which DNA molecule expresses an antibody protein, or an amino acid sequence specifying the antibody, wherein the sequence of amino acid or DNA sequence has been obtained using recombinant DNA or amino acid sequencing technology that is available and known in the art. The term "antigen" refers to a molecule that elicits an immune response. This immune response may involve either the production of antibodies, or the activation of specific immunologically competent cells, or both. It will be understood by the skilled artisan that any macromolecule, including virtually all proteins or peptides, can serve as an antigen. Furthermore, the antigens can be derived from recombinant or genomic DNA. One of skill will understand that any DNA, comprising a nucleotide sequence or a partial nucleotide sequence encoding a protein that elicits an immune response, therefore encodes an antigen as that term is used herein. Furthermore, one skilled in the art will understand that an antigen need not be encoded solely by a full-length nucleotide sequence of a gene. It is evident that the present description includes, but is not limited to, the use of partial nucleotide sequences of more than one gene and that these sequences of IVIA / I / U / 4400 nucleotides are arranged in various combinations to encode polypeptides that elicit the desired immune response. In one aspect, the disclosure provides a CAR, comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain binds antigen of GPRC5D. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 66, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 67, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 68; a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 58, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 60; a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 39, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40 and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 41; a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 43 and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 44; or a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 45, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and a heavy chain CDR3 having the amino acid sequence from SEQ ID NO: 47; wherein the extracellular antigen binding domain binds the antigen of GPRC5D. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 66, a heavy chain CDR2 having MA / t / ZUZI / U / 4430 has the amino acid sequence of SEQ ID NO: 67 and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 68; wherein the extracellular antigen binding domain binds the antigen of GPRC5D. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 58, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and a heavy chain CDR3 heavy having the amino acid sequence of SEQ ID NO: 60; wherein the extracellular antigen binding domain binds the antigen of GPRC5D. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 39, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40, and a heavy chain CDR3 heavy weight having the amino acid sequence of SEQ ID NO: 41; wherein the extracellular antigen binding domain binds the antigen of GPRC5D. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 43, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 44 wherein the extracellular antigen binding domain binds the GPRC5D antigen. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having the sequence amino acid sequence of SEQ ID NO: 45, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 47; wherein the extracellular antigen binding domain binds the antigen of GPRC5D. In one embodiment, the extracellular antigen-binding domain comprises ΜΛ / t / ZUZ I / U / 4400 the extracellular antigen-binding domain comprising the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 66, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 67, and the heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 68, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 69, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 70, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 71; the extracellular antigen-binding domain comprising the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 58, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and CDR3 heavy chain having the amino acid sequence of SEQ ID NO: 60, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 61, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 62 and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 63 the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 39, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40, and the heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 41, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 48, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 49 and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 50; the extracellular antigen-binding domain comprises heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 43, and CDR3 of heavy chain having the amino acid sequence of SEQ ID NO: 44, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 51, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 52, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 53; or the extracellular antigen-binding domain comprises heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 45, heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and CDR3 heavy chain having the amino acid sequence of SEQ ID NO: 47, and MA / t / ZUZI / U / 4400 further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 54, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 55, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 56. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having an amino acid sequence selected from the group consisting of SEQ ID NO: 66, SEQ ID NO: 58, SEQ ID NO: 39, SEQ ID NO: 42, and SEQ ID NO: : 45, and conservative modifications thereof, wherein the extracellular antigen-binding domain of GPRC5D binds antigen. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR2 having an amino acid sequence selected from the group consisting of SEQ ID NO: 67, SEQ ID NO: 59, SEQ ID NO: 40, SEQ ID NO: 43, and SEQ ID NO: : 46, and conservative modifications thereof, wherein the extracellular antigen-binding domain of GPRC5D binds antigen. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR3 having an amino acid sequence selected from the group consisting of SEQ ID NO: 68, SEQ ID NO: 60, SEQ ID NO: 41, SEQ ID NO: 44, and SEQ ID NO: : 47, and conservative modifications thereof, wherein the extracellular antigen-binding domain of GPRC5D binds antigen. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having an amino acid sequence selected from the group consisting of SEQ ID NO: 66, SEQ ID NO: 58, SEQ ID NO: 39, SEQ ID NO: 42, and SEQ ID NO: : 45, and conservative modifications of these; a heavy chain CDR2 having a selected amino acid sequence MA / t / ZUZI / U / 4400 from the group consisting of SEQ ID NO: 67, SEQ ID NO: 59, SEQ ID NO: 40, SEQ ID NO: 43, and SEQ ID NO: 46, and conservative modifications of these; and a heavy chain CDR3 having an amino acid sequence selected from the group consisting of SEQ ID NO: 68, SEQ ID NO: 60, SEQ ID NO: 41, SEQ ID NO: 44, and SEQ ID NO: 47, and conservative modifications of these; wherein the extracellular antigen binding domain binds the antigen of GPRC5D. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a light chain CDR1 having an amino acid sequence selected from the group consisting of SEQ ID NO: 69, SEQ ID NO: 54, SEQ ID NO: 48, SEQ ID NO: 51, and SEQ ID NO: : 54, and conservative modifications thereof, wherein the extracellular antigen-binding domain of GPRC5D binds antigen. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a light chain CDR2 having an amino acid sequence selected from the group consisting of SEQ ID NO: 70, SEQ ID NO: 55, SEQ ID NO: 49, SEQ ID NO: 52, and SEQ ID NO: : 55, and conservative modifications thereof, wherein the extracellular antigen-binding domain of GPRC5D binds antigen. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a light chain CDR3 having an amino acid sequence selected from the group consisting of SEQ ID NO: 71, SEQ ID NO: 56, SEQ ID NO: 50, SEQ ID NO: 53, and SEQ ID NO: : 56, and conservative modifications thereof, wherein the extracellular antigen-binding domain of GPRC5D binds antigen. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a light chain CDR1 having a selected amino acid sequence MA / t / ZUZI / U / 4400 from the group consisting of SEQ ID NO: 69, SEQ ID NO: 54, SEQ ID NO: 48, SEQ ID NO: 51, and SEQ ID NO: 54, and conservative modifications of these; a light chain CDR2 having an amino acid sequence selected from the group consisting of SEQ ID NO: 70, SEQ ID NO: 55, SEQ ID NO: 49, SEQ ID NO: 52, and SEQ ID NO: : 55, and conservative modifications of these; and a light chain CDR3 having an amino acid sequence selected from the group consisting of SEQ ID NO: 71, SEQ ID NO: 56, SEQ ID NO: 50, SEQ ID NO: 53, and SEQ ID NO: NO: 56, and conservative modifications of these; wherein the extracellular antigen binding domain binds the antigen of GPRC5D. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having an amino acid sequence selected from the group consisting of SEQ ID NO: 66, SEQ ID NO: 58, SEQ ID NO: 39, SEQ ID NO: 42, and SEQ ID NO: : 45, and conservative modifications of these; a heavy chain CDR2 having an amino acid sequence selected from the group consisting of SEQ ID NO: 67, SEQ ID NO: 59, SEQ ID NO: 40, SEQ ID NO: 43, and SEQ ID NO: : 46, and conservative modifications of these; and a heavy chain CDR3 having an amino acid sequence selected from the group consisting of SEQ ID NO: 68, SEQ ID NO: 60, SEQ ID NO: 41, SEQ ID NO: 44, and SEQ ID NO: NO: 47, and conservative modifications of these; and a light chain CDR1 having an amino acid sequence selected from the group consisting of SEQ ID NO: 69, SEQ ID NO: 54, SEQ ID NO: 48, SEQ ID NO: 51, and SEQ ID NO: NO: 54, and conservative modifications of these; a light chain CDR2 having an amino acid sequence selected from the group consisting of SEQ ID NO: 70, SEQ ID NO: 55, SEQ ID NO: 49, SEQ ID NO: 52, and SEQ ID NO: : 55, and conservative modifications of these; and a light chain CDR3 having an amino acid sequence selected from the group consisting of SEQ ID NO: 71, SEQ ID NO: 56, SEQ ID NO: 50, SEQ ID NO: 53, and SEQ ID NO: NO: 56, and conservative modifications of these; wherein the extracellular antigen binding domain binds the antigen of GPRC5D. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and a signaling domain. intracellular MA / t / ZUZI / U / 4400, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 66, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 67, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 68, and further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 69, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 70, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 71 In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 58, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 60, and further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 61, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 62, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 63. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 39, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 41, and further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 48, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 49, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 50. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, a heavy chain CDR2 having the amino acid sequence of IVIA / t / ZUZ I / U / 4430 SEQ ID NO: 43, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 44, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 51, a CDR2 light chain having the amino acid sequence of SEQ ID NO: 52, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 53. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 45, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 47, and further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 54, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 55, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 56. In one embodiment, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 73, 65, 1, 3, and 5, or a heavy chain variable region (HCVR) comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 72, 64, 2, 4 and 6, or a combination of an LCVR comprising an amino acid sequence selected from the group consisting of SEQ ID NOs: 73, 65, 1, 3, and 5, and an HCVR comprising an amino acid sequence selected from the group consisting of SEQ ID NOs: 72, 64, 2, 4, and 6. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence selected from any one of SEQ ID NO: 73, 65, 1, 3, or 5. In some embodiments , the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70% , at least 75%, at least 80%, at least 85%, at least %, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least %, at at least 97%, at least 98%, or at least 99% sequence identity to any one of SEQ ID NO: 73, 65, 1, 3, or 5. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising a IVIA / I / U / 4400 amino acid sequence of SEQ ID NO: 73. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence that is at least 50 %, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least %, at least 92% , at least 93%, at least 94%, at least 95%, at least 96%, at least %, at least 98%, or at least 99% sequence identity to SEQ ID NO: 73. In some embodiments , the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence of SEQ ID NO: 65. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% , of sequence identity to SEQ ID NO: 65. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence of SEQ ID NO: 1. In some In other embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70% %, 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%, or at least 99% sequence identity to SEQ ID NO: 1. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence of SEQ ID NO: 3. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence that is at least 50%, at least 55%, at least %, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least %, at least 91%, at least 92%, at least 93% , at least 94%, at least 95%, at least %, at least 97%, at least 98%, or at least 99%, sequence identity to SEQ ID NO: 3. In some embodiments, the binding domain to the extracellular antigen comprises a light chain variable region (LCVR) comprising an amino acid sequence of SEQ ID NO: 5. In some embodiments, the extracellular antigen binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, identity of MA / t / ZUZI / U / 4400 sequence with SEQ ID NO: 5. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence selected from any one of SEQ ID NO: 72, 64, 2, 4, or 6. In some In other embodiments, the extracellular antigen-binding domain comprises a heavy chain variable region (HCVR) comprising an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70% %, 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%, or at least 99% sequence identity to any one of SEQ ID NO: 72, 64, 2, 4, or 6. In some embodiments, the domain binding to the extracellular antigen comprises a light chain variable region (LCVR) comprising an amino acid sequence of SEQ ID NO: 72. In some embodiments, the extracellular antigen binding domain comprises a heavy chain variable region (HCVR) comprising a amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity with SEQ ID NO: 72. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence of SEQ ID NO: 2. In some embodiments, the binding domain to the extracellular antigen comprises a heavy chain variable region (HCVR) comprising an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99% sequence identity to SEQ ID NO: 64. In some embodiments, the extracellular antigen-binding domain comprises a heavy chain variable region (HCVR) comprising an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 2. In some embodiments, the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence of SEQ ID NO: 6. In some embodiments, the extracellular antigen-binding domain comprises a heavy chain variable region (HCVR) comprising an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99% sequence identity with SEQ / U / 4430 ID NO: 4. In some embodiments, the extracellular antigen-binding domain comprises a heavy chain variable region (HCVR) comprising an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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 at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to SEQ ID NO: 6. In some embodiments, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 73, or an amino acid sequence that is at least 50%, at least 55%, at least %, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least %, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 97%, at least 97%, at least 98%, at least 99% sequence identity thereto, and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 72, or an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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 %, sequence identity of this. In some embodiments, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 65, or an amino acid sequence that is at least 50%, at least 55%, at least %, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least %, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 97%, at least 97%, at least 98%, at least 99% sequence identity thereto, and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 64, or an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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 %, sequence identity of this. In some embodiments, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 1, or an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% sequence identity thereto, and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 2, or MA / t / ZUZI / U / 4400 an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% sequence identity thereof. In some embodiments, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 3, or an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% sequence identity thereto, and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 4, or an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% sequence identity thereof. In some embodiments, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 5, or an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% sequence identity thereto, and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 6, or an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% sequence identity thereof. In some embodiments, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 73 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: :72. In some embodiments, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 65 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: :64. In some embodiments, the extracellular antigen-binding domain comprises: / U / 4400 a light chain variable region comprising an amino acid sequence of SEQ ID NO: 1 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 2. In some embodiments, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 3 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 3 : 4. In some embodiments, the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 5 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 5 :6. In the present disclosure, in embodiments where the amino acid sequence of the VH domain exhibits less than 100% sequence identity to a given reference VH sequence it may nonetheless comprise heavy chain CDRs that are identical to HCDR1, HCDR2 and HCDR3 from the reference sequence while exhibiting amino acid sequence variation within the framework regions. Likewise, embodiments where the VL domain amino acid sequence exhibits less than 100% sequence identity to a given reference sequence may nonetheless comprise light chain CDRs that are identical to LCDR1, LCDR2 and LCDR3 from the reference sequence while exhibiting amino acid sequence variation within the framework regions. Similarly, where a scFv or extracellular domain of a CAR of the disclosure exhibits less than 100% sequence identity to a given reference VH sequence it may nonetheless comprise heavy chain CDRs that are identical to HCDR1, HCDR2 and HCDR3 of the reference sequence and light chain CDRs that are identical to LCDR1, LCDR2 and LCDR3 of the reference sequence, while exhibiting amino acid sequence variation within framework regions. In one embodiment, the extracellular antigen-binding domain comprises an scFv. In some embodiments, the scFv comprises a polypeptide linker between the light chain variable region and the heavy chain variable region. In certain embodiments, the extracellular antigen-binding domain is a scFv comprising an amino acid sequence selected from the group consisting of SEQ ID NOs: 78, 77, 75, 76, 8, 9, 10, 24, 25, and 26 , and specifically binds to a GPRC5D polypeptide (eg, a human GPRC5D polypeptide having the amino acid sequence of SEQ ID NO: 57, or fragments thereof). In some embodiments, the scFv comprises, from the N to the C terminus, a VH, a linker, and a VL (VH-linker-VL). ΜΛ / t / ZUZ I / U / 4400 In some embodiments, the scFv comprises, from the N to the C terminus, the VL, a linker, and the VH (VL-linker-VH). In recombinant expression systems, the linker is a peptide linker and can include any naturally occurring amino acid. Illustrative amino acids that can be included in the linker are Gly, Ser Pro, Thr, Glu, Lys, Arg, lie, Leu, His, and The. The linker should be of a length that is adequate to link the VH and VL in such a way that they form the correct conformation with respect to each other so as to retain the desired activity, such as binding to GPRC5D. The linker can be approximately 5-50 amino acids long. In some embodiments, the linker is approximately 10-40 amino acids long. In some embodiments, the linker is approximately 10-35 amino acids long. In some embodiments, the linker is approximately 10-30 amino acids long. In some embodiments, the linker is approximately 10-25 amino acids long. In some embodiments, the linker is approximately 10-20 amino acids long. In some embodiments, the linker is approximately 15-20 amino acids long. In some embodiments, the linker is 6 amino acids long. In some embodiments, the linker is 7 amino acids long. In some embodiments, the linker is 8 amino acids long. In some embodiments, the linker is 9 amino acids long. In some embodiments, the linker is 10 amino acids long. In some embodiments, the linker is 11 amino acids long. In some embodiments, the linker is 12 amino acids long. In some embodiments, the linker is 13 amino acids long. In some embodiments, the linker is 14 amino acids long. In some embodiments, the linker is 15 amino acids long. In some embodiments, the linker is 16 amino acids long. In some embodiments, the linker is 17 amino acids long. In some embodiments, the linker is 18 amino acids long. In some embodiments, the linker is 19 amino acids long. In some embodiments, the linker is 20 amino acids long. In some embodiments, the linker is 21 amino acids long. In some embodiments, the linker is 22 amino acids long. In some embodiments, the linker is 23 amino acids long. In some embodiments, the linker is 24 amino acids long. In some embodiments, the linker is 25 amino acids long. In some embodiments, the linker is 26 amino acids long. In some embodiments, the linker is 27 amino acids long. In some embodiments, the linker is 28 amino acids long. In some embodiments, the linker is 29 amino acids long. In some embodiments, the linker is 30 amino acids long. In some embodiments, the linker is 31 amino acids long. In some embodiments, the linker is 32 amino acids long. In some embodiments, the linker is 33 amino acids long. In some embodiments, the linker is 34 amino acids long. In some embodiments, the linker is 35 amino acids long. In some embodiments, the linker has 36 MA / t / ZUZI / U / 4400 amino acids long. In some embodiments, the linker is 37 amino acids long. In some embodiments, the linker is 38 amino acids long. In some embodiments, the linker is 39 amino acids long. In some embodiments, the linker is 40 amino acids long. Illustrative linkers that can be used are Gly-rich linkers, Gly- and 5-Ser-containing linkers, Gly- and Ala-containing linkers, Ala and Ser-containing linkers, and other flexible linkers. In one embodiment, the linker polypeptide comprises an amino acid sequence of SEQ ID NO: 7. Other linker sequences may include portions of immunoglobulin hinge area, CL or CH1 derived from any immunoglobulin heavy or light chain isotype. Illustrative linkers that can be used are shown in Table 1. Additional linkers are described, for example, in International Patent Publication No. WO2019 / 060695, incorporated by reference herein in its entirety. In one embodiment, the linker polypeptide comprises a 15 amino acid sequence from any one of SEQ ID NO: 91-123. / U / 4400 Table 1. Linker Name Amino Acid Sequence SEQ ID NO: Linker 1 GGSEGKSSGSGSESKSTGGS 91 Linker 2 GGGSGGGS 92 Linker 3 GGGSGGGSGGGS 93 Linker 4 GGGSGGGSGGGSGGGS 94 Linker 5 GGGSGGGSGGGSGGGSGGGS 95 Linker 6 GGGGS GGGGSGGGGS 96 Linker 7 GGGGSGGGGSGGGGSGGGGS 97 Linker 8 GGGGSGGGGSGGGGSGGGGSGGGGS 98 Linker 9 GSTSGSGKPGSGEGSTKG 99 Linker 10 IRPRAIGGSKPRVA 100 Linker 11 GKGGSGKGGSGKGGS 101 Linker 12 GGKGSGGKGSGGKGS 102 Linker 13 GGGKSGGGKSGGGKS 103 Linker 14 GKGKSGKGKSGKGKS 104 Linker 15 GGGKSGGKGSGKGGS 105 Linker 16 GKPGSGKPGSGKPGS 106 Linker 17 GKPGSGKPGSGKPGSGKPGS 107 Linker 18 GKGKSGKGKSGKGKSGKGKS 108 Linker 19 STAGDTHLGGEDFD 109 Linker 20 GEGGSGEGGSGEGGS 110 Linker 21 GGEGSGGEGSGGEGS 111 Linker 22 GEGESGEGESGEGES 112 Linker 23 GGGES GGEGSGEGGS 113 Linker 24 GEGESGEGESGEGESGEGES 114 Linker 25 GSTSGSGKPGSGEGSTKG 115 Linker 26 PRGASKSGSASQTGSAPGS 116 Linker 27 GTAAAGAGAAGGAAAGAAG 117 Linker 28 GTSGSSGSGSGGSGSGGGG 1 18 Linker 29 GKPGSGKPGSGKPGSGKPGS 119 Linker 30 GSGS 120 Linker 31 APAPAPAPAP 121 Linker 32 APAPAPAPAPAPAPAPAPAPAP 122 Linker 33 AEAAAKEAAAKEAAAAAKEAAAAKEEAAAAAKAAA 123 In one embodiment, the scFv comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 78, 77, 75, 76, 8, 9, 10, 24, 25, and 26. In some embodiments, the scFv comprises an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity with any one of SEQ ID NO: 78, 77, 75, 76, 8, 9, 10, 24, 25 and 26. In some embodiments, the scFv comprises an amino acid sequence of SEQ ID NO: 78. In some embodiments, the scFv comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99% sequence identity to SEQ ID NO: 78. In some embodiments, the scFv comprises an amino acid sequence of SEQ ID NO: 77. In some embodiments, the scFv comprises an amino acid sequence that is at least 50%, at least %, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least % , at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least %, at least 96%, at least 97%, at least 98% or at least 99%, sequence identity to SEQ ID NO: 77. In some embodiments, the scFv comprises an amino acid sequence of SEQ ID NO: 75. In some embodiments, the scFv comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99% sequence identity to SEQ ID NO: 75. In some embodiments, the scFv comprises an amino acid sequence of SEQ ID NO: 76. In some embodiments, the scFv comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99% sequence identity to SEQ ID NO: 76. In some embodiments, the scFv comprises an amino acid sequence of SEQ ID NO: 8. In some embodiments, the scFv comprises an amino acid sequence that is at least 50 %, at least %, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least %, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to SEQ ID NO: 8. In some embodiments, the scFv comprises an amino acid sequence of SEQ ID NO: 9. In some embodiments, the scFv comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 9. In some embodiments, the scFv comprises an amino acid sequence of SEQ ID NO: 10. In In some embodiments, the scFv comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99 %, sequence identity to SEQ ID NO: 10. In some embodiments, the scFv comprises an amino acid sequence of SEQ ID NO: 24.In some embodiments, the scFv comprises an amino acid sequence that is at least 50%, at least %, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least % , at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least %, at least 96%, at least 97%, at least 98% or at least 99%, sequence identity to SEQ ID NO:24. In some embodiments, the scFv comprises an amino acid sequence of SEQ ID NO:25. In some embodiments, the scFv comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99% sequence identity to SEQ ID NO: 25. In some embodiments, the scFv comprises a . IVIA / I / U / 4400 amino acid sequence of SEQ ID NO: 26. In some embodiments, the scFv comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65% , at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 26. In one embodiment, the extracellular antigen-binding domain comprises a signal polypeptide. In some embodiments, the signal polypeptide comprises an amino acid sequence of SEQ ID NO: 11. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 11. In one aspect, the disclosure provides a CAR comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 82, 81, 80, 79, 17, 18, 19, 20, 21 and 22, or a sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% sequence identity thereof. Another feature of CAR having an extracellular antigen-binding domain comprises an amino acid sequence selected from the group consisting of SEQ ID NOs: 82, 81, 80, 79, 17, 18, 19, 20, 21 and 22 is that the extracellular antigen-binding domain binds the antigen of GPRC5D. In one embodiment, the intracellular signaling domain comprises a polypeptide component selected from the group consisting of a component of TNF receptor superfamily member 9 (CD137), a component of the surface glycoprotein CD3 zeta chain (CD3z) from T cells, a component of the differentiation cluster (CD27), a component of the differentiation cluster superfamily member (such as, eg, CD28 or inducible T cell costimulator (ICOS)), and a combination of these. In some embodiments, the CD137 component comprises an amino acid sequence of SEQ ID NO: 12. In some embodiments, the CD137 component comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%, sequence identity to the SEQ ID NO: 12. In some embodiments, the CD3z component comprises a sequence of ΜΛ / t / ZUZ I / U / 4400 amino acids of SEQ ID NO: 13. In some embodiments, the CD3z component comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%, sequence identity to SEQ ID NO: 13. In some embodiments, the intracellular signaling domain comprises a CD137 component and a CD3z component. In one embodiment, the intracellular signaling domain comprises the amino acid sequence of SEQ ID NO: 14. In some embodiments, the intracellular signaling domain comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99%, of identity sequence with SEQ ID NO: 14. The CAR transmembrane domain can be derived from the transmembrane domain of CD8, an α, β or ζ chain of a T cell receptor, CD28, CD3 epsilon, CD45, CD4, CD5, CD8, CD9, CD16, CD22, CD33, CD37, CD64, CD80, CD86, CD134, CD137, CD154, KIRDS2, OX40, CD2, CD27, LFA-1 (CDI la, CD18), ICOS (CD278), 4-1 BB (CD137), 4-1 BBL, GITR, CD40, BAFFR, HVEM (LIGHTR), SLAMF7, NKp80 (KLRFI), CD160, CDI 9, IL2R beta, IL2R gamma, IL7R a, ITGA1, VLA1, CD49a, ITGA4, IA4, CD49D, ITGA6, VLA-6, CD49f, ITGAD, CDI Id, ITGAE, CD103, ITGAL, CDI la, LFA-1, ITGAM, CDI Ib, UGAX, CDI le, ITGB1, CD29, ITGB2, CDI 8, LFA-1, ITGB7, TNFR2, DNAM1 (CD226), SLAMF4 (CD244, 2B4), CD84, CD96 (touch), CEACAM1, CRT AM, Ly9 (CD229), CD160 (BY55), PSGL1, CD100 (SEMA4D), SLAMF6 (NTB-A, Lyl08), SLAM (SLAMF1, CD150 , IPO-3), BLAME (SLAMF8), SELPLG (CD162), LTBR, ​​PAG / Cbp, NKp44, NKp30, NKp46, NKG2D, and / or NKG2C. In one embodiment, the transmembrane domain comprises a CD8a transmembrane region (CD8a-TM) polypeptide. In some embodiments, the CD8a-TM polypeptide comprises an amino acid sequence of SEQ ID NO: 15. In some embodiments, the CD8a-TM polypeptide comprises an amino acid sequence that is at least 50%, at least 55% , at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or at least 99% , of sequence identity with SEQ ID NO: 15. In one embodiment, the transmembrane domain comprises at least the transmembrane region(s) of the α, β or ζ chain of the T cell receptor, CD28, CD3 epsilon, CD45, CD4, CD5, CD8, CD8d, CD9, CD16, CD22, CD33, CD37, CD40, CD64, CD80, CD86, CD134, CD137, or CD154. In another embodiment, the transmembrane domain comprises at least the transmembrane domain of ζ, η or FcsRly and -β, MB1 (Iga.), B29 or CD3-y, ζ, or η. In another embodiment, the transmembrane domain is synthetic, eg. e.g., comprising predominantly hydrophobic residues such as leucine and valine, MA / t / ZUZI / U / 4400 a phenylalanine triplet, or tryptophan. In one embodiment, the CAR further comprises a hinge region linking the transmembrane domain to the extracellular antigen-binding domain. In some embodiments, the hinge region is a CD8a hinge region. In some embodiments, the CD8a hinge region comprises an amino acid sequence of SEQ ID NO: 16. In some embodiments, the CD8a hinge region comprises an amino acid sequence that is at least 50, at least 55, at least 60, at least 65, at least 70, at least 75, at least 80, at least 85, at least 90, at least 95, at least 98, or at least 99% sequence identity to SEQ ID NO: 16. In some embodiments , the hinge region comprises the sequence EPKSCDKTHTCPPCP (SEQ ID NO: 124), or comprises an amino acid sequence having at least 50, at least 55, at least 60, at least 65, at least 70, at least 75, at least 80, at least 85, at least 90, at least 95, at least 98, or at least 99% sequence identity to EPKSCDKTHTCPPCP (SEQ ID NO: 124). In some embodiments, the hinge region comprises the sequence ERKCCVECPPCP (SEQ ID NO: 125), or comprises an amino acid sequence having at least 50, at least 55, at least 60, at least 65, at least 70, at least 75 , at least 80, at least 85, at least 90, at least 95, at least 98, or at least 99% sequence identity to ERKCCVECPPCP (SEQ ID NO: 125). In some embodiments, the hinge region comprises the sequence ELKTPLGDTTHTCPRCP(EPKSCDTPPPCPRCP)3(SEQ ID NO: 126), or comprises an amino acid sequence having at least 50, at least 55, at least 60, at least 65, at least 70 , at least 75, at least 80, at least 85, at least 90, at least 95, at least 98, or at least 99% sequence identity to ELKTPLGDTTHTCPRCP(EPKSCDTPPPCPRCP)3 (SEQ ID NO: 126). In some embodiments, the hinge region comprises the sequence ESKYGPPCPSCP (SEQ ID NO: 127), or comprises an amino acid sequence having at least 50, at least 55, at least 60, at least 65, at least 70, at least 75 , at least 80, at least 85, at least 90, at least 95, at least 98, or at least 99% sequence identity to ESKYGPPCPSCP (SEQ ID NO: 127). In one embodiment, the CAR comprises an extracellular antigen-binding domain, a hinge region, a transmembrane domain, and an intracellular signaling domain. In such an embodiment, the hinge region is a CD8a hinge region, the transmembrane domain is a CD8a-TM domain, and the intracellular signaling domain comprises a CD3-zeta domain and a 4-1BB / CD137 domain. In one embodiment, the hinge region is a C8a hinge region comprising the amino acid sequence of SEQ ID NO: 16, the transmembrane domain is a CD8a-TM domain comprising the amino acid sequence of SEQ ID NO: 15, and the intracellular signaling domain comprises a CD3zeta domain and a 4-1BB / CD137 domain, wherein the intracellular signaling domain comprises the amino acid sequence of SEQ ID NO: 14. In one embodiment, the extracellular antigen-binding domain comprises a ΜΛ / t / ZUZ I / U / 4400 amino acid sequence selected from the group consisting of SEQ ID NOs: 82, 81, 80, 79, 17, 18, 19, 20, 21, and 22. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99%, sequence identity with any one of SEQ ID NO: 82, 81, 80, 79, 17, 18, 19, 20, 21, and 22. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 82. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 82. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 81. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 81. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 80. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 80. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 79. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 79. MA / t / ZUZI / U / 4400 In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 17. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 17. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 18. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 18. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 19. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 19. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 20. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 20. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 21. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 21. IVIA / t / ZUZ I / U / 4430 In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence of SEQ ID NO: 22. In some embodiments, the extracellular antigen-binding domain comprises an amino acid sequence that is at least 50%, at least 55% %, at least 60%, at least 65%, at least 70%, 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%, or at least 99%, sequence identity to SEQ ID NO: 22. In one embodiment, a CAR of the present disclosure comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 86, 85, 83, 84, 27, 28, 29, 30, 31, and 32. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 75%, at least 80%, at least 85% %, at least 90%, at least 91%, at least %, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least % or at least 99%, of sequence identity with any one of SEQ ID NO: 86, 85, 83, 84, 27, 28, 29, 30, 31 and 32. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence of SEQ ID NO: 86. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 86. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence of SEQ ID NO: 85. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 85. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence of SEQ ID NO: 83. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 83. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence of SEQ ID NO: 84. In some embodiments, the CAR of the present disclosure comprises ΜΛ / t / ZUZ I / U / 4400 an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99%, sequence identity to SEQ ID NO: 84. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence of SEQ ID NO: 27. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 27. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence of SEQ ID NO: 28. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 28. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence of SEQ ID NO: 29. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 29. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence of SEQ ID NO: 30. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 30. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence of SEQ ID NO: 31. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 31. In some embodiments, the CAR of the present description comprises a sequence of MA / t / ZUZI / U / 4400 amino acids of SEQ ID NO: 32. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 32. In certain embodiments, the CAR may comprise a signal peptide. In certain embodiments, the signal peptide is at the N-terminus of the CAR sequence. In certain embodiments, the signal peptide is at the C-terminus of the CAR sequence. In certain embodiments, the signal peptide comprises or consists of the amino acid sequence of SEQ ID NO: 11. CAR and CAR Constructs Expressing Immunosensitive Cells In one aspect, the disclosure provides isolated nucleic acid molecules that encode the CARs described herein. In some embodiments, the nucleic acid molecule comprises a nucleic acid sequence selected from the group consisting of SEQ ID NO: 90, 89, 87, 88, 33, 34, 35, 36, 37, and 38. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to a nucleotide sequence of SEQ ID NO: 90, 89, 87, 88, 33, 34, 35 , 36, 37, or 38. In certain embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 90. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82 %, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to a nucleotide sequence of SEQ ID NO: 90. In certain embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 89. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% , 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 89. In certain embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 87. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88 %, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 87. In certain In some embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 88. In some / U / 4400 embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81% , 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98 % or 99% identical to a nucleotide sequence of SEQ ID NO: 88. In certain embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 33. In some embodiments, the nucleic acid molecule isolated comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 33. In certain embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 34. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87% , 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 34. In certain embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 35. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82 %, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to a nucleotide sequence of SEQ ID NO: 35. In certain embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 36. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% , 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 36. In certain embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 37. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88 %, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 37. In certain In some embodiments, the nucleic acid molecule comprises a nucleic acid sequence of SEQ ID NO: 38. In some embodiments, the isolated nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 38. The term coding refers to the inherent property of specific nucleotide sequences in a polynucleotide, such as a gene, cDNA, or mRNA, to serve ΜΛ / t / ZUZ I / U / 4400 as templates for the synthesis of other polymers and macromolecules in biological processes that have a defined sequence of nucleotides (eg, rRNA, tRNA, and mRNA) or a defined sequence of amino acids and the biological properties resulting from it. Thus, a gene, cDNA, or RNA, encodes a protein if transcription and translation of mRNA corresponding to that gene produces the protein in a cell or other biological system. Both the coding strand, the nucleotide sequence of which is identical to the mRNA sequence, and the non-coding strand, used as a template for transcription of a gene or cDNA, can be referred to as encoding the protein or other product of that gene or cDNA. Unless otherwise specified, a nucleotide sequence encoding an amino acid sequence includes all nucleotide sequences that are redundant versions of each other and that encode the same amino acid sequence. The nucleotide sequence of a phrase encoding a protein or RNA may also include introns to the extent that the nucleotide sequence encoding the protein may contain intron(s) in some version. The term isolated refers to a homogeneous population of molecules (such as polynucleotides or synthetic polypeptides) that has been separated and / or substantially purified from other components of the system in which the molecules are produced, such as a recombinant cell, as well as a protein that has undergone at least one isolation or purification step. "Isolated" refers to a molecule that is substantially free of other cellular material and / or chemicals and encompasses molecules that are isolated at a higher purity, such as 80%, 81%, 82%, 83%, 84%, 85%. %, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% purity. In some embodiments, the present disclosure provides an expression vector comprising the described nucleic acid molecules (eg, SEQ ID NO: 90, 89, 87, 88, 33, 34, 35, 36, 37, or 38). In some embodiments, the expression vector comprises a nucleic acid molecule comprising a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88 %, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to a nucleotide sequence of SEQ ID NO: 90, 89, 87, 88, 33, 34, 35, 36, 37, or 38. In some embodiments, the expression vector comprises a nucleic acid molecule of SEQ ID NO: 90. In some embodiments, the expression vector comprises a nucleic acid molecule that comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97% , 98% or 99% identical to a nucleotide sequence of SEQ ID NO: 90. In some embodiments, the expression vector comprises an acid molecule IVIA / I / U / 4400 of SEQ ID NO: 89. In some embodiments, the expression vector comprises a nucleic acid molecule comprising a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 89. In some embodiments, the expression vector comprises a nucleic acid molecule of SEQ ID NO: 87. In some embodiments, the expression vector comprises a nucleic acid molecule comprising a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 87. In some embodiments, the expression vector comprises a nucleic acid molecule of the SEQ ID NO: 88. In some embodiments, the expression vector comprises a nucleic acid molecule comprising a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86 %, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 88. In some embodiments, the expression vector comprises a nucleic acid molecule of SEQ ID NO: 33. In some embodiments, the expression vector comprises a nucleic acid molecule that comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96 %, 97%, 98% or 99% identical to a nucleotide sequence of SEQ ID NO: 33. In some embodiments, the expression vector comprises a nucleic acid molecule of SEQ ID NO: 34. In some embodiments, the expression vector comprises a nucleic acid molecule comprising a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89% , 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 34. In some embodiments, the vector The expression vector comprises a nucleic acid molecule of SEQ ID NO: 35. In some embodiments, the expression vector comprises a nucleic acid molecule that comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 35. In some embodiments, the expression vector comprises a nucleic acid molecule of SEQ ID NO: 36. In some embodiments, the expression vector comprises a nucleic acid molecule comprising a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 36. In some embodiments, the expression vector comprises a molecule of acid IVIA / I / U / 4400 nucleic acid of SEQ ID NO: 37. In some embodiments, the expression vector comprises a nucleic acid molecule comprising a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 37. In some embodiments, the expression vector comprises a nucleic acid molecule of SEQ ID NO: 38. In some embodiments, the expression vector comprises a nucleic acid molecule comprising a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ ID NO: 38. The described nucleic acid molecules encode amino acid sequences selected from the group consisting of SEQ ID NO: 86, 85, 83, 84, 27, 28, 29, 30, 31 and 32, or a variant thereof. In some embodiments, the expression vector comprises a nucleic acid molecule that encodes the amino acid sequence of SEQ ID NO: 86. In some embodiments, the expression vector comprises a nucleic acid molecule that encodes an amino acid sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95% , 96%, 97%, 98% or 99% identical to an amino acid sequence of SEQ ID NO: 86. In some embodiments, the expression vector comprises a nucleic acid molecule encoding the amino acid sequence of SEQ ID NO: 85. In some embodiments, the expression vector comprises a nucleic acid molecule encoding an amino acid sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to an amino acid sequence of SEQ ID NO: 85. In some embodiments, the expression vector comprises a nucleic acid molecule encoding the amino acid sequence of SEQ ID NO: 83. In some embodiments, the expression vector comprises a nucleic acid molecule encoding an amino acid sequence which is at least approximately 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to an amino acid sequence of SEQ ID NO: 83. In some embodiments, the expression vector comprises a nucleic acid molecule encoding the amino acid sequence of the SEQ ID NO: 84. In some embodiments, the expression vector comprises a nucleic acid molecule encoding an amino acid sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86 %, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to an amino acid sequence of SEQ ID NO: 84. In some embodiments, the expression vector comprises a nucleic acid molecule encoding the amino acid sequence of SEQ ID NO: 27. In some embodiments, the MA / t / ZUZI / U / 4400 expression vector comprises a nucleic acid molecule encoding an amino acid sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to an amino acid sequence of SEQ ID NO: 27. In some embodiments, the expression vector comprises a nucleic acid molecule encoding the amino acid sequence of SEQ ID NO: 28. In some embodiments, the expression vector comprises a nucleic acid molecule encoding an amino acid sequence which is at least approximately 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to an amino acid sequence of SEQ ID NO: 28. In some embodiments, the expression vector comprises a nucleic acid molecule encoding the amino acid sequence of the SEQ ID NO: 29. In some embodiments, the expression vector comprises a nucleic acid molecule encoding an amino acid sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86 %, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to an amino acid sequence of SEQ ID NO: 29. In some embodiments, the expression vector comprises a nucleic acid molecule encoding the amino acid sequence of SEQ ID NO: 30. In some embodiments, the expression vector comprises a nucleic acid molecule encoding a sequence of amino acids that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94 %, 95%, 96%, 97%, 98% or 99% identical to an amino acid sequence of SEQ ID NO: 30. In some embodiments, the expression vector comprises a nucleic acid molecule encoding the amino acid sequence of SEQ ID NO: 31. In some embodiments, the expression vector comprises a nucleic acid molecule encoding an amino acid sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85% , 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to an amino acid sequence of the SEQ ID NO: 31. In some embodiments, the expression vector comprises a nucleic acid molecule encoding the amino acid sequence of SEQ ID NO: 32. In some embodiments, the expression vector comprises a nucleic acid molecule encoding an amino acid sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93% , 94%, 95%, 96%, 97%, 98% or 99% identical to an amino acid sequence of SEQ ID NO: 32. In the present disclosure, the structure of nucleic acid molecules is found at defined locations on the basis of % sequence identity with a reference sequence mentioned (with a given seq. id. no.). In this context, % sequence identity with respect to nucleic acid molecules refers to the similarity between at least two different nucleic acid sequences. When a position in both compared sequences is occupied by the same base / U / 4400, e.g. For example, if a position in each of two DNA molecules is occupied by adenine, then the molecules are identical at that position. The percent identity between two sequences is a function of the number of matching or homologous positions shared by the two sequences divided by the number of compared positions and multiplied by 100. For example, if 6 out of 10 of the positions in two sequences are matching or homologous, then the two sequences are 60% identical (or homologous). As an example, the DNA sequences ATTGCC and TATGGC share 50% identity (or homology). Generally, a comparison is made when two sequences align to give maximum homology. The respective percent identity can be determined by standard alignment algorithms, eg the Basic Local Alignment Search Tool (BLAST) described by Altsshul et al. ((1990) 1 Mol. Biol. 215:403-10 ); the algorithm of Needleman et al. ((1970) 1 Mol. Biol. 48:444-53 ); or the algorithm of Meyers et al. ((1988) Comput. Solic. Biosci. 4:11-17). One set of parameters can be the Blosum 62 scoring matrix with a break penalty of 12, a break extension penalty of 4, and a frameshift break penalty of 5. The percent identity between two sequences Amino acid length can also be determined using the Meyers and Miller ((1989) CABIOS 4:11-17) algorithm, which has been incorporated into the ALJGN program (version 2.0), using a PAM120 weight residue table, a length penalty for interrupt of 12, and an interrupt penalty of 4. Percent identity is usually calculated by comparing sequences of similar length. The term "expression vector" refers to a vector comprising a recombinant polynucleotide comprising expression control sequences operably linked to a nucleotide sequence to be expressed. An expression vector comprises sufficient cis-acting elements for expression; other elements for expression can be delivered by the host cell or in an in vitro expression system. Expression vectors include all those known in the art, including cosmids, plasmids (eg, naked or contained in liposomes), and viruses (eg, lentiviruses, retroviruses, adenoviruses, and adeno-associated viruses) incorporating the recombinant polynucleotide. In one embodiment, the present disclosure provides a cell that expresses the nucleic acid molecule described in the present disclosure. In one embodiment, the present disclosure provides a cell that expresses a CAR of the present disclosure. In one embodiment, the CAR of the present disclosure comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 86, 85, 83, 84, 27, 28, 29, 30, 31, and 32. In some embodiments, the CAR of the present disclosure comprises an amino acid sequence having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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 ΜΛ / t / ZUZ I / U / 4400 minus 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to any one of SEQ ID NO: 86, 85 , 83, 84, 27, 28, 29, 30, 31 and 32. MA / t / ZUZI / U / 4400 In some embodiments, the CAR comprises an amino acid sequence of SEQ ID NO: 86. In some embodiments, the CAR comprises an amino acid sequence of SEQ ID NO: 85. In some embodiments, the CAR comprises an amino acid sequence of SEQ ID NO: 83. In some embodiments, the CAR comprises an amino acid sequence of SEQ ID NO: 84. In some embodiments, the CAR comprises an amino acid sequence of SEQ ID NO: 27. In some embodiments, some embodiments, some embodiments, the CAR comprises the CAR comprises the CAR comprises the CAR comprises a sequence of a sequence of a sequence of a sequence of amino acids of the amino acid of the amino acid of the amino acid of the SEQ ID NO: 28. In SEQ ID NO: 29. In SEQ ID NO: 30. In SEQ ID NO: 31. In some embodiments, the CAR comprises an amino acid sequence of SEQ ID NO: 32. In some embodiments, the CAR comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99%, sequence identity to SEQ ID NO: 86. In some embodiments, the CAR comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 85. In some embodiments, the CAR comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 83. In some embodiments, the CAR comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 75%, at least 80%, at least 85%, at least 90% %, at least 91%, at least %, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least %, or at least 99%, sequence identity with SEQ ID NO: 84. In some embodiments, the CAR comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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% or at least 99% sequence identity to SEQ ID NO: 27. In some embodiments, the CAR comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99% sequence identity to SEQ ID NO: 28. In some embodiments, the CAR comprises an amino acid sequence having at least 50%, at least 55%, at least 60%, at least %, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 98%, or at least 99%, sequence identity to SEQ ID NO: 29. In In some embodiments, the CAR comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, 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%, or at least 99 %, sequence identity to SEQ ID NO: 30. In some embodiments, the CAR comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least % , at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least %, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least %, or at least 99% sequence identity to SEQ ID NO: 31. In some embodiments, the CAR comprises an amino acid sequence that is at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, sequence identity with the SEQ ID NO: 32. In one aspect, the present disclosure provides isolated immunoresponsive cells comprising the CARs described herein. In some embodiments, the isolated immunoresponsive cell is transduced with the CAR, eg, CAR is constitutively expressed on the surface of the immunoresponsive cell. In certain embodiments, the isolated immunoresponsive cell is further transduced with at least one costimulatory ligand such that the immunoresponsive cell expresses the at least one costimulatory ligand. In certain embodiments, the at least one costimulatory ligand is selected from the group consisting of 4-1BBL, CD48, CD70, CD80, CD86, OX40L, TNFRSF14, and combinations thereof. In certain embodiments, the isolated immunoresponsive cell is further transduced with at least one cytokine, such that the immunoresponsive cell secretes the at least one cytokine. In certain embodiments, the at least one cytokine is selected from the group consisting of IL-2, IL-3, IL-6, IL-7, IL-11, IL-12, IL-15, IL-17, IL-21 , and combinations of these. In some embodiment, the isolated immunosensitive cell is selected from the group consisting of a T lymphocyte (T cell), a natural killer (NK) cell, a cytotoxic T lymphocyte (CTL) , MA / t / ZUZI / U / 4400 a regulatory T cell, a human embryonic stem cell, a lymphoid progenitor cell, a T cell precursor cell, and a pluripotent stem cell from which lymphoid cells can differentiate. The nucleic acid sequence of the invention encoding a CAR can be introduced into a cell by transfection, transformation, or transduction. Transfection, transformation, or transduction, as used herein, refers to the introduction of one or more foreign polynucleotides into a host cell using physical or chemical methods. Many transfection techniques are known in the art and include, for example, calcium phosphate DNA coprecipitation (see, eg, Murray EJ. (ed.), Methods in Molecular Biology, Vol. 7, Gene Transfer and Expression Protocols, Humana Press (1991)); DEAEdextran; electroporation; cationic liposome-mediated transfection; microparticle bombardment facilitated by tungsten particles (Johnston, Nature, 346: 776-777 (1990)); and strontium phosphate DNA coprecipitation (Brash et al., Mol. Cell Biol., 7:2031-2034 (1987)). Phage or viral vectors can be introduced into host cells, after growth of infectious particles in suitable packaging cells, many of which are commercially available. In one embodiment, the described CAR T cells can be generated by introducing a lentiviral vector comprising a desired CAR, eg, a CAR comprising anti-GPRC5D, CD8a hinge and transmembrane domains, and 4- signaling domains. 1BB and human CD3-zeta, in cells. The CAR T cells of the invention are capable of replicating in vivo, resulting in long-term persistence that can lead to sustained tumor control. Embodiments of the invention further provide host cells comprising any one of the recombinant expression vectors described herein. As used herein, the term "host cell" refers to any type of cell that can contain the recombinant expression vector. The host cell may be a eukaryotic cell, e.g. eg, plant, animal, or algae, fungi, or may be a prokaryotic cell, e.g. eg, bacteria or protozoa. The host cell can be a cultured cell or a primary cell, ie isolated directly from an organism, e.g. eg, a human being. The host cell can be an adherent cell or a suspended cell, ie, a cell that grows in suspension. Suitable host cells are known in the art and include, for example, E. coii DH577 cells, Chinese hamster ovary cells, monkey VERO cells, COS cells, HEK293 cells, and the like. For the purposes of amplifying or replicating the recombinant expression vector, the host cell may be a prokaryotic cell, e.g. eg, a DH5o cell. For the purposes of producing a recombinant CAR, polypeptide or protein, the host cell may be a mammalian cell. The host cell may be a / U / 4430 human cell. Although the host cell can be of any cell type, can originate from any type of tissue, and can be of any stage of development, the host cell can be a peripheral blood lymphocyte (PBL). ). The host cell may be a T cell. For purposes of the present description, the T cell can be any T cell, such as a cultured T cell, e.g. eg, a primary T cell, or a T cell from a cultured T cell line, e.g. eg, Jurkat, SupTl, etc., or a T cell obtained from a mammal. If obtained from a mammal, the T cell can be obtained from numerous sources, including but not limited to bone marrow, blood, lymph node, the thymus, or other tissues or fluids. T cells can also be enriched or purified. The T cell may be a human T cell. The T cell may be a T cell isolated from a human. The T cell can be any type of T cell and can be of any stage of development, including but not limited to CD4+ / CD8+ double positive T cells, CD8+ double T cells (eg, cytotoxic T cells), CD4+ cooperative T, e.g. eg, Thi and Th2 cells, peripheral blood mononuclear cells (PBMC), peripheral blood leukocytes (PBL), tumor-infiltrating cells, memory T cells, naive T cells, and the like. The T cell may be a CD8+ T cell or a CD4+ T cell. Also included are NKT cells, which refers to a specialized population of T cells that express a semi-invariant αβ T cell receptor, but also express a variety of molecular markers that are typically associated with NK cells, such as NK1.1. NKT cells include NK1.1+ and NK1.1- cells, as well as CD4+, CD4-, CD8+, and CD8- cells. The TCR on NKT cells is unique in that it recognizes glycolipid antigens presented by the MHC I CD Id-like molecule. NKT cells can have protective or deleterious effects due to their abilities to produce cytokines that promote inflammation or immune tolerance . Also included are gamma-delta T cells (γδ T cells), which refer to a specialized population as a small subset of T cells that possess a distinct TCR on their surface, and unlike most T cells in which the TCR is composed of two glycoprotein chains called the TCR-α and TCR-β chains, the TCR in γδ T cells is composed of a γ chain and a δ chain. γδ T cells may play a role in immunosurveillance and immunoregulation, and were found to be an important source of IL-17 and induce a robust CD8+ cytotoxic T cell response. Also included are regulatory T cells or Tregs which refers to T cells that suppress an abnormal or excessive immune response and play a role in immune tolerance. Treg cells are typically Foxp3 transcription factor positive CD4+ T cells and may also include Foxp3 transcription factor negative regulatory T cells which are CD4+ T cells that produce IL-10. ΜΛ / t / ZUZ I / U / 4400 T cell lines are available from e.g. The American Collection of Type Cultures (ATCC, Manassas, VA), and the German Collection of Microorganisms and Cell Cultures (DSMZ) and include, for example, Jurkat cells (ATCC TIB-152), Sup-TI cells (ATCC CRL-1942), RPMI 8402 cells (DSMZ ACC-290), Karpas 45 cells (DSMZ ACC-545), and derivatives thereof. In another embodiment, the host cell is a natural killer (NK) cell. NK cells are a type of cytotoxic lymphocyte that play a role in the innate immune system. NK cells are defined as large granular lymphocytes and are the third cell type differentiated from the common lymphoid progenitor that also gives rise to B and T lymphocytes (see, eg, Immunobiology, 5th ed., Janeway et al., eds. ., Garland Publishing, New York, NY (2001)). NK cells differentiate and mature in the bone marrow, lymph node, spleen, tonsils, and thymus. After maturation, NK cells enter the circulation as large lymphocytes with distinctive cytotoxic granules. NK cells are capable of recognizing and killing some abnormal cells, such as, for example, some tumor cells and virus-infected cells, and are believed to be important in the innate immune defense against intracellular pathogens. As described above with respect to T cells, the NK cell can be any NK cell, such as a cultured NK cell, e.g. eg, a primary NK cell, or an NK cell from a cultured NK cell line, or an NK cell obtained from a mammal. If obtained from a mammal, the NK cell can be obtained from numerous sources, including but not limited to blood, bone marrow, lymph node, the thymus, or other tissues or fluids. NK cells can also be enriched or purified. The NK cell is preferably a human NK cell (eg, isolated from a human). NK cell lines are available from, e.g. eg, the American Collection of Type Cultures (ATCC, Manassas, VA) and include, for example, NK-92 cells (ATCC CRL-2407), NK92MI cells (ATCC CRL-2408), and derivatives thereof. Also provided is a cell population comprising at least one host cell described herein. The cell population may be a heterogeneous population comprising the host cell comprising any one of the recombinant expression vectors described, plus at least one other cell, e.g. eg, a host cell (eg, a T cell), not comprising any of the recombinant expression vectors, or a cell other than a T cell, e.g. eg, a B cell, a macrophage, an erythrocyte, a neutrophil, a hepatocyte, an endothelial cell, an epithelial cell, a muscle cell, a brain cell, etc. Alternatively, the cell population may be a substantially homogeneous population, wherein the population primarily comprises (eg, consisting essentially of) host cells comprising the recombinant expression vector. The population may also be a clonal population of cells, in which all cells in the population are clones of a single host cell comprising a vector of cells. IVIA / t / ZUZI / U / 4400 recombinant expression, such that all cells in the population comprise the recombinant expression vector. In one embodiment, the cell population is a clonal population comprising host cells comprising a recombinant expression vector as described herein. Pharmaceutical Compositions / Administration In embodiments of the present disclosure, CAR-expressing cells may be provided in compositions, e.g. eg, suitable pharmaceutical composition(s) comprising the cells expressing CAR and a pharmaceutically acceptable carrier. In one aspect, the present disclosure provides pharmaceutical compositions comprising an effective amount of a lymphocyte expressing one or more of the described CARs and a pharmaceutically acceptable excipient. The pharmaceutical compositions of the present disclosure may comprise a CAR-expressing cell, e.g. eg, a plurality of CAR-expressing cells, as described herein, in combination with one or more pharmaceutically or physiologically acceptable carriers, excipients or diluents. A pharmaceutically acceptable carrier can be an ingredient in a pharmaceutical composition, other than an active ingredient, that is non-toxic to a subject. A pharmaceutically acceptable carrier can include, but is not limited to, a regulator, excipient, stabilizer, or preservative. Examples of pharmaceutically acceptable carriers are solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption retarding agents, and the like that are physiologically compatible, such as salts, buffers, antioxidants, saccharides, aqueous carriers or not. aqueous agents, preservatives, wetting agents, surfactants or emulsifying agents, or combinations of these. The amounts of pharmaceutically acceptable carrier(s) in pharmaceutical compositions can be determined experimentally based on the activities of the carrier(s) and desired characteristics of the formulation, such as stability and / or minimal oxidation. Such compositions may comprise buffers such as acetic acid, citric acid, formic acid, succinic acid, phosphoric acid, carbonic acid, malic acid, aspartic acid, histidine, boric acid, Tris buffers, HEPPSO, HEPES, neutral buffered saline, saline. phosphate buffered and the like; carbohydrates such as glucose, mannose, sucrose or dextrans, mannitol; proteins; polypeptides or amino acids such as glycine; antioxidants; chelating agents, such as EDTA or glutathione; adjuvants (eg, aluminum hydroxide); antibacterial and antifungal agents; and preservatives. The compositions of the present disclosure can be formulated for a variety of means of parenteral or non-parenteral administration. In one embodiment, the compositions can be formulated for intravenous administration or infusion. The compositions described herein can be provided, for example, as preparations MA / t / ZUZI / U / 4400 sterile liquids, p. eg, isotonic aqueous solutions, emulsions, suspensions, dispersions, or viscous compositions, which can be adjusted to a desired pH. Formulations suitable for oral administration may include suitable liquid solutions, capsules, sachets, tablets, lozenges and dragees, powder-in-liquid suspensions and emulsions. The term pharmaceutically acceptable, as used herein with respect to pharmaceutical compositions, means approved by a federal or state government regulatory agency or listed in the US Pharmacopeia or other generally recognized pharmacopeia for use in animals and / or in humans. In one aspect, the disclosure relates to the administration of a genetically modified T cell expressing a CAR for the treatment of a subject having cancer or at risk of having cancer using lymphocyte infusion. In at least one embodiment, infusion of autologous lymphocytes is used in the treatment. Autologous PBMCs are harvested from a subject in need of treatment and the T cells are activated and expanded using methods described herein and known in the art and then reinfused into the subject. In one aspect, the disclosure relates generally to treatment of a subject at risk of developing cancer. The invention also includes treating a malignancy or an autoimmune disease in which chemotherapy and / or immunotherapy in a subject results in significant immunosuppression, thereby increasing the subject's risk of developing cancer. In one aspect, the present disclosure provides methods of preventing cancer, the methods comprising administering a quantity of a lymphocyte expressing one or more of the described CARs to a subject in need thereof. In one aspect, the present disclosure provides methods of treating a subject having cancer, the methods comprising administering a therapeutically effective amount of a lymphocyte expressing one or more of the described CARs to a subject in need thereof, whereby the lymphocyte induces or modulates the destruction of cancer cells in the subject. In another aspect, the present disclosure provides methods of reducing tumor burden in a subject having cancer, the methods comprising administering a therapeutically effective amount of a lymphocyte expressing one or more of the CARs described herein to a subject having needs it, whereby the lymphocyte induces the destruction of cancer cells in the subject. In another aspect, the present disclosure provides methods for increasing the survival of a subject having cancer, the methods comprising administering a therapeutically effective amount of a lymphocyte expressing one or more of the described CARs to a subject in need thereof, by which lengthens the survival of the subject. Generally, the lymphocytes expressing the CAR(s) induce the destruction of cancer cells in the subject and result in the reduction or eradication of tumors / cancer cells in the subject. not a list MA / t / ZUZI / U / 4400 limiting cancers, including metastatic lesions, that can be targeted, includes lung cancer, gastric cancer, colon cancer, hepatocellular carcinoma, renal cell carcinoma, bladder urothelial carcinoma, metastatic melanoma, cancer breast, ovarian cancer, cervical cancer, head and neck cancer, pancreatic cancer, glioma, glioblastoma, non-Hodgkin lymphoma (NHL), acute lymphocytic leukemia (ALL), chronic lymphocytic leukemia (CLL), chronic myelogenous leukemia (CML) , smoldering multiple myeloma (SMM), multiple myeloma (MM), acute myeloid leukemia (AML), and combinations thereof. In one embodiment, the cancer being treated in a subject is multiple myeloma. In one aspect, the methods described herein are applicable to the treatment of non-cancerous conditions that are at risk of developing into a cancerous condition, such as, e.g. eg, monoclonal gammopathy of uncertain significance (MGUS), which is at risk of developing in a blood cancer, such as MM or lymphoma, and myelodysplastic syndrome, which is at risk of developing in a cancer of the blood. blood, such as leukemia. In one aspect, methods of treating a subject having cancer are provided comprising administering a therapeutically effective amount of a lymphocyte expressing a CAR, the CAR having an extracellular antigen-binding domain that binds the GPRC5D antigen, to a subject in need, whereby the lymphocyte induces the destruction of cancer cells in the subject. In some embodiments, the at least one of the CARs comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 86, 85, 83, 84, 27, 28, 29, 30, 31, and 32. In one aspect, a method for targeted killing of a cancer cell is disclosed, the method comprising contacting the cancer cell with a lymphocyte expressing one or more of the described CARs, whereby the lymphocyte induces killing of the cell. cancerous. A non-limiting list of cancer cells, including metastatic cancer cells, that may be targeted include a lung cancer cell, a gastric cancer cell, a colon cancer cell, a hepatocellular carcinoma cell, a cell carcinoma cell, cells, one bladder urothelial carcinoma cell, one metastatic melanoma cell, one breast cancer cell, one ovarian cancer cell, one cervical cancer cell, one head and neck cancer cell, one pancreatic cancer cell , a glioma cell, a glioblastoma cell, and a non-Hodgkin lymphoma (NHL) cell, an acute lymphocytic leukemia (ALL) cell, a chronic lymphocytic leukemia (CLL) cell, a chronic myelogenous leukemia (CML) cell ), a smoldering multiple myeloma (SMM) cell, a multiple myeloma (MM) cell, an acute myeloid leukemia (AML) cell, and combinations thereof. In one embodiment, the cancer cell is a multiple myeloma cell. IVIA / t / ZUZ I / U / 4430 The pharmaceutical compositions of the present disclosure can be administered in a manner suitable for the disease to be treated (or prevented). The amount and frequency of administration will be determined by such factors as the condition of the subject, and the type and severity of the subject's disease, although suitable dosages can be determined by clinical trials. The terms "treat" or "treatment" refer to therapeutic treatment where the goal is to slow (lessen) an unwanted physiological change or disease, or to provide a beneficial or desired clinical outcome during treatment. Beneficial or desired clinical outcomes include relief of symptoms, reduction in the extent of the disease, steady state (i.e., not worsening) of the disease, slowing or delaying the progression of the disease, improvement or relief of the state of the disease, and / or remission (partial or total), whether detectable or not. Treatment may also mean prolonging survival compared to expected survival, if the subject does not receive treatment. Those in need of treatment include those subjects who already have the disease or the unwanted physiological change as well as those subjects prone to have the disease or the physiological change. A therapeutically effective amount or effective amount, used interchangeably herein, refers to an effective amount, at the dose and for periods of time necessary, to achieve a desired therapeutic result. A therapeutically effective amount may vary according to factors such as the disease state, age, sex, weight of the individual, and the ability of a therapeutic agent or combination of therapeutic agents to induce a desired response in the individual. . Illustrative indicators of an effective therapy or combination of therapies including, for example, increased patient well-being, reduced tumor burden, delayed arrest or shrinkage of a tumor, and / or the absence of cancer cell metastasis to other locations in the body. As used herein, the term "subject" refers to an animal. The terms subject and patient may be used interchangeably in the present description with reference to a subject. As such, a subject includes a human being being treated for a disease, or prevention of a disease, such as a patient. The methods described in the present description can be used to treat an animal belonging to any classification. Examples of such animals include mammals. Mammals include, but are not limited to, mammals of the order Rodentia, such as mice and hamsters, and mammals of the order Logomorpha, such as rabbits. Mammals can be of the order Carnivora, which includes felines (cats) and canines (dogs). Mammals can be from the order Artiodactyla, which includes bovines (cows) and porcine (pigs), or from the order Perssodactyla, which includes equines (horses). Mammals can be of the order Primates, Ceboides, or Simoids. IVIA / I / U / 4400 (monkeys) or the order Anthropoides (humans and apes). In one embodiment, the mammal is a human. When a therapeutically effective amount is indicated, the precise amount of the compositions of the present disclosure to be administered can be determined by a physician considering individual differences in age, weight, tumor size, degree of infection or metastasis, and condition of the subject. . Generally, it can be said that a pharmaceutical composition comprising the T cells described in the present disclosure can be administered at a dosage of about 104 to about 1010 cells / kg of body weight, in some cases, from about 105 to about 106 cells / kg of body weight, which includes all integer values ​​within those ranges. In some embodiments, a pharmaceutical composition comprising the T cells described herein can be administered at a dosage of approximately 10 6 cells / kg of body weight. The T cell compositions can also be administered multiple times at these dosages. The cells can be administered using infusion techniques that are commonly known in immunotherapy (see, eg, Rosenberg et al., New Eng. J. OfMed. 319:1676, 1988). Delivery systems useful in the context of embodiments of the invention may include extended-release, delayed-release, and sustained-release delivery systems, such that delivery of the T-cell compositions occurs sooner, and in sufficient time. to provoke, the sensitization of the site to be treated. The composition can be used in conjunction with other therapeutic agents or therapies. Such systems may avoid repeated administrations of the composition, thereby increasing convenience for the subject and the physician, and may be particularly suitable for certain embodiments of the composition of the invention. Many types of delivery delivery systems are available and are known to those skilled in the art. These include polymer-based systems such as poly(lactidaglycolide), copolyoxalates, polyesteramides, polyorthoesters, polycaprolactones, polyhydroxybutyric acid, and polyanhydrides. Microcapsules of the above drug-containing polymers are described, for example, in US Pat. 5,075,109. Delivery systems also include non-polymeric systems that are lipids including sterols, such as cholesterol, cholesterol esters, and fatty acids or neutral fats, such as mono-, di-, and triglycerides; silastic systems; peptide-based systems; hydrogel delivery systems; wax coatings; compressed tablets using conventional binders and excipients; partially fused implants; and the like. Specific examples include, but are not limited to: (a) erosional systems in which the active composition is contained in a form within a matrix, such as those described in US Pat. 4,452,775; 4,667,014; 4,748,034; and 5,239,660, and (b) systems MA / t / ZUZI / U / 4400 diffusionals in which an active component permeates at a controlled rate from a polymer as described in US Pat. 3,854,480 and 3,832,253. In addition, pump-based hardware delivery systems may be used, some of which are adapted for implantation. In certain aspects, it may be desirable to administer activated T cells to a subject and then draw blood again (or perform apheresis), activate the T cells, in accordance with the present disclosure, and boost the subject with these activated T cells and expanded. This process can be carried out multiple times every few weeks. In certain aspects, T cells can be activated from 10 cc to 400 cc blood draws. In certain aspects, T cells are activated from 20 cc, 30 cc, 40 cc, 50 cc, 60 cc, 70 cc, 80 cc, 90 cc, or 100 cc blood draws. Administration of the CAR-T cells and compositions can be done in any manner, e.g. eg, by parenteral or non-parenteral administration, including aerosol inhalation, injection, infusions, ingestion, transfusion, implantation or transplantation. For example, CAR-T cells and the compositions described herein can be administered to a patient via transarterial, intradermal, subcutaneous, intratumoral, intramedullary, intranasal, intramuscular, intravenous (i.v.) injection, or intraperiphoneal injection. In one aspect, the compositions of the present disclosure are administered by i.v. In one aspect, the compositions of the present disclosure are administered to a subject by intradermal or subcutaneous injection. The T cell compositions can be injected, for example, directly into a tumor, lymph node, tissue, organ, or site of infection. Administration can be autologous or non-autologous. For example, immunoresponsive cells expressing a specific CAR g protein-coupled receptor (eg, GPRC5D) can be obtained from a subject, and administered to the same or a different matched subject. The peripheral blood-derived T cells of the present disclosure, or expanded T cells (eg, derived from in vivo, ex vivo or in vitro) can be administered via, eg. eg, intravenous injection, localized injection, systemic injection, catheter delivery, or parenteral administration. In particular embodiments, subjects may undergo leukapheresis, where leukocytes are collected, enriched or depleted ex vivo to select and / or isolate cells of interest, e.g. eg, T cells. These T cell isolates can be expanded by methods known in the art and treated such that one or more CAR constructs of the present disclosure can be introduced, thereby creating a CAR-T cell. Subjects in need can undergo standard treatment with high-dose chemotherapy followed by peripheral blood stem cell transplantation. In certain respects, after or ΜΛ / t / ZUZ I / U / 4400 Simultaneously with transplantation, subjects receive an infusion of the expanded CAR-T cells. In one aspect, the expanded cells are administered before or after surgery. The dosage administered to a patient having a malignancy is sufficient to alleviate or at least partially arrest the disease being treated (therapeutically effective amount). The dosage of the above treatments to be administered to a subject will vary with the precise nature of the condition being treated and the recipient of the treatment. Dosage scaling for human administration can be done in accordance with generally accepted practices in the art. The CAR T cells of the invention can undergo T cell expansion in vivo and can establish GPRC5D-specific memory cells that persist at high levels for a prolonged amount of time in blood and bone marrow. In some cases, the CAR T cells of the invention infused into a subject can kill cancer cells, e.g. eg, leukemic cells, in vivo in subjects with advanced cancer resistant to chemotherapy. In one embodiment, a CAR of the present disclosure is introduced into T cells, e.g. using in vitro transcription, and the subject (eg, human) receives an initial administration of CAR-T cells of the description, and one or more subsequent administrations of CAR-T cells, wherein the one or more subsequent administrations are administered less than 15 days, e.g. eg, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, or 2 days after the previous administration. In one embodiment, more than one administration of the CAR-T cells is administered to the subject (eg, a human) per week, are administered, e.g. eg, 2, 3 or 4 administrations of CAR-T cells per week. In one embodiment, the subject receives more than one administration of the CAR-T cells per week (eg, 2, 3, or 4 administrations per week) (also referred to herein as a cycle), followed by a week without administrations. of CAR-T cells, and then the subject is administered one or more additional administrations of the CAR-T cells (eg, more than one administration of the CAR-T cells per week). In another embodiment, the subject receives more than one cycle of CAR-T cells, and the time between each cycle is less than 10, 9, 8, 7, 6, 5, 4, or 3 days. In one embodiment, CAR-T cells are administered every other day for 3 administrations per week. In one embodiment, the CAR-T cells are administered for at least two, three, four, five, six, seven, eight, or more weeks. In one embodiment, administration can be repeated after one day, two days, three days, four days, five days, six days, one week, two weeks, three weeks, one month, five weeks, six weeks, seven weeks, two months, three months, four months, five months, six months or more. Repeated treatment courses are also possible, as is chronic administration. Repeated administration can be at the same dose or at a different dose. IVIA / I / U / 4400 CAR-T cells can be administered in the methods of the invention by maintenance therapy, such as e.g. eg, once a week for a period of 6 months or more. In one embodiment, CAR-T cells are generated using lentiviral viral vectors, such as lentiviruses. CAR-T cells generated with such viral vectors will generally have stable expression of CAR. In one embodiment, CAR-T cells transiently express CAR vectors for 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 days post transduction. The transient expression of CARs can be affected by the supply of CAR RNA vector. In one embodiment, the CAR RNA is transduced into the T cell by electroporation. If a patient is at high risk of generating an anti-CAR antibody response during the course of transient CAR therapy (such as those generated by RNA transfusions), breaks in CAR-T infusion should not last more than ten to fourteen days. A CAR-expressing cell described herein can be used in combination with other known agents and therapies. Administered in combination, as used herein, means that two (or more) different treatments are delivered to the subject during the course of the subject's treatment, e.g. eg, the two or more treatments are given after the subject has been diagnosed with the cancer and before the cancer has been cured or eliminated or treatment ceased for other reasons. In some embodiments, delivery of one treatment still occurs when delivery of the second begins, so there is overlap in terms of delivery. This is sometimes referred to in the present description as simultaneous or concurrent delivery. In other embodiments, delivery of one treatment ends before delivery of the other treatment begins. In some case modalities, treatment is more effective due to combined administration. For example, the second treatment is more effective, e.g. For example, an equivalent effect is seen with less of the second treatment, or the second treatment reduces symptoms to a greater extent than would be seen if the second treatment were given in the absence of the first treatment, or the analogous situation is seen with the second treatment. first treatment. In some modalities, delivery is such that the reduction in one symptom, or other disorder-related parameter is greater than would be observed with one treatment delivered in the absence of the other. The effect of the two treatments can be partially additive, fully additive, or more than additive. The delivery may be such that an effect of the first treatment delivered is still detectable when the second is delivered. In one embodiment, other therapeutic agents, such as factors, can be administered before, after, or at the same time (simultaneously with) the CAR-T cells, including, but not limited to, interleukins, e.g. IL-2, IL-3, IL 6, IL-7, IL-11, IL-12, IL-15, IL-21, as well as the other interleukins, colony-stimulating factors, such as G-, M- and GM-CSF, and ΜΛ / t / ZUZ I / U / 4400 interferons, e.g. eg, interferon γ. A CAR-expressing cell described herein and the at least one additional therapeutic agent may be administered simultaneously, in the same or separate compositions, or sequentially. For sequential administration, the CAR-expressing cell described herein may be administered first, and the additional agent may be administered second, or the order of administration may be reversed. In additional embodiments, a CAR-expressing cell described herein can be used in a treatment regimen in combination with surgery, radiation, chemotherapy, immunosuppressive agents, such as methotrexate, cyclosporine, azathioprine, mycophenolate, and FK506, antibodies, or others. immunoablative agents, such as anti-CD3 antibodies or other antibody therapies, cytotoxin, fludarabine, cyclosporine, FK506, rapamycin, mycophenolic acid, steroids, FR901228, cytokines, and irradiation. In one embodiment, a CAR-expressing cell described herein can be used in combination with a chemotherapeutic agent. Illustrative chemotherapeutic agents include, but are not limited to, an anthracycline (eg, doxorubicin (eg, liposomal doxorubicin)), a vinca alkaloid (eg, vinblastine, vincristine, vindesine, vinorelbine), an alkylating agent (eg, cyclophosphamide, decarbazine, melphalan, ifosfamide, temozolomide), an immune cell antibody (eg, alemtuzamab, gemtuzumab, rituximab, tositumomab), an antimetabolite (including, eg, folic acid antagonists, pyrimidine analogues, purine analogues, and adenosine deaminase inhibitors (eg, fludarabine)), an mTOR inhibitor, a glucocorticoid-induced TNFR-related protein (GUR) agonist ), a proteasome inhibitor (eg, aclacinomycin A, gliotoxin, or bortezomib), an immunomodulator such as thalidomide, or a thalidomide derivative (eg, lenalidomide). A non-exhaustive list of chemotherapeutic agents considered for use in combination therapies include anastrozole (Arimidex®), bicalutamide (Casodex®), bleomycin sulfate (Blenoxane®), busulfan (Myleran®), leucovorin calcium, melphalan (Alkeran®), 6mercaptopurine (Purinethol®), methotrexate (Folex®), mitoxantrone (Novantrone®), mylotarg, paditaxel (Taxol®), phoenix (Yttr¡um90 / MX-DTPA), pentostatin, polyfeprosan 20 with carmustine implant (Gliadel®), dactinomycin (Actinomycin D, Cosmegan), daunorubicin hydrochloride (Cerubidine®), daunorubicin citrate liposome injection (DaunoXome®), dexamethasone, docetaxel (Taxotere®), doxorubicin hydrochloride (Adriamycin®, Rubex®), etoposide (Vepesid ®), busulfan injection (Busulfex®), capecitabine (Xeloda®), N4-pentoxycarbonyl-5-deox¡-5fluorocytidine, carboplatin (Paraplatin®), carmustine (BiCNU®), chlorambucil (Leukeran®), cisplatin (Platinol® ), cladribine (Leustatin®), cyclophosphamide (Cytoxan® or Neosar®), cytarabine, cytosine arabinoside (Cytosar-U®), cytarabine liposome injection (DepoCyt®), dacarbazine (DTIC-Dome®), MA / t / ZUZI / U / 4400 fludarabine phosphate (Fludara®), 5-fluorouracil (Adrucil®, Efudex®), flutamide (Eulexin®), tezacitibine, gemcitabine (difluorodeoxycytidine), hydroxyurea (Hydrea®), Idarubicin (Idamycin ®), ifosfamide (IFEX®), irinotecan (Camptosar®), L-asparaginase (ELSPAR®), tamoxifen citrate (Nolvadex®), teniposide (Vumon®), 6-thioguanine, thiotepa, tirapazamine (Tirazone®), hydrochloride topotecan for injection (Hycamptin®), vinblastine (Velban®), vincristine (Oncovin®), and vinorelbine (Navelbine®). Illustrative alkylating agents include, but are not limited to, nitrogen mustards, ethyleneimine derivatives, alkyl sulfonates, nitrosoureas, and triazenes: uracil mustard (Aminouracil Mustard®, Chlorethaminacil®, Haemanthamine®, Nordopan®, Uracil Nitrogen Mustard®, Uracillost®, Uracilmostard® ®, Uramustin®, Uramustine®), chlormethine (Mustargen®), cyclophosphamide, (Cytoxan®, Neosar®, Clafen®, Endoxan®, Procytox®, Revimmune™), ifosfamide (Mitoxana®), melphalan (Alkeran®), chlorambucil (Leukeran®), pipobromane (Amedel®, Vercyte®), triethylenemelamine (Hemel®, Hexalen®, Hexastat®), Demethyldopan®, Desmethyldopan®, triethylenethiophosphoramine, temozolomide (Temodar®), thiotepa (Thioplex®), busulfan (Busilvex® , Myleran®), carmustine (BiCNU®), lomustine (CeeNU®), streptozocin (Zanosar®), and dacarbazine (DTIC-Dome®). Illustrative additional alkylating agents include, without limitation, oxaliplatin (Eloxatin®); Melphalan (also known as L-PAM, L-sarcolysine, and phenylalanine mustard, Alkeran®); altretamine (also known as hexamethylmelamine (HMM), Hexalen®); Carmustine (BiCNU®); Bendamustine (Treanda®); Busulfan (Busulfex® and Myleran®); Carboplatin (Paraplatin®); Temozolomide (Temodar® and Temodal®); Dactinomycin (also known as actinomycin-D, Cosmegen®); Lomustine (also known as CCNU, CeeNU®); Cisplatin (also known as CDDP, Platinol®, and Platinol®-AQ); Chlorambucil (Leukeran®); Cyclophosphamide (Cytoxan® and Neosar®); Dacarbazine (also known as DTIC, DIC and Imidazole Carboxamide, DTIC-Dome®); altretamine (also known as hexamethylmelamine (HMM), Hexalen®); Ifosfamide (Ifex®); Prednumustine; Procarbazine (Matulane®); Mechlorethamine (also known as Nitrogen Mustard, Mostine, and Mechlorethamine Hydrochloride, Mustargen®); Streptozocin (Zanosar®); Thiotepa (also known as thiophosphoamide, TESPA and TSPA, Thioplex®); Cyclophosphamide (Endoxan®, Cytoxan®, Neosar®, Procytox®, Revimmune®); and Bendamustine HCI (Treanda®). Examples of immunomodulators useful in the present disclosure include, but are not limited to, e.g. eg, afutuzumab (available from he®); pegfilgrastim (Neulasta®); lenalidomide (CC-5013, Revlimid®); thalidomide (Thalomid®), actimide (CC4047); and IRX-2 (mixture of human cytokines including interleukin 1, interleukin 2, and interferon y, CAS 951209-71-5, available from IRX Therapeutics). In one embodiment, the subject may be administered an agent that enhances the activity of a CAR-expressing cell. For example, in one embodiment, the agent can be an agent that inhibits an inhibitory molecule. Inhibitory molecules, e.g. eg, scheduled death 1 MA / t / ZUZI / U / 4400 (PD1), may, in some embodiments, decrease the ability of a CAR-expressing cell to mount an effector immune response. Examples of inhibitory molecules include PD1, PD-L1, CTLA4, TIM3, LAG3, VISTA, BTLA, TIGIT, LAIR1, CD160, 2B4, and TGFR beta. The following is a description of illustrative embodiments. Embodiment 1. A chimeric antigen receptor (CAR), comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 66, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 67, and a heavy chain CDR3 heavy having the amino acid sequence of SEQ ID NO: 68; a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 58, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and a heavy chain CDR3 heavy having the amino acid sequence of SEQ ID NO: 60; a heavy chain complementarity determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 39, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40, and a heavy chain CDR3 heavy weight having the amino acid sequence of SEQ ID NO: 41; a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 43, and a heavy chain CDR3 having the amino acid sequence from SEQ ID NO: 44; or a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 45, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and a heavy chain CDR3 having the sequence of amino acids of SEQ ID NO: 47; wherein the extracellular antigen-binding domain binds antigen from anti-G protein receptor family C group 5 member D (GPRC5D). Mode 2. The CAR of mode 1, wherein the extracellular antigen-binding domain comprises the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 66, the heavy chain CDR2 having the sequence of amino acids of SEQ ID NO: 67, and the heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 68, and MA / t / ZUZI / U / 4400 further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 69, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 70, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 71; the extracellular antigen-binding domain comprising the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 58, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and CDR3 heavy chain having the amino acid sequence of SEQ ID NO: 60, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 61, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 62, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 63; the extracellular antigen-binding domain comprising the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 39, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40, and CDR3 heavy chain having the amino acid sequence of SEQ ID NO: 41, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 48, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 49, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 50; the extracellular antigen-binding domain comprising the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 43, and CDR3 heavy chain having the amino acid sequence of SEQ ID NO: 44, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 51, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 52, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 53; or the extracellular antigen-binding domain comprising the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 45, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and the Heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 47, and further comprising a light chain CDR1 having the amino acid sequence of SEQ ID NO: 54, a light chain CDR2 having the sequence of amino acids of SEQ ID NO: 55, and a light chain CDR3 having the amino acid sequence / U / 4430 of SEQ ID NO: 56. Mode 3. The CAR of mode 1 or 2, wherein the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 73, 65, 1, 3, and 5, or a heavy chain variable region (HCVR) comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 72, 64, 2, 4, and 6, or a combination of a LCVR comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 73, 65, 1, 3 and 5, and an HCVR comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 72, 64, 2, 4 and 6. Mode 4. The CAR of modes 1-3, wherein the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 73 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 72; a light chain variable region comprising an amino acid sequence of SEQ ID NO: 65 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 64; a light chain variable region comprising an amino acid sequence of SEQ ID NO: 1 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 2; a light chain variable region comprising an amino acid sequence of SEQ ID NO: 3 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 4; or a light chain variable region comprising an amino acid sequence of SEQ ID NO: 5 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 6. Mode 5. The CAR of any of modes 1-4, wherein the extracellular antigen binding domain comprises a single chain variable fragment (scFv). Mode 6. The CAR of mode 5, wherein the scFv comprises a polypeptide linker between the light chain variable region and the heavy chain variable region. Embodiment 7. The CAR of claim 6, wherein the linker polypeptide comprises an amino acid sequence of SEQ ID NO: 7. Mode 8. The CAR of any of modes 5-7, wherein the scFv comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 78, 77, 75, 76, 8, 9, 10, 24, 25 and 26. IVIA / I / U / 4400 Mode 9. The CAR of any of modes 1-8, wherein the extracellular antigen-binding domain comprises a signal polypeptide. Embodiment 10. The CAR of claim 9, wherein the signal polypeptide comprises an amino acid sequence of SEQ ID NO: 11. Mode 11. The CAR of any of modes 1-10, wherein the intracellular signaling domain comprises a polypeptide component selected from the group consisting of a component of TNF receptor superfamily member 9 (CD137), a component of the CD3 zeta chain (CD3z) of the T cell surface glycoprotein, a cluster of the differentiation component (CD27), a cluster of the differentiation superfamily member component, and a combination of these. Mode 12. The CAR of mode 11, wherein the CD137 component comprises an amino acid sequence of SEQ ID NO: 12. Mode 13. The CAR of mode 11, wherein the Cd3z component comprises an amino acid sequence of SEQ ID NO: 13. Mode 14. The CAR of mode 11, wherein the intracellular signaling domain comprises an amino acid sequence of SEQ ID NO: 14. Embodiment 15. The CAR of any of Embodiments 1-14, wherein the transmembrane domain comprises a CD8a transmembrane region (CD8a-TM) polypeptide. Mode 16. The CAR of mode 15, wherein the CD8a-TM polypeptide comprises an amino acid sequence of SEQ ID NO: 15. Mode 17. The CAR of any of modes 1-16, further comprising a hinge region connecting the transmembrane domain to the extracellular antigen-binding domain. Mode 18. The CAR of mode 17, wherein the hinge region is a CD8a hinge region. Mode 19. The CAR of mode 18, wherein the Cd8a hinge region comprises an amino acid sequence of SEQ ID NO: 16. Mode 20. The CAR of any of modes 1-19, wherein the extracellular antigen-binding domain comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 82, 81, 80, 79, 17, 18 , 19, 20, 21, and 22. Mode 21. The CAR of any of modes 1-20, wherein the CAR comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 86, 85, 83, 84, 27, 28, 29, 30, 31 and 32. Mode 22. An isolated lymphocyte expressing the CAR of any of modes 1-21. ΜΛ / t / ZUZ I / U / 4400 Mode 23. The isolated lymphocyte of mode 22, wherein the lymphocyte is a T lymphocyte. Mode 24. An isolated nucleic acid molecule encoding the CAR of any of Modes 1-21. Embodiment 25. The isolated nucleic acid molecule of Embodiment 24, wherein the nucleic acid molecule comprises a nucleotide acid sequence selected from the group consisting of SEQ ID NO: 90, 89, 87, 88, 33, 34, 35, 36, 37 and 38. Embodiment 26. The isolated nucleic acid molecule of Embodiment 24, wherein the nucleic acid molecule comprises a nucleotide sequence that is at least about 80%, 81%, 82%, 83%, 84%, 85%, 86 %, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% identical to a nucleotide sequence of SEQ IDs NO: 90, 89, 87, 88, 33, 34, 35, 36, 37 and 38. Embodiment 27. A vector comprising the nucleic acid molecule of any of Embodiments 24-26. Mode 28. A cell expressing the nucleic acid molecule of any of modes 24-26. Embodiment 29. A pharmaceutical composition, comprising an effective amount of the lymphocyte of any of Embodiments 22-23. Embodiment 30. A pharmaceutical composition, comprising an effective amount of the lymphocyte of any of Embodiments 22-23 and a pharmaceutically acceptable excipient. Modality 31. The CAR of any of modalities 1-21 or the pharmaceutical composition of modality 29 or 30 for use in therapy. Embodiment 32. The CAR of any of the Embodiments 1-21 or the pharmaceutical composition of Embodiment 29 or 30 for use in a method of treating a subject having cancer. Modality 33. A method of treating a subject having cancer; The method comprises: administering a therapeutically effective amount of the lymphocyte of any of the modalities 22-23 to a subject in need thereof, whereby the lymphocyte induces the destruction of cancer cells in the subject. Modality 34. The method of modality 33, or the CAR or pharmaceutical composition for use in a method of modality 32, wherein the cancer is selected from the group consisting of lung cancer, gastric cancer, breast cancer, colon, hepatocellular carcinoma, renal cell carcinoma, bladder urothelial carcinoma, metastatic melanoma, breast cancer, ovarian cancer, cervical cancer, head and neck cancer, pancreatic cancer, glioma , a glioblastoma, and a non-Hodgkin lymphoma (NHL), an acute lymphocytic leukemia IVIA / t / ZUZI / U / 4400 (ALL), chronic lymphocytic leukemia (CLL), chronic myelogenous leukemia (CML), smoldering multiple myeloma (SMM), multiple myeloma (MM), acute myeloid leukemia (AML) ), and combinations of these. Mode 35. The method of mode 33 or 34, or the CAR or pharmaceutical composition for use in a method of mode 32 or 34, where the cancer is multiple myeloma. Mode 36. A method of targeted destruction of a cancer cell, the method comprising: contacting the cancer cell with the lymphocyte in any of the modalities 22-23, whereby the lymphocyte induces the destruction of the cancer cell. Mode 37. The method of mode 36, wherein the cancer cell is selected from the group consisting of lung cancer, gastric cancer, colon cancer, hepatocellular carcinoma, renal cell carcinoma, urothelial carcinoma of bladder, metastatic melanoma, breast cancer, ovarian cancer, cervical cancer, head and neck cancer, pancreatic cancer, glioma, glioblastoma, and other solid tumors, and non-Hodgkin lymphoma (NHL ), acute lymphocytic leukemia (ALL), chronic lymphocytic leukemia (CLL), chronic myelogenous leukemia (CML), smoldering multiple myeloma (SMM), multiple myeloma (MM), acute myeloid leukemia (AML), and other liquid tumors, and combinations of these. Mode 38. The method of mode 36 or 37, wherein the cancer cell is a multiple myeloma cell. Mode 39. A method of detecting the presence of cancer in a subject, comprising: (a) contacting a cell sample obtained from the subject with the CAR of claim 1, thereby forming a CAR cell complex, and (b) detecting the complex, wherein detection of the complex is indicative of the presence of cancer in the subject. Preferably, the modality is performed in vitro. examples The following examples are provided to better describe some of the embodiments described in the present description. The examples are intended to illustrate, and not limit, the embodiments described. MA / t / ZUZI / U / 4400 Example 1 - Expression of a-GPRC5D scFv CARs Primary human pan T cells were electroporated with either no mRNA (mock) or with 10 pg of mRNA expressing an isotypic control CAR or O-GPRC5D scFv CAR. 24 hours after electroporation, surface CAR expression was measured by flow cytometry after staining with biotinylated protein L and streptavidin-conjugated PE. (Figure 1). Percent CAR expression was determined by protein L staining. Expression was determined to be 95, 88, 70, and 67% positive for CAR A, CAR B, CAR C, and isotypic CAR, respectively. Mock T cells were only electroporated, but no mRNA was added to the cells. Mock T cells did not express any CAR structure, as expected. These data indicated that the T cells expressed the CAR structure to a high degree. The open histogram is simulated, the gray filled histogram is the CAR-T population. The amino acid sequences for the components of the GPRC5D-targeted CAR constructs were as shown in Table 2. Table 2 MA / t / ZUZI / U / 4400 Domain Sequence Signal sequence MAWVWTLFLMAAAQSIQA (SEQ ID NO: 11) GPRC5D-specific extracellular scFv EIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGS GSGTDFTLTISSLEPEDFAVYYCQQRSNWPLTFGQGTKVEIKGTEGK SSGSGSESKSTEVQLVQ SGAEVKKPGESLKISCKGSGYSFTSYFIGWVRQMPGKGLEWMGIIYPGKSDTRYSPSFQGQVTI SADKSISTAYLQWSSLKASDTAMYYCARVYSFGGRHKALFDYWGQGTLVTVSS (SEQ ID NO: 8) DIQMTQSPSSLSASVGDRVT1TCRASQSISSYLN WYQQKPGKAPKLLIYAASSLQSGVPSRFSGS GSGTDFTLTISSLQPEDFATYYCQQSYSTPLTFGQGTKVEIKGTEGKSSGSGSGSESKSTQVQLVQS GAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTANYAQKFQGRVTIT ADESTSTAYME LSSLRSEDTAVYYCARESRWRGYKLDYWGQGTLVTVSS (SEQ ID NO: 9) DIQMTQSPSSLSASVGDRVTITCKASQNVATHVGWYQQKPGKAPKRLIYSASYRYSGVPSRFSG SGSGTEFTLTISNLQPEDFATYYCQQYNRYPYTFGQGTKLEIKGTEGKSSGSGSSESK STQVQLV QSGAEVKKPGASVKVSCKASGYSFTGYTMNWVRQAPGQGLEWMGLINPYNSDTNYAQKLQGR VTMTTD1S1 b 1AYMELRSLRSDDTAVYYCARVALRVALDYWGQGTLVTVSS (SEQ ID NO: 10) EVQLVQSGAEVKKPGESLKISCKGSGYSFTSYFIGWVRQMPGKGLEWMGIIYPGKSDTRYSPSF QGQVTISADKSISTAYLQWSSLKASDTAMYYCARVYSFGGRHKALFDYWGQGTLVTVSSGTEG KSSGSGSESKSTEIVLTQSPATLSSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASN RATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPLTFGQGTKVEIK (SEQ ID NO: 24) QVQLVQSGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLE WMGGIIPIFGTANYAQK FQGRVTrTADESTSTAYMELSSLRSEDTAVYYCARESRWRGYKLDYWGQGTLVTVSSGTEGKS SGSGSESKSTDIQMTQSPSSLSASVGDRVTFrCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQ SGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQS YSTPLTFGQGTKVEIK (SEQ ID NO: 25) QVQLVQSGAEVKKPGASVKVSCKASGYSFTGYTMNWVRQAPGQGLEWMGLINPYNSDTNYAQ KLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARVALRVALDYWGQGTLVTVSSGTEGKSS GSGSESKSTDIQMTQSPSSLSASVG DRVTrrCKASQNVATHVGWYQQKPGKAPKRLIYSASYRY SGVPSRFSGSGSGTEFTLTISNLQPEDFATYYCQQYNRYPYTFGQGTKLEIK (SEQ ID NO: 26) QLQLQESGPGLVKPSETLSLTCTVSGGSLSSSSYWWGWTRQPPGRGLEWIGTIMYYSGNI YYNP SLQSRATISVDTSKNQFSLKLSSVTAADTAVYYCARHVGYSYGRRFWYFDLWGRGTLVTVSSG GSEGKSSGSGSESKSTGGSEIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPR LLIYDASNRATGIPARFSGSGSG1DF1LTISSLEPEDFAVYYCQQRSNWPPTF GQGTKVEIK (SEQ ID NO: 75) EIVLTQSPATLSSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGS GSGTDFTLTISSLEPEDFAVYYCQQRSNWPPTFGQGTKVEIKGGSEGKSSGSGSESKSTGGSQL QLQESGPGLVKPSETLSLTCTVSGGSLSSSS YWWGWTRQPPGRGLEWIGTMYYSGNIYYNPSL QSRATISVDTSKNQFSLKLSSVTAADTAVYYCARHVGYSYGRRFWYFDLWGRGTLVTVSS (SEQ ID NO : 76) QVTLKESGPVLVKPTETLTLTCTVSGFSLTNIRMSVSWIRQPPGKALEWLAHIFSNDEKSYSSSL KSRLTISRDT5KSQWLTLTNVDPVDTATYYCARMRLPYGMDVWGQG11V1VSSGGSEGKSSG SGSESKSTGGSDIVMTQTPLSSPVTLGQPASISCRSSQSLVHSDGNTY LSWLQQRPGQPPRLLI YKISNRFFGVPDRFSGSGAGTDFTLKISRVEAEDVGVYYCMQATQFPHTFGQGTKLEIK (SEQ ID NO: 77) DIVMTQTPLSSPVTLGQPASISCRSSQSLVHSDGNTYLSWLQQRPGQPPRLLIYKISNRFFGVPD RFSGSGAGTDFTLKISRVEAEDVGVYYCM QATQFPHTFGQGTKLEIKGGSEGKSSGSGSESKST GGSQVTLKESGPVLVKPTETLTLTCTVSGFSLTNIRMSVSWIRQPPGKALEWLAHIFSNDEKSYS SSLKSRLTISRDTSKSQVVLTLTNVDPVDTATYYCARMRLPYGMDVWGQGTTVTVSS (SEQ ID NO: 78) Hinge sequence of CD8 human TSTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACD (SEQ ID NO: 16) Sequence of lYIWAPLAGTCGVLLLSLVrTLYC CD8 TM domain (SEQ ID NO: fifteen) human Intracellular sequence of human CD137 KRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCEL (SEQ ID NO: 12) intracellular domain RVKFSRSADAPAYKQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNEL of CD3 zeta QKDKMAEAYSEIGMKGERRRRGKGH D GLYQGLSTATKDTYDALH MQALPPR human (SEQ ID NO: 13) ΜΛ / t / ZUZ I / U / 4400 Example 2 - Induction of Activation Markers in Antigen-Stimulated CAR-T Cells Twenty-four hours after transient transfection, primary pan T cells were labeled with Cell Trace Violet (CTV) fluorescent proliferation dye and then cocultured with the cell line. of multiple myeloma, H929. Four days after cocultivation, cells were pregated in the CD8+CD4- population and the surface expression of the activation markers CD25 and CD71 on CAR-T were compared to T cells cultured alone or in the presence of aCD3 / microspheres. CD28. (Figure 2). The same CAR T cells from Figure 1 were analyzed for a T cell activation response to H929 cells expressing GPRC5D antigen. Four days after electroporation, CAR A and CAR B showed an increase in T cell activation response, shown by an increase in CD25 and CD71 expression in response to culture with H929 cells. In comparison, mock cells and cells expressing CAR C demonstrated decreased T cell activation in response to H929 cells. As a negative control, the same cells were grown in the absence of any GPRC5D or T cell antigen and showed minimal increases in CD25 or CD71. As a positive control, mock, CAR A, CAR B, and CAR C cells were cocultured with CD3 / CD28 microspheres. Each of the four cell populations showed similar increases in the expression of CD25 and CD71. In total, these data show that CAR A and CAR B cells demonstrated the greatest T cell activation response to H929 cells expressing GPRC5D. Example 3 - Cytokine profile of antigen-stimulated CAR-T cells Primary pan T cells transiently transfected 24 hours earlier with CAR-expressing mRNA were cocultured in a 1:1 ratio with various myeloma cell lines, expressing the target antigen, GPRC5D, at high (+++), medium (+ +), low (+) or negative (-). Sixteen hours after coculture, supernatants were collected and cytokine profile analysis was performed using the Meso Scale Discovery (MSD) method of the coculture supernatants. (Figure 3). GPRC5D CAR-T cell supernatants showed an increase in proinflammatory cytokines INF-γ, TNF-α, or IL-2. The increase in each one of the proinflammatory cytokines was respective to the expression of GPRC5D of the cell lines cocultured with the CAR-T cells of GPRC5D. Cocultivation with MM.1S resulted in the highest expression of INF-γ and TNF-a, while cocultivation with KMS11 cells resulted in higher levels of IL-2. The K562 cell line was used as a negative control, demonstrating basal levels of basal cytokines with a cell line that does not express GPRC5D. Twenty-four hours after transient transfection with CAR-expressing mRNA, primary pan T cells were cocultured (in a 1:1 ratio) with autologous peripheral blood mononuclear cells (PBMCs) and the multiple myeloma cell line, H929. Sixteen hours after cocultivation, the supernatants were collected. MSD cytokine profile analysis of supernatants from cocultures containing all three populations (CAR-T, H929, autologous PBMCs) were compared to control cocultures lacking CAR-T cells, PBMCs, or H929, with each population of cells grown in isolation. (Figure 4). Similar to Figure 3, mock, CAR-T A, CAR-T B, CAR-T C, or isotypic CAR-T cells were cocultured with H929 and / or autologous PBMC. Increases in TNF-α and IL-2 with CAR-T A and CAR-T B cells were observed when H929 cells were cocultured with the PBMCs. When CAR-T C cells were cocultured with H929 and PBMC, limited to undetectable levels of INF-γ release were observed. Overall, CAR-T C cells demonstrated decreased cytokine release consistent with reduced markers of T cell activation in Figure 2. CAR-T cells, H929, and PBMC were grown alone as negative controls and showed background cytokine levels. Example 4 - Targeted Cytotoxicity of Tumor Cell Lines Expressing GPRC5D: High / Low / Aue Target Cell Lines Do Not Express GPRC5D The cytotoxic potential of CAR-T cells on myeloma cells expressing GPRC5D was assessed by flow cytometry. Primary pan T cells (transiently expressing one of the three CARs described above) were cocultured at the indicated effector:target (E:T) ratios with fluorescently labeled myeloma cell lines, MM1R, H929, and K562, for eight hours, time at which the cocultures were stained with viability dye. Percent kill is the ratio of the absolute number of live target (CTV positive) (viability dye negative) cells remaining in the coculture relative to the number of live targets cultured without CAR-T cells. (Figure 5). CAR A, CAR B, CAR C, isotypic CAR and mock T cells were cocultured with GPRC5D+ MM1R and H929 cell lines or GPRC5D-K562 cells for eight hours. Various effector to target relationships were analysed, showing that CAR A, CAR B and CAR C cells were able to induce MM1R cell cytotoxicity. Increases in cytotoxicity were correlated with higher effector to target ratios. Isotype and mock controls are included as controls and showed approximately 20-30% cytotoxicity. Similarly, CAR A and CAR B cells induced H929 cell cytotoxicity. CAR A cells and IVIA / I / U / 4400 CAR B demonstrated similar cytotoxicity activity to isotype and mock cells. These data demonstrate the specificity of CAR A and CAR B cells to MM1R and H929 cells, but not to K562 (GPRC5D) cells. Example 5 - Targeted Cytotoxicity of Tumor Cell Lines Expressing GPRC5D: T-Cells Derived from Multiple Myeloma Patients The cytotoxic potential of CAR-T cells on myeloma cells expressing GPRC5D was assessed by flow cytometry. Primary T cells from patients with multiple myeloma (transiently expressing one of two CARs as described above) in the indicated effector:target (E:T) ratios were cocultured with the fluorescently labeled myeloma cell line MM.1S or negative cell line. of GPRC5D KG-1 control for 48 hours, at which time the co-cultures were stained with viability stain. Percent cytotoxicity was determined as the percentage of fluorescently labeled cells that stained positive for the viability dye, indicating cell death. (Figure 6). Primary T cells from multiple myeloma patients transduced with either GC5B81_LH or GC5B483_LH both induced cytotoxicity of MM.1S GPRC5D+ cells with increased numbers of effector cells compared to mock T cells. There was no observable cytotoxicity with the GPRC5D GC5B81_LH or GC5B483_LH CAR-T cells when cocultured with the KG-1-GPRC5D cell line. These data show that GPRC5D CAR-transduced multiple myeloma T cells can cause the killing of GPRC5D+ cells, but not GPRC5D cells. Example 6 - Antigen-stimulated proliferative response of CAR-T cells of O-GPRC5D The CAR-T cell proliferative capacity of O-GPRC5D was assessed by flow cytometry. Fluorescently labeled pan T cells (transiently expressing an O-GPRC5D CAR or an isotypic CAR control) were cocultured at a 1 effector:1 target ratio with H929 for four days. Proliferation was measured as the absolute number of live CAR-T (viability dye negative) cells that had diluted fluorescent tracer (CTV). Proliferation in response to H929 was compared to CAR-T proliferation after four days of stimulation of O-CD3 / CD28 microspheres and cultured CAR-T alone (no stimulation control). (Figure 7). Mock, CAR isotypic, CAR-T A, CAR-T B, and CAR-T C cells were cocultured with GPRC5D+ H929 cells, CD3 / CD28 beads, or no stimuli. After four days, CD4 and CD8 populations were analyzed for total live counts, reflecting the proliferative capacity of the cells in response to the GPRC5D antigen. In the CD4 population, CD3 / CD28 microspheres were used as a positive control and all cell populations demonstrated an increase in CD4 events compared to no stimulation. only the IVIA / I / U / 4400 CAR-T A and CAR-T B cells showed a strong increase in counts in response to H929 cells compared to isotypic and mock cells. Similar results were observed for the CD8 population; however, CAR-T C did not show a proliferation response in response to H929 cells. Taken together, these data show that CAR-T A and CAR-T B cells proliferate in response to H929 GPRC5D+ cells. Example 7 - GPRC5D CAR Expression in Healthy Donor T Cells Six primary human pan T cells were activated and expanded using the Miltenyi Biotec T cell transaction system. 24 hours after activation, T cells were transduced with lentivirus comprising a nucleotide sequence encoding the GC5B680-N68S-LH CAR of GPRC5D (SEQ ID NO: 90). Cells were allowed to expand for 12 days, with surface CAR expression measured by flow cytometry on days 6 and 10 using a commercially available rabbit anti-human H+L detection antibody. Results are shown in Figure 8, data represent the mean ± SD of 6 healthy donors. The shaded gray bars (mock) immediately to the left of the black bars (GCB6800-N68S-LH) represent background CAR detection using the commercial antibody in non-transduced cells (mock). Black bars represent CAR-T cells transduced with GPRC5D GC5B680-N68S-LH. ΜΛ / t / ZUZ I / U / 4400 Example 8 - Expression of CD4, CD8, v Memory Markers in GPRC5D CAR-T Cells Pan T cells from six healthy donors were transduced with lentivirus comprising a nucleotide sequence encoding the GPRC5D GC5B680-N68S-LH CAR (GPRC5D CAR; SEQ ID NO:90). Mock (non-transduced) cells and transduced cells (T-cell group including cells with superficial CAR (expressing CAR or CAR+) and cells without superficial CAR (not expressing CAR or CAR-)] were evaluated for the proportion of cells with Superficial CD4 (CD4+) and the proportion of cells with superficial CD8 (CD8+).Data are shown in Figures 9A-9C.Data in Figure 9C show that GPRC5D CAR was detected in both CD4+ and CD8+ T cells. , as expected Figures 9A-9C also show that the CD4:CD8 ratio was similar among all cell populations tested, including CAR+ cells, CAR' cells, and mock cells. T cell subtypes in the CAR-T population were determined using two surface markers CD45RA and CD62L to differentiate between four memory cell populations: RA+ (Temra+) effector memory T cells, Tem effector memory cells, naive T cells, and T cells. memory stem Tn / scm, and central memory T cells (Tcm). The data is shown in Figures 9D-9F. Figure 9D is a representative flow cytogram from a donor sample highlighting a compartmentalization strategy to distinguish the four different memory populations using the two surface markers. Figures 9E and 9F show that GPRC5D GC5B680-N68S-LH was mainly expressed in Tn / scm and Tcm cells, which are known to have high proliferative capacity, survival, and therapeutic efficacy. Example 9 - GPRC5D CAR-T cytotoxicity assay at 6 hours v 24 hours GPRC5D GC5B680-N68S-LH transduced T cells from one of six healthy donors, or non-transduced (mock) T cells, were added in various E:T ratios to (i) GPRC5D+ MM.1S tumor cell cultures comprising a luciferase transgene or to (ii) GPRC5D K562 tumor cell cultures comprising a luciferase transgene. Cytotoxicity was assessed at each E:T ratio after 6 hours or 24 hours of incubation. The data is illustrated in Figure 1OA for the 6 hour time point, and in Figure 1OB for the 24 hour time point. Percent specific lysis was calculated (i) by measuring the luciferase signal in tumor cells incubated in the presence of CAR-T at 6 or 24 hours divided by the luciferase signal in tumor cells incubated alone at the same time points. time and multiplied by 100 and (ii) by subtracting that number from 100. The equation is: 100-[(CAR-T + tumor luminescence) / (average luminescence of tumor only)] x 100. The dashed line highlights zero lysis . Negative lysis is indicative of cell growth. Example 10 - GPRC5D CAR-T Cytotoxicity Assay at 48 Hours GPRC5D GC5B680-N68SLH transduced and non-transduced (mock) T cells were prepared from healthy donors. Either (i) GPRC5D GC5B680-N68S-LH transduced T cells or (ii) non-transduced (mock) T cells were added at various E:T ratios to GPRC5D+ H929 cells, GPRC5D+ MM.1S, GPRC5D+ MM.1R GPRC5D+, GPRC5D+ MOLP-2, GPRC5D+ EJM and GPRC5D K562 labeled with carboxyfluorescein succinimidyl ester (CFSE). After 48 hours of incubation, cells were stained with a live / dead stain and evaluated for percentage dead cells and CFSE+ (% cytotoxicity). Percent cytotoxicity was plotted against a log-transformed x-axis (E:T ratios) with a 4-parameter non-linear regression curve fit, with data shown in Figures 11A-11F as mean ± SD. Mock negative control T cells induced some degree of cytotoxicity in all GPRC5D+ cell lines other than E3M, but to a lesser degree than GPRC5D GC5B680-N68S-LH cells, especially at the higher E:T ratios. Without theoretical limitations of any kind, the reduced cytotoxicity likely arose from an allogeneic response. Furthermore, the cytotoxicity of GPRC5D CAR cells varied depending on the cell line. / U / 4400 Example 11 - GPRC5D CAR-T Activation Assay at 48 Hours GPRC5D GC5B680-N68S-LH transduced and non-transduced (mock) T cells were prepared from healthy donors. GPRC5D GC5B680-N68S-LH transduced or non-transduced (mock) T cells were added at an E:T ratio of 3:1 to GPRC5D+ H929, GPRC5D+ MM.1S, GPRC5D+ MOLP-2, GPRC5D+ and K562 cells. of GPRC5D labeled with succinimidyl ester (CFSE). After 48 hours of incubation, cells were stained with a live / dead stain, anti-CD25, anti-CD3, and anti-CAR visual markers. Cells were then assessed for surface expression of CD25. Data are expressed in Figure 12 as the mean ± SD. As shown in Figure 12, less than 13% background surface expression of CD25 was observed in the mock cells (ie, no activation). In contrast, GC5B680N68S-LH CAR-T cells were activated in the presence of GPRC5D+ cell lines, as shown by increased levels of CD25 expression. In both (i) mock CAR-T cells and (ii) GC5B680-N68S-LH CAR-T cells alone, low levels of surface CD25 expression were observed after incubation with K562 cells or after incubation alone. Example 12 - GPRC5D CAR-T polyfunctionality assay Cells (CAR-T) transduced with GC5B680-N68S-LH were incubated with PMA / ionomycin (as a positive control), a GPRC5D+ cell line H929 (H929), GPRC5D' K562 (K562) cells (CFSE-labeled), or alone, for 18 hours. Cells were incubated at an E:T ratio of 1:2 when incubated in the presence of H929 or K562 cells. Cells were then first stained with a live / dead, anti-CD3, and antiidiotype stain followed by fixation, permeabilization, and intracellular staining with anti-IFN-γ, anti-IL-2, and anti-TNF-α. The stained cells were then analyzed by flow cytometry. Percentages of individual cytokine levels were calculated after analysis of flow cytograms using Boolean (hierarchical) compartmentalization, with percentages represented in Tables 3-6 below. Also in Tables 3-6, the levels of release of polyfunctional cytokines for each group are highlighted in gray with the sums of means represented. Table 3. Expression of cytokines in CAR-T cells incubated in the presence of H929. ΜΛ / t / ZUZ I / U / 4400 Polyfunctional Populations CAR-T Diana Ident. from T cell donor IFNy+ IL2 TNFa+ IFNy+ IL2 TNFa- IFNy+ IL2- TNFa+ IFNyIL2 TNFa+ IFNY+ IL2 TNFa- IFNyIL2 TNFa- IFNyIL2 TNFa+ IFNyIL2 TNFa- GC5B680- N68S-LH H929 D 204071 2.1 0.2 4.4 18.1 0.8 1.8 43.2 29.4 GC5B680- N68S-LH H929 D270235 4.1 0.5 8.5 10.9 3.8 2.2 31.4 38.6 GC5B680- N68S-LH H929 110039522 1.3 0.1 1.8 19.1 0.5 0.5 42.2 3 4.6 GC5B680-N68S-LH H929 D202896 13.5 0.0 30.7 6.8 2.1 0.4 27.1 19.5 GC5B680-N68S-LH H929 D328058 7.0 0.1 12.2 18.2 0.8 0.2 32.9 28.7 GC5B680- N68S-LH H929 D204395 4.3 0.0 4.6 30.5 0.4 0.3 37.9 22.1 Percentage of polyfunctional H929 33 .1 IVIA / C / 2U2I / U / 4400 Table 4, Expression of cytokines in CAR-T cells incubated in the presence of K562 Polyfunctional Populations CAR-T Diana Ident. from T cell donor IFNy+ IL2 TNFa + IFNy+ IL2 TNFa- IFNY+ IL2 TNFa + IFNyIL2 TNFa+ IFNy+ IL2 TNFa- IFNyIL2 TNFa- IFNyIL2 TNFa + IFNyIL2 TNFa- GC5B680- N68S-LH K562 D2 04071 0.0 0.0 0.5 0.5 1.5 3.2 5.7 88.5 GC5B680- N68S -LH K562 D270235 0.2 0.5 2.0 1.1 2.7 3.0 7.7 83.0 GC5B680- N68S-LH K562 110039522 0.1 0.3 0.3 0.2 1.0 1.1 3.6 93.4 GC5B680- N68S- LH K562 D202896 0.2 0.2 1.3 0.5 2.3 4.5 3.7 87.4 GC5B680- N68S-LH K562 D328058 0.2 0.1 1.4 0.3 1.6 2.1 6.1 88.1 GC5B680- N68S-LH K562 D204395 0.1 0.2 0.5 0.5 0.7 3.1 9.4 85.5 Percentage of polyfunctional K562 1.9 Table 5 Expression of cytokines in CAR-T cells incubated alone / U / 4430 Polyfunctional Populations CAR-T Diana Ident. from T cell donor IFNy+ IL2 TNFa + IFNY+ IL2 TNFd- IFNy+ IL2 TNFa+ IFNyIL2 TNFa+ IFNY+ IL2 TNFd- IFNyIL2 TNFd- IFNyIL2 TNFd + IFNyIL2 TNFd- GC5B680- N68S-LH CART only D204 071 0.0 0.4 0.7 0.1 2.0 3.2 4.3 89.2 GC5B680- N68S -LH CART only D270235 0.4 0.8 1.8 0.4 4.1 3.7 6.5 82.4 GC5B680- N68S-LH CART only 110039522 0.1 0.4 0.2 0.2 1.7 1.4 1.9 94.0 GC5B680- N68S-LH CART only D202896 0.1 0.6 1.8 0.4 2.4 6.8 2.1 86.0 GC5B680- N68S-LH CART only D328058 0.2 0.4 1.0 0.3 1.4 3.2 3.9 89.6 GC5B680- N68S-LH CART only D204395 0.1 0.3 0.7 0.5 1.6 5.0 7.2 84.5 Percentage of multifunctional CAR-T alone 2.0 Table 6. Expression of cytokines in CAR-T cells incubated in the presence of PMA / lonomycin. Polyfunctional Populations CAR-T Diana Ident. from T cell donor IFNy+ IL2 TNFd+ IFNy+ IL2 TNFd- IFNy+ IL2 TNFd+ IFNyIL2 TNFd+ IFNY+ IL2 TNFd- IFNyIL2 TNFd- IFNyIL2 TNFd + IFNyIL2 TNFd- GC5B680- N68S-LH PMA / iono mycin D204071 10.8 0.1 6.0 62.7 0.2 1.5 15.8 2.9 GC5B680- N68S -LH PMA / ionomycin D270235 31.0 0.2 16.7 43.9 0.3 0.4 7.0 0.6 GC5B680- N68S-LH PMA / ionomycin 110039522 10.5 0.0 2.8 68.8 0.0 0.4 16.1 1.5 G C5B680- N68S-LH PMA / ionomycin D202896 42.8 0.3 29.1 20.0 0.5 0.1 6.2 1.0 GC5B680- N68S-LH PMA / ionomycin D328058 33.6 0.1 15.4 42.1 0.2 0.2 7.5 0.9 GC5B680- N68S-LH PMA / ionomycin D204395 21.2 0.0 6.1 59.3 0.4 1.0 10.7 1.3 Percentage of polyfunctional PMA / ionomycin 87.3 IVIA / I / U / 4400 Example 13 - GPRC5D CAR-T proliferation assay GC5B680-N68S-LH cells were prepared using cells from a donor. The (i) cells transduced with GC5B680-N68S-LH and (ii) mock cells were incubated in the presence or absence of GPRC5D+ (MM.1S and H929) cells. Mock (non-transduced) cells were used as a negative control. The degree of cell proliferation was measured after a 6-day incubation by assaying the degree of dilution of the CELLTRACE Violet dye (CTV) concentration in the cells, with the amount represented by the X-axis of the graphs in Figure 13. CAR+ cells were stained using an anti-idiotype antibody, with the degree of staining represented by the Y-axis of the graphs in Figure 13. As shown in Figure 13, CTV-labeled mock CAR T cells, alone or in the presence of GPRC5D-K562 cells, demonstrated little or no cell proliferation as seen from a low to zero dilution of CTV dye. CD3 / CD28 agonist microspheres (serving as positive control) resulted in proliferation of all T cell populations tested, as predicted. When CAR-T cells were incubated with GPRC5D+ (H929 or MM.1S) target cells, proliferation was enriched mainly in transduced cells expressing GC5B680-N68S-LH on their surface (CAR+) (as shown in the upper quadrants in the graphs of Figure 13). This result suggested that the proliferation of GC5B680-N68S-LH cells is enhanced in the presence of GPRC5D+ target cells. The data shown in Figure 13 are representative of similar observations made using cells prepared from other donors. Example 14 - GPRC5D CAR-T proliferation assay GC5B680-N68S-LH (CAR-T) cells were incubated with staurosporine positive control, GPRC5D+ H929 cells, GPRC5D- K562 cells, or alone, for 24 hours. An E:T ratio of 1:2 was used for incubations of GC5B680-N68S-LH cells (CAR-T) with H929 or K562 cells. Cells were then stained with a live / dead stain, anti-CD3, anti-idiotype, and cleaved anti-caspase 3 / 7 stain. Stained cells were analyzed by flow cytometry. The data is expressed in the graph of Figure 14. As shown in Figure 14, staurosporine induced cleaved caspase 3 / 7 staining in both CAR+ and CAR T cell populations. Also, there were 50-65% positive cells from 4 hours after the 24 hour time point. Neither the CAR+ nor CAR- T cell populations demonstrated significant differences in caspase 3 / 7 levels between the negative control incubations (K562 and CART alone) and incubations in the presence of H929. Example 15 - Efficacy test of GC5B680-N68S-LH, GC5B680-N68S-HL, GP5B83 N24T N31S-LH, and GP5B83 N24T N31S-HL in MM xenoinierts. Established IS of human MM in NSG-B2M mice The antitumor efficacy of transduced T cells (CAR-T cells) of GC5B680-N68S-LH (SEQ ID NO:86), GC5B680-N68S-HL (SEQ ID NO:85), GP5B83_N24T_N31S-LH (SEQ ID NO:84) , and GP5B83_N24T_N31S-HL (SEQ ID NO:83) was evaluated in the subcutaneous human multiple myeloma (MM) xenograft model MM.1S (se) established in female NSG B2 m (alternatively referred to as NOD-scid II2rgniJl0B2mnul°, or NOD -scid gamma B2m). CAR-T cells from (i) GC5B680-N68S-LH, (ii) GC5B680-N68S-HL, (iii) GP5B83_N24T_N31S-LH, or (iv) GP5B83_N24T_N31S-HL were administered at a dose of CAR cells+lxlO6o cells CAR+5x1o6 intravenously (iv) on day 13 for a total of one dose. Three groups of mice bearing MM.1S xenograft were evaluated: (i) mice treated with PBS, (ii) mice that underwent mock transduction, and (iii) mice that were transduced with GPRC5D. The delta percent tumor growth inhibition (%ATGI) of the three groups of mice bearing MM.1S SC xenografts (subcutaneous) was calculated at day 26 post-tumor implantation by using the formula: ([ (TVc-TVc0)-(TVt-TVt0)] / (TVc-TVc0))xl00, where 'TVc' is the mean tumor burden of a given control group, 'TVcO' is the baseline mean tumor burden of a given control group of given control, 'TVt' is the median tumor burden of the treated group, and 'TVtO' is the baseline median tumor burden of the treated group. Statistical significance was calculated using linear mixed effects analysis in R, with treatment and time as fixed effects and animal as random effect. Log transformation (base 10) was performed if individual longitudinal response trajectories were not linear. Information derived from this statistical model was used to make pairwise treatment comparisons with PBS control or sham transduced groups, with p-values ​​considered statistically significant when <0.05. All four CAR-T constructs targeting GPRC5D produced statistically significant % ATGI at dose levels of 1 x 106 and 5 x 106 CAR+T cells compared to PBS and mock CAR-T controls, as summarized in Table 7. and Figure 15. Complete responses (complete tumor regression, no palpable tumor) were assessed at day 47 post tumor implantation. MA / t / ZUZI / U / 4400 Table 7. Efficacy summary of CAR-T targeting GPRC5D in xenopositives of human MM MM.1S established in NSG-B2M mice ΜΛ / t / ZUZ I / U / 4400 Construct CAR+ Cell Dose Total T-Cell Dose (CAR+ and CAR cell count) % ATGI CR (n of group) Mock - 28.6 x 106 21% 0 / 10 GC5B680-N68S-LH 1 x 106 5 x 106 5.71 x 106 28.6 x 106 50% 97% 8 / 10 10 / 10 GC5B680-N68S-HL 1 x 106 5 x 106 5.71 x 106 28.6 x 106 52% 95% 8 / 10 10 / 10 GP5B83 N24T N31S-LH 1 x 106 5 GP5B83 N24T N31S-HL 1 x 106 5 x 106 5.71 x 106 28.6 x 106 70% 99% 10 / 10 10 / 10 p<0.05 vs. PBS controls and mock CAR-T, except where indicated not significant (ns). CR = complete response Example 16 - Efficacy of GC5B680-N68S-LH, GC5B680-N68S-HL, GP5B83 N24T N31S-LH and GP5B83 N24T N31S-HL in H929IV xenoinitiates of human MM in NSG mice The efficacy of GC5B680-N68S-LH (SEQ ID NO: 86; encoded by SEQ ID NO: nucleotides: 90), GC5B680-N68S-HL (SEQ ID NO: 85; encoded by SEQ ID NO: nucleotides: 89) , GP5B83_N24T_N31S-LH (SEQ ID NO: 84; encoded by SEQ ID NO: nucleotides: 88), and GP5B83_N24T_N31S-HL (SEQ ID NO: 83; encoded by SEQ ID NO: nucleotides: 87) transduced T cells were assessed. in a model of human H929 MM disseminated (iv) in female NSGTM mice (alternatively referred to as NOD scid gamma, or as NOD.Cg-PrkdcscidII2rgtmlWjl / SzJ). In this example, (CAR+) T cells expressing GC5B680-N68SLH, GC5B680-N68S-HL, GP5B83_N24T_N31S-LH, or GP5B83_N24T_N31S-HL were administered as a single iv dose of CAR+lxlO6 cells or CAR+5xl06 cells on day 9 post-treatment. tumor graft. A survival assessment was performed in which the percentage survival on various study days was plotted against the study days. Hindlimb paralysis or other clinical signs of excessive disseminated tumor burden were used as surrogate endpoints for destruction. Median survival was determined using the Kaplan Meier survival analysis. Percent ILS (%ILS) was defined as the difference between the median survival of the treated group compared to the control group and was calculated as ILS = ([MSt-MSc] / MSc)x 100, where 'MSc' is the median survival of a given control group and 'MSc' is the median survival of a particular treatment group. Animals that did not reach the surrogate titer due to adverse clinical signs (such as ulcerated tumors, loss of body weight, etc.) or non-treatment related death were censored for survival assessment. Survival was plotted using a Kaplan-Meier curve and assessed using the log-rank test (Mantel-Cox) using GraphPad Prism software (version 7.0). Median survival of 50% was achieved at day 52 post tumor implantation (43 days post CAR+ injection) for PBS-treated control mice. Median survival of 50% was achieved at day 44 post tumor implantation (35 days post CAR-T injection) for mice treated with mock CAR-T cells. Median survival of 50% was achieved after day 111 (102 days after CAR-T injection) for mice treated with GC5B680-N68S-LH CAR+ cells administered at a dose of 1x106. Median survival of 50% was achieved at day 63.5 (54.5 days after CAR-T injection) for mice treated with CAR+GC5B680-N68S-HL cells administered at a dose of lxlO6 cells, respectively. Median survival of 50% was achieved at day 93.5 (84.5 days after CAR-T injection) for mice treated with CAR+GP5B83_N24T_N31S-LH cells administered at a dose of lxlO6 cells. Median survival of 50% was achieved after day 111 (102 days after CAR-T injection) for mice treated with CAR+GP5B83_N24T_N31S-HL cells administered at a dose of 1x106 cells. Percentage increase in shelf life (ILS) was assessed using the Kaplan-Meier curve and was assessed using the Mantel-Cox log-rank test. All four CAR-T constructs targeting GPRC5D produced statistically significant % ILS at the 1 x 106 dose level compared to PBS and mock CAR-T controls, as described below and summarized in Table 8 and in Figure 16. Animals surviving to day 111 were considered CR. Table 8. Summary of the Efficacy of CAR-T Targeting GPRC5D in H929 Xenoprimers Disseminated from Human MM in NSG Mice Construct CAR+ T Cells Total T Cells Median Survival Days % of ILS CR (n of group) PBS - - 52 - 0 / 10 Sham - 37.1 x 106 44 - 0 / 10 GC5B680-N68S-LH 1 x 106 7.42 x 106 >111 >113.5% 8 / 10 GC5B680-N68S-HL 1 x 106 7.42 x 106 63.5 22.1% 2 / 10 GP5B83 N24T N31S-LH 1 x 106 7.42 x 106 93.5 79.8% 4 / 10 GP5B83 N24T N3 1S-HL 1 x 106 7.42 x 106 >111 >113.5% 7 / 10 p<0.05 vs. PBS controls and mock CAR-T, except where indicated not significant (ns). CR = complete response Adverse clinical signs associated with progressive tumor disease burden were observed in the PBS-treated control group from day 52 after tumor engraftment, while clinical signs of graft-versus-host disease developed in the PBS-treated groups. CAR-T with simulated transduction or with GPRC5D from day 48 posttumor graft. The teachings of all patents, published applications, and references cited herein are incorporated by reference in their entirety for all purposes. While the illustrative embodiments have been particularly shown and described, it will be understood by those skilled in the art that various changes may be made in the form and detail thereof without departing from the scope of the embodiments encompassed by the appended claims. LIST OF SEQUENCES MA / t / ZUZI / U / 4400 Light chain sequence 1 (GC5B4831 (SEO ID NO: 11 EIVLTQSPATLSSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTI SSLEPEDFAVYYCQQRSNWPLTFGQGTKVEIK Heavy chain sequence 1 (GC5B4831 (SEO ID NO: 21 EVQLVQSGAEVKKPGESLKISCKGSGYSFTSYFIGWVRQMPGKGLEWMGIIYPGKSDTRYSPSFQGQVTISAD KSISTAYLQWSSLKASDTAMYYCARVYSFGGRHKALFDYWGQGTLVTVSS Light chain sequence 2 (GC5B811 (SEO ID NO: 31 DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTI SSLQPEDFATYYCQQSYSTPLTFGQGTKVEIK heavy chain sequence 2 (GC5B811 (SEO ID NO: 41 QVQLVQSGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTANYAQKFQGRVTITAD ESTSTAYMELSSLRSEDTAVYYCARESRWRGYKLDYWGQGTLVTVSS Light chain sequence 3 (GC5B5961 (SEO ID NO: 51 DIQMTQSPSSLSASVGDRVTITCKASQNVATHVGWYQQKPGKAPKRLIYSASYRYSGVPSRFSGSGSGTEFTL TISNLQPEDFATYYCQQYNRYPYTFGQGTKLEIK Stopped chain sequence 3 (GC5B5961 (SEO ID NO: 61 QVQLVQSGAEVKKPGASVKVSCKASGYSFTGYTMNWVRQAPGQGLEWMGLINPYNSDTNYAQKLQGRVTMT TDTSTSTAYMELRSLRSDDTAVYYCARVALRVALDYWGQGTLVTVSS Linker polypeptide sequence (SEO ID NO: 7) GTEGKSSGSGSSESKST scFv Sequence 1 (GC5B483) (SEO ID NO: 8) EIVLTQSPATLSSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTI SSLEPEDFAVYYCQQRSNWPLTFGQGTKVEIKGTEGKSSGSGSESKSTEVQLVQSGAEVKKPGESLKISCKGSG YSFTSYFIGWVRQMPGKGLEWMGIIYPGKSDTRY SPSFQGQVTISADKSISTAYLQWSSLKASDTAMYYCARV YSFGGRH KALFDYWGQGTLVTVSS scFv 2 sequence (GC5B811 (SEO ID NO: 91 DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTI SSLQPEDFATYYCQQSYSTPLTFGQGTKVEIKGTEGKSSGSGSESKSTQVQLVQSGAEVKKPGSSVKVSCKASG GTFSSYAISWVRQAPGQGLEWMG GIIPIFGTANYAQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCARES RWRGYKLDYWGQGTLVTVSS scFv 3 sequence (GC5B5961 (SEO ID NO: 101 DIQMTQSPSSLSASVGDRVTITCKASQNVATHVGWYQQKPGKAPKRLIYSASYRYSGVPSRFSGSGSGTEFTL TISNLQPEDFATYYCQQYNRYPYTFGQGTKLEIKGTEGKSSGSGSESKSTQVQLVQSGAEVKKPGASVKVSCKA SGYSFTGYTMNWVRQAPG QGLEWMGLINPYNSDTNYAQKLQGRVTMTTDTSSTAYMELRSLRSDDTAVYY CARVALRVALDYWGQGTLVTVSS Signal sequence (SEO ID NO: 111 MAWVWTLFLMAAAQSIQA CD137 sequence (SEO ID NO: 121 KRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCEL CD3z sequence (SEO ID NO: 131 RVKFSRSADAPAYKQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYS EIGMKGERRRGKGHHDGLYQGLSTATKDTYDALHMQALPPR / U / 4400 Intracellular signaling domain (SEO ID NO: 141 KRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCELRVKFSRSADAPAYKQGQNQLYNELNLGRREE YDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEIGMKGERRRGKGHHDGLYQGLSTATKDTYD ALHMQALPPR CD8a-TM sequence (SEO ID NO: 15) IYIWAPLAGTCGVLLLSLVITLYC Hinge sequence of Cd8a (SEO ID NO: 16) TSTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACD Extracellular binding domain (GC5B483) (SEO ID NO: 17) MAWVWTLFLMAAAQSIQAEIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNR ATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPLTFGQGTKVEIKGTEGKSSGSGSESKSTEVQLV QSGAEVKKPGESLKISCKGSGYSFTSYFIGWVRQMP GKGLEWMGIIYPGKSDTRYSPSFQGQVTISADKSISTA YLQWSSLKASDTAMYYCARVYSFGGRHKALFDYWGQGTLVTVSS Extracellular binding domain (GC5B81) (SEO ID NO: 18) MAWVWTLFLMAAAQSIQADIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSL QSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPLTFGQGTKVEIKGTEGKSSGSGSESKSTQVQLV QSGAEVKKPGSSVKVSCKASGGTFSSY AISWVRQAPGQGLEWMGGIIPIFGTANYAQKFQGRVTITADESTST AYMELSSLRSEDTAVYYCARESRWRGYKLDYWGQGTLVTVSS Extracellular binding domain (GC5B596) (SEO ID NO: 19) MAWVWTLFLMAAAQSIQADIQMTQSPSSLSASVGDRVTITCKASQNVATHVGWYQQKPGKAPKRLIYSASY RYSGVPSRFSGSGSGTEFTLTISNLQPEDFATYYCQQYNRYPYTFGQGTKLEIKGTEGKSSGSGSESKSTQVQL VQSGAEVKKPGASVKVSCKASG YSFTGYTMNWVRQAPGQGLEWMGLINPYNSDTNYAQKLQGRVTMTTDTS TSTAYMELRSLRSDDTAVYYCARVALRVALDYWGQGTLVTVSS Extracellular binding domain (GC5B483) (SEO ID NO: 20) MAWVWTLFLMAAAQSIQAEVQLVQSGAEVKKPGESLKISCKGSGYSFTSYFIGWVRQMPGKGLEWMGIIYP GKSDTRYSPSFQGQVTISADKSISTAYLQWSSLKASDTAMYYCARVYSFGGRHKALFDYWGQGTLVTVSSGTE GKSSGSGSESKSTEIVLTQSPATLSSLSPGERATLSC RASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARF SGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPLTFGQGTKVEIK MA / t / ZUZI / U / 4400 Extracellular binding domain (GC5B81) (SEO ID NO: 21) MAWVWTLFLMAAAQSIQAQVQLVQSGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIP IFGTANYAQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCARESRWRGYKLDYWGQGTLVTVSSGTEGKS SGSGSESKSTDIQMTQSPSSLSASVGDRVTITCRAS QSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPSRFSG SGSGTDFTLTISSLQPEDFATYYCQQSYSTPLTFGQGTKVEIK Extracellular binding domain (GC5B596) (SEO ID NO: 22) MAWVWTLFLMAAAQSIQAQVQLVQSGAEVKKPGASVKVSCKASGYSFTGYTMNWVRQAPGQGLEWMGLIN PYNSDTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARVALRVALDYWGQGTLVTVSSGTEGKS SGSGSESKSTDIQMTQSPSSLSASVGDRVTITCKASQN VATHVGWYQQKPGKAPKRLIYSASYRYSGVPSRFS GSGSGTEFTLTISNLQPEDFATYYCQQYNRYPYTFGQGTKLEIK scFv Sequence 4 (GC5B483) (SEO ID NO: 24) EVQLVQSGAEVKKPGESLKISCKGSGYSFTSYFIGWVRQMPGKGLEWMGIIYPGKSDTRYSPSFQGQVTISAD KSISTAYLQWSSLKASDTAMYYCARVYSFGGRHKALFDYWGQGTLVTVSSGTEGKSSGSGSESKSTEIVLTQS PATLSLSPGERATLSCRASQSVSSYLAWYQQK PGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTISSLEPED FAVYYCQQRSNWPLTFGQGTKVEIK scFv Sequence 5 (GC5B81) (SEO ID NO: 25) QVQLVQSGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTANYAQKFQGRVTITAD ESTSTAYMELSSLRSEDTAVYYCARESRWRGYKLDYWGQGTLVTVSSGTEGKSSGSGSESKSTDIQMTQSPSS LSASVGDRVTITCRASQSISSYLNWYQQKPG KAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFAT YYCQQSYSTPLTFGQGTKVEIK scFv 6 sequence (GC5B596) (SEO ID NO: 26) QVQLVQSGAEVKKPGASVKVSCKASGYSFTGYTMNWVRQAPGQGLEWMGLINPYNSDTNYAQKLQGRVTMT TDTSTSTAYMELRSLRSDDTAVYYCARVALRVALDYWGQGTLVTVSSGTEGKSSGSGSGSESKSTDIQMTQSPSS LSASVGDRVTITCKASQNVATHVGWYQQKPGK APKRLIYSASYRYSGVPSRFSGSGSGTEFTLTISNLQPEDFA TYYCQQYNRYPYTFGQGTKLEIK Sequence GC5B483-LH-CAR of ODR000074490 (SEO ID NO: 27) MAWVWTLFLMAAAQSIQAEIVLTQSPATLSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNR ATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPLTFGQGTKVEIKGTEGKSSGSGSESKSTEVQLV QSGAEVKKPGESLKISCKGSGYSFTSYFIGWVRQMP GKGLEWMGIIYPGKSDTRYSPSFQGQVTISADKSISTA YLQWSSLKASDTAMYYCARVYSFGGRHKALFDYWGQGTLVTVSSTSTPAPRPPTPAPTIASQPLSLRPEACRPA AGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEE IVIA / I / U / 4400 100 EGGCELRVKFSRSADAPAYKQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDK MAEAYSEIGMKGERRRGKGHHDGLYQGLSTATKDTYDALHMQALPPR Sequence GC5B81-LH-CAR of oDR000074489 (SEO ID NO: 28) MAWVWTLFLMAAAQSIQADIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSL QSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPLTFGQGTKVEIKGTEGKSSGSGSESKSTQVQLV QSGAEVKKPGSSVKVSCKASGGTFSSY AISWVRQAPGQGLEWMGGIIPIFGTANYAQKFQGRVTITADESTST AYMELSSLRSEDTAVYYCARESRWRGYKLDYWGQGTLVTVSSTSTPAPRPPTPAPTIASQPLSLRPEACRPAAG GAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEG GCELRVKFSRSADAPAYKQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMA EAYSEIGMKGERRRGKGHHDGLYQGLSTATKDTYDALHMQALPPR Sequence GC5B596-LH-CAR of oDR000074488 (SEO ID NO: 29) MAWVWTLFLMAAAQSIQADIQMTQSPSSLSASVGDRVTITCKASQNVATHVGWYQQKPGKAPKRLIYSASY RYSGVPSRFSGSGSGTEFTLTISNLQPEDFATYYCQQYNRYPYTFGQGTKLEIKGTEGKSSGSGSESKSTQVQL VQSGAEVKKPGASVKVSCKASG YSFTGYTMNWVRQAPGQGLEWMGLINPYNSDTNYAQKLQGRVTMTTDTS TSTAYMELRSLRSDDTAVYYCARVALRVALDYWGQGTLVTVSSTSTPAPRPPTPAPTIASQPLSLRPEACRPAA GGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCCREE EE GGCELRVKFSRSADAPAYKQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKM AEAYSEIGMKGERRRGKGHHDGLYQGLSTATKDTYDALHMQALPPR Sequence GC5B483-HL-CAR of ODR000074483 (SEO ID NO: 30) MAWVWTLFLMAAAQSIQAEVQLVQSGAEVKKPGESLKISCKGSGYSFTSYFIGWVRQMPGKGLEWMGIIYP GKSDTRYSPSFQGQVTISADKSISTAYLQWSSLKASDTAMYYCARVYSFGGRHKALFDYWGQGTLVTVSSGTE GKSSGSGSESKSTEIVLTQSPATLSSLSPGERATLSC RASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARF SGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPLTFGQGTKVEIKTSTPAPRPPTPAPTIASQPLSLRPEACRPA AGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEE EGGCELRVKFSRSADAPAYKQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDK MAEAYSEIGMKGERRRGKGHHDGLYQGLSTATKDTYDALHMQALPPR SEQ ID NO: 30 Sequence GC5B81-HL-CAR of PDR000074482 (SEO ID NO: 31) MAWVWTLFLMAAAQSIQAQVQLVQSGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIP IFGTANYAQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCARESRWRGYKLDYWGQGTLVTVSSGTEGKS SGSGSESKSTDIQMTQSPSSLSASVGDRVTITCRAS QSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPSRFSG SGSGTDFTLTISSLQPEDFATYYCQQSYSTPLTFGQGTKVEIKTSTPAPRPPTPAPTIASQPLSLRPEACRPAAG GAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRF PEEEEG 101 GCELRVKFSRSADAPAYKQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMA EAYSEIGMKGERRRGKGHHDGLYQGLSTATKDTYDALHMQALPPR Sequence GC5B596-HL-CAR of dDR000074481 (SEO ID NO: 32) MAWVWTLFLMAAAQSIQAQVQLVQSGAEVKKPGASVKVSCKASGYSFTGYTMNWVRQAPGQGLEWMGLIN PYNSDTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARVALRVALDYWGQGTLVTVSSGTEGKS SGSGSESKSTDIQMTQSPSSLSASVGDRVTITCKASQN VATHVGWYQQKPGKAPKRLIYSASYRYSGVPSRFS GSGSGTEFTLTISNLQPEDFATYYCQQYNRYPYTFGQGTKLEIKTSTPAPRPPTPAPTIASQPLSLRPEACRPAA GGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPMFMRVQTTQEEDGCSCR FPEEEE GGCELRVKFSRSADAPAYKQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKM AEAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR DNA sequence for GC5B483-LH-CDS from dDR000074490 (SEO ID NO: 33) GAGATCGTGCTGACCCAGAGCCCAGCCACCCTGAGCCTGAGCCCAGGCGAGCGCGCCACCCTGAGCTGCCGCGC CTCTCAGAGCGTGAGCAGCTACCTGGCTTGGTATCAGCAGAAGCCCGGACAGGCCCCACGCCTGCTGATCTACGA CGCCAGCAACCGCCACCGGCATCCCAGCCCGCTTCAGCGGCAGCGGCAGCGGCA CCGACTTCACCCTGACCAT CAGCAGCCTGGAGCCAGAGGACTTCGCCGTGTACTACTGCCAGCAGCGCAGCAACTGGCCACTGACCTTCGGCCA GGGCACCAAGGTGGAGATCAAGGGTACAGAGGGCAAGTCTAGTGGAAGTGGTAGCGAAAGTAAGAGTACCGAG GTGCAGCTGGTGCAGAGCGGCGCTGAGGTCAAAA AGCCAGGCGAAAGCCTTAAAATATCATGCAAAGGAAGTGG ATATTCCTTTACCAGCTACTTCATCGGCTGGGTGCGCCAGATGCCAGGCAAGGGCCTGGAGTGGATGGGCATCA TCTACCCAGGCAAGAGCGACACCCGCTACAGCCCAAGCTTCCAGGGCCAGGTGACCATCAGCGCCGACAAGAGCA TCAGCACCGCCTACCTG CAGTGGAGCAGCCTGAAGGCCAGCGACACCGCCATGTACTACTGCGCCCGCGTGTACA GCTTCGGCGGCCGCCACAAGGCCCTGTTCGACTACTGGGGCCAGGGCACCCTGGTGACCGTGAGCAGCACTAGT ACCCCAGCCCCACGCCCTCCCACCCCTGCTCCTACAATAGCATCCCAGCCCTTGTCACTTCGCCCCGAAGCATGCA GACCAGCCGCAGGCGGTGCTGrGCATACCCGAGGACrGGACTTCGCCTGCGACATCrACATCTGGGCCCCACTG GCCGGCACCTGCGGCGTGCTGCTGCTGCTGAGCCTGGTGATCACCCTGTACTGCAAGCGCGGCCGCAAGAAGCTGCT GTACATCTTCAAGCAGCCATTCATGCGCCCAGTGCAGACCACCCAGGA GGAGGACGGCTGCAGCTGCCGCTTCCC AGAGGAGGAGGAGGGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCCGACGCCCCAGCCTACAAGCAG GGCCAGAACCAGCTGTACAACGAGCTGAACCTGGGCCGCCGCGAGGAGTACGACGTGCTGGACAAGCGCCGCGG CCGCGACCAGAGATGGGCGGCAAGCCAC GCCGCAAGAACCCACAGGAGGGCCTGTACAACGAGCTGCAGAAGG ACAAGATGGCCGAGGCCTACAGCGAGATCGGCATGAAGGGCGAGCGCCGCCGCGGCAAGGGCCACGACGGCCT GTACCAGGGCCTGAGCACCGCCACCAAGGACACCTACGACGCCCTGCACATGCAGGCCCTGCCACCACGC DNA sequence for GC5B81-LH-CDS from PDR000074489 (SEO ID NO: 34) GACATCCAGATGACCCAGAGCCCAAGCAGCCTGAGCGCCAGCGTGGGCGACCGCGTAACCATTACTTGTCGGGC IVIA / I / U / 4400 102 TTCCCAAAGCATTAGTAGCTATTTGAATTGGTATCAACAAAAACCAGGCAAGGCCCCAAAGCTGCTGATCTACGCC GCCTCTAGCCTGCAGAGCGGAGTGCCAAGCCGCTTCAGCGGCAGCGGCAGCGGCACCGACTTCACCCTGACCAT CAGCAGCCTGCAGCCAGAGGACTTCGCCACCTACTACTGCCAGCAGAGCTACAGCACCCCACTGA CCTTCGGCCA GGGCACCAAGGTGGAGATCAAGGGTACAGAGGGCAAGTCTAGTGGAAGTGGTAGCGAAAGTAAGAGTACCCAGG TGCAGCTGGTGCAGAGCGGCGCCGAGGTGAAGAAGCCAGGCAGCAGCGTGAAGGTGAGCTGCAAGGCCAGCGG CGGCACCTTCAGCAGCTACGCCATCAGCTGGG TGCGCCAGGCCCCAGGCCAGGGACTGGAGTGGATGGGCGGCA TCATCCCAATCTCGGCACCGCCAACTACGCCCAGAAGTTCCAGGGCCGCGTGACCATCACCGCCGACGAGAGCA CCAGCACCGCCTACATGGAGCTGAGCAGCCTGCGCAGCGAGGACACCGCCGTGTACTACTGCGCACGCGAGAGC CGCTGGCGCGGC TACAAGCTGGACTACTGGGGCCAGGGCACCCTGGTGACCGTGAGCAGCACTAGTACCCCAGC CCCACGCCCTCCCACCCCTGCTCCTACAATAGCATCCCAGCCCTTGTCACTTCGCCCCGAAGCATGCAGACCAGCC GCAGGCGGTGCTGTGCATACCCGAGGACTGGACTTCGCCTGCGAATCTACATCTGGGCCCCACTGGCCG GCAC CTGCGGCGTGCTGCTGCTGAGCCTGGTGATCACCCTGTACTGCAAGCGCGGCCGCAAGAAGCTGCTGTACATCT TCAAGCAGCCATTCATGCGCCCAGTGCAGACCACCCAGGAGGAGGACGGCTGCAGCTGCCGCTTCCCAGAGGAGGAGGAGGGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCC GACGCCCCAGCCTACAAGCAGGGCCAGAA CCAGCTGTACAACGAGCTGAACCTGGGCCGCCGCGAGGAGTACGACGTGCTGGACAAGCGCCGCGGCCGCGACC CAGAGATGGGCGGCAAGCCACGCCGCAAGAACCCACAGGAGGGCCTGTACAACGAGCTGCAGAAGGACAAGATG GCCGAGGCCTACAGCGAGATCGGCATGA AGGGCGAGCGCCGCCGCGGCAAGGGCCACGACGGCCTGTACCAGG GCCTGAGCACCGCCACCAAGGACACCTACGACGCCCTGCACATGCAGGCCCTGCCACCACGC DNA sequence for GC5B596-LH-CDS from ODR000074488 (SEO ID NO: 35) GACATCCAGATGACCCAGAGCCCAAGCAGCCTGAGCGCCAGCGTGGGCGACCGCGTTACAATAACTTGTAAAGCA AGCCAAAATGTTGCTACTCACGTCGGATGGTATCAGCAAAAGCCAGGCAAGGCCCCAAAGCGCCTGATCTACAGC GCCAGCTACCGCTACAGCGGAGTGCCAAGCCGCTTCAGCGGCAGCGGCAGCGGCACCGA GTTCACCCTGACCAT CAGCAACCTGCAGCCAGAGGACTTCGCCACCTACTACTGCCAGCAGTACAACCGCTACCCATACACCTTCGGCCA GGGCACCAAGCTGGAGATCAAGGGrACAGAGGGCAAGTCTAGTGGAAGTGGTAGCGAAAGTAAGAGTACCCAGG TGCAGCTGGTGCAGAGCGGAGCCGAGGTGAAGAAGCCAGGCG CCAGCGTGAAGGTGAGCTGCAAGGCCAGCGG CTACAGCTTCACCGGCTACACCATGAACTGGGTGCGCCAGGCCCCAGGCCAGGGACTGGAGTGGATGGGCCTGA TCAACCCATACAACAGCGAACCAACTACGCCCAGAAGCTGCAGGGCCGCGTGACCATGACCACCGACACCAGCA CCAGCACCGCCTACATGGAGCTGCGCA GCCTGCGCAGCGACGACACCGCCGTGTACTACrGCGCCCGCGTGGCC CTGCGCGTGGCCCTGGACTACTGGGGACAGGGCACCCTGGTGACCGTGAGCAGCACTAGTACCCCAGCCCCACGCCTCCCACCCCTGCrCCTACAATAGCATCCCAGCCCTTGTCACTTCGCCCCGAAGCATGCAGACCAGCCGCAGG CGG TGCTCTGCATACCCGAGGACTGGACTTCGCCTGCGACATCTACATCTGGGCCCCACTGGCCGGCACCTGCG GCGTGCTGCTGCTGAGCCTGGTGATCACCCTGTACTGCAAGCGCGGCCGCAAGAAGCTGCTGTACATCTTCAAGC AGCCATTCATGCGCCCAGTGCAGACCACCCAGGAGGAGGACGGCTGCAGCTGCC GCTTCCCAGAGGAGGAGGAG GGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCCGACGCCCCAGCCTACAAGCAGGGCCAGAACCAGCT 103 GTACAACGAGCTGAACCTGGGCCGCCGCGAGGAGTACGACGTGCTGGACAAGCGCCGCGGCCGCGACCCAGAGA TGGGCGGCAAGCCACGCCGCAAGAACCCACAGGAGGGCCTGTACAACGAGCTGCAGAAGGACAAGATGGCCGAG GCCTACAGCGAGATCGGCATGAAGGGCGAGCGCCGCCGCGGCAAGGGCCACGA CGGCCTGTACCAGGGCCTGAGCACCGCCACCAAGGACACCTACGACGCCCTGCACATGCAGGCCCTGCCACCACGC DNA sequence for GC5B483-HL-CDS from PDR000074483 (SEO ID NO: 36) GAGGTGCAGCTGGTGCAGAGCGGCGCTGAGGTCAAAAAGCCAGGCGAAAGCCTTTAAAATATCATGCAAAGGAAG TGGATATTCCTTTACCAGCTACTTCATCGGCTGGGTGCGCCAGATGCCAGGCAAGGGCCTGGAGTGGATGGGCA TCATCTACCCAGGCAAGAGCGACACCCGCTACAGCCCAAGCTTCCAGGGCCAG GTGACCATCAGCGCCGACAAGA GCATCAGCACCGCCTACCTGCAGTGGAGCAGCCTGAAGGCCAGCGACACCGCCATGTACTACTGCGCCCGCGTGT ACAGCTTCGGCGGCCGCCACAAGGCCCTGTTCGACTACTGGGGCCAGGGCACCCTGGTGACCGTGAGCAGCGGT ACAGAGGGCAAGTCTAGTGGAAGTGGTA GCGAAAGTAAGAGTACCGAGATCGTGCTGACCCAGAGCCCAGCCAC CCTGAGCCTGAGCCCAGGCGAGCGCGCCACCCTGAGCTGCCGCGCCTCTCAGAGCGTGAGCAGCTACCTGGCTT GGTATCAGCAGAAGCCCGGACAGGCCCCACGCCTGCTGATCTACGACGCCAGCAACCGCGACCACCGGCATCCCAG CCCGCTTCAGCGGCAGCG GCAGCGGCACCGACTTCACCCTGACCATCAGCAGCCTGGAGCCAGAGGACTTCGCC GTGTACTACTGCCAGCAGCGCAGCAACTGGCCACTGACCTTCGGCCAGGGCACCAAGGTGGAGATCAAGACTAG TACCCCAGCCCCACGCCCTCCCACCCCTGCTCCTACAATAGCATCCCAGCCCTTGTCACTTCGCCCCGAAGCATGC AGACCAGCC GCAGGCGGTGCTGTGCATACCCGAGGACTGGACTTCGCCTGCGAATCTACATCTGGGCCCCACT GGCCGGCACCTGCGGCGTGCTGCTGCTGAGCCTGGTGATCACCCTGTACTGCAAGCGCGGCCGCAAGAAGCTGC TGTACATCTTCAAGCAGCCATTCATGCGCCCAGTGCAGACCACCCAGGAGGAGGACGG CTGCAGCTGCCGCTTCC CAGAGGAGGAGGAGGGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCCGACGCCCCAGCCTACAAGCA GGGCCAGAACCAGCTGTACAACGAGCTGAACCTGGGCCGCCGCGAGGAGTACGACGTGCTGGACAAGCGCCGCG GCCGCGACCCAGAGATGGGCGGCAAGCCACGCCGCAAGA ACCCACAGGAGGGCCTGTACAACGAGCTGCAGAAG GACAAGATGGCCGAGGCCTACAGCGAGATCGGCATGAAGGGCGAGCGCCGCCGCGGCAAGGGCCACGACGGCC TGTACCAGGGCCTGAGCACCGCCACCAAGGACACCTACGACGCCCTGCACATGCAGGCCCTGCCACCACGC DNA sequence for GC5B81-HL-CDS from PDR000074482 (SEO ID NO: 37) CaggTGCagTGGGTGGagGGCGCGGGTGAAGCCGGCagGGTGGTGGTGTGCCCCCCA GCGGGGCCCCTTTTTCAGCAGCCTGCTGGGTG cutgcagcA cut CCCAATCTCGGCCCCCCCCCCCCAAGITTCCagGCGCGTGCATCCCGCGCGAGGGGGGGCCCCCCCCCTGGGTGGGCCTGCGCGCGGGACCGCGTGTTACTGCGCGCGGGA GAGCCTGGGGCGTACAAGAAGAAGAAGAAGAAG CtggactactgGGGCGGGCCCTGGTGCGTGAGGCGTACAGAGG GGCAAGTTGTGGGGGTGGTAGGCGAAAGTAAGGTACCCCCAGAGACCCAGCCCCAAGGCTGGGGGGGGGGGGCGGCGGCGG TTCCCAAAGCATTAGTATTATTTGTGGTATCA ACAAAACGGCCCCCAAAGCTGTGTGTCCGCCCTCTAGCCTGGCAGGGGGTGCCAAGCGCTTT 104 CAGCGGCAGCGGCAGCGGCACCGACTTCACCCTGACCATCAGCAGCCTGCAGCCAGAGGACTTCGCCACCTACTA CTGCCAGCAGAGCTACAGCACCCCACTGACCTTCGGCCAGGGCACCAAGGTGGAGATCAAGACTAGTACCCCAGCCCACGCCCTCCCACCCCTGCTCCTACAATAGCATCCCAGCCCTTGTCACTTCGCCCCGAAGCAT GCAGACCAGCC GCAGGCGCTGCTGTGCATACCCGAGGACTGGACTTCGCCTGCGAATCTACATCTGGGCCCCACTGGCCGGCAC CTGCGGCGTGCTGCTGCTGAGCCTGGTGATCACCCTGTACTGCAAGCGCGGCCGCAAGAAGCTGCTGTACATCT TCAAGCAGCCATTCATGCGCCCAGTGCAGACCACCCAGGA GGAGGACGGCTGCAGCTGCCGCTTCCCAGAGGAG GAGGAGGGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCCGACGCCCCAGCCTACAAGCAGGGCCAGAA CCAGCTGTACAACGAGCTGAACCTGGGCCGCCGCGAGGAGTACGACGTGCTGGACAAGCGCCGCGGCCGCGACC CAGAGATGGGCGGCAAGCCAC GCCGCAAGAACCCACAGGAGGGCCTGTACAACGAGCTGCAGAAGGACAAGATG GCCGAGGCCTACAGCGAGATCGGCATGAAGGGCGAGCGCCGCCGCGGCAAGGGCCACGACGGCCTGTACCAGGGCCTGAGCACCGCCACCAAGGACACCTACGACGCCCTGCACATGCAGGCCCTGCCACCACGC DNA sequence for GC5B596-HL-CDS from PDR000074481 (SEO ID NO: 38) CAGGTGCAGCTGGTGCAGAGCGGAGCCGAGGTGAAGAAGCCAGGCGCCAGCGTGAAGGTGAGCTGCAAGGCCA GCGGCTACAGCTTCACCGGCTACACCATGAACTGGGTGCGCCAGGCCCCAGGCCAGGGACTGGAGTGGATGGGC CTGATCAACCCATACAACAGCGACACCAACTACGCCCAGAAGCTGCAGG GCCGCGTGACCATGACCACCGACACC AGCACCAGCACCGCCTACATGGAGCTGCGCAGCCTGCGCAGCGACGACACCGCCGTGTACTACTGCGCCCGCGT GGCCCTGCGCGTGGCCCTGGACTACTGGGGACAGGGCACCCTGGTGACCGTGAGCAGCGCTACAGAGGGCAAG TCTAGTGGAAGTGGTAGCGAAAGTA AGAGTACCGACATCCAGATGACCCAGAGCCCAAGCAGCCTGAGCGCCAG CGTGGGCGACCGCGnTACAATAACTTGTAAAGCAAGCCAAAATGnTGCTACTCACGTCGGATGGTATCAGCAAAA GCCAGGCAAGGCCCCAAAGCGCCTGATCTACAGCGCCAGCTACCGCTACAGCGGAGTGCCAAGCCGCTTCAGCGGCAGCGGCAGCG GCACCGAGTTCACCCTGACCATCAGCAACCTGCAGCCAGAGGACTTCGCCACCTACTACTGCC AGCAGTACAACCGCTACCCATACACCTTCGGCCAGGGCACCAAGCTGGAGATCAAGACTAGTACCCCAGCCCCAC GCCCTCCCACCCCTGCTCCTACAATAGCATCCCAGCCCTTGTCACTTCGCCCCGAAGCATGCAGACCAGCCGCAG GCGGTGCT GTGCATACCCGAGGACTGGACTTCGCCTGCGAATCTACATCTGGGCCCCACTGGCCGGCACCrGC GGCGTGCTGCTGCTGAGCCTGGTGATCACCCTGTACTGCAAGCGCGGCCGCAAGAAGCrGCTGTACATCTCAA GCAGCCATTCATGCGCCCAGTGCAGACCACCCAGGAGGAGGACGGCTGCAGCTGCC GCTTCCCAGAGGAGGAGG AGGGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCCGACGCCCCAGCCTACAAGCAGGGCCAGAACCAG CTGTACAACGAGCTGAACCTGGGCCGCCGCGAGGAGTACGACGTGCTGGACAAGCGCCGCGGCCGCGACCCAGA GATGGGCGGCAAGCCACGCCGCAAGAACCCACAGGA GGGCCTGTACAACGAGCTGCAGAAGGACAAGATGGCCG AGGCCTACAGCGAGATCGGCATGAAGGGCGAGCGCCGCCGCGGCAAGGGCCACGACGGCCTGTACCAGGGCCT GAGCACCGCCACCAAGGACACCrACGACGCCCTGCACATGCAGGCCCTGCCACCACGC 105 HCDR1 (GC5B81) (SEO ID NO: 39) GGTFSSY HCDR2 (GC5B81) (SEO ID NO: 40) ESRWRGYKLDY HCDR3 (GC5B81) (SEO ID NO: 41) IPIFGT HCDR1 (GC5B483) (SEO ID NO: 42) GYSFTSY HCDR2 (GC5B483) (SEO ID NO: 43) YPGKSD HCDR3 (GC5B483) (SEO ID NO: 44) VYSFGGRHKALFDY HCDR1 (GC5B596) (SEO ID NO: 45) GYSFTGY HCDR2 (GC5B596) (SEO ID NO: 46) NPYNSD HCDR3 (GC5B596) (SEO ID NO: 47) VALRVALDY LCDR1 (GC5B81) (SEO ID NO: 48) RASQSISSYLN LCDR2 (GC5B81) (SEO ID NO: 49) AASSLQS LCDR3 (GC5B81) (SEO ID NO: 50) QQSYSTPLT 106 LCDR1 (GC5B4831 (SEO ID NO: 511 RASQSVSSYLA LCDR2 (GC5B4831 (SEO ID NO: 521 DASNRAT LCDR3 (GC5B4831 (SEO ID NO: 531 QQRSNWPLT LCDR1 (GC5B5961 (SEO ID NO: 541 KASQNVATHVG LCDR2 (GC5B5961 (SEO ID NO: 551 SASYRYS LCDR3 (GC5B5961 (SEO ID NO: 561 QQYNRYPYT Human GPRC5D polypeptide (SEO ID NO: 571 MYKDCIESTGDYFLLCDAEGPWGIILESLAILGIWTILLLAFLFLMRKIQDCSQWNVLPTQLLFLLSVLGLFGLA FAFIIELNQQTAPVRYFLFGVLFALCFSCLLAHASNLVKLVRGCVSFSWTTILCIAIGCSLLQIIIATEYVTLIMTRG MMFVNMTPCQLNVDFVVLLVYVLFLMALTFFVS KATFCGPCENWKQHGRLIFITVLFSIIIWWWISMLLRGNP QFQRQPQWDDPWCIALVTNAWVFLLLYIVPELCILYRSCRQECPLQGNACPVTAYQHSFQVENQELSRARDS DGAEEDVALTSYGTPIQPQTVDPTQECFIPQAKLSPQQDAGGV HCDR1 (GP5B831 (SEO ID NO: 581 GGSLSSSSY HCDR2 (GP5B831 (SEO ID NO: 591 YYSGN HCDR3 (GP5B831 (SEO ID NO: 601 HVGYSYGRRFWYFDL LCDR1 (GP5B831 (SEO ID NO: 611 RASQSVSSYLA Ma / E / ZUZI / U / 4400 107 LCDR2 (GP5B83) (SEO ID NO: 621 DASNRAT LCDR3 (GP5B83) (SEO ID NO: 631 QQRSNWPPT Heavy chain sequence (GP5B83) (SEO ID NO: 64) QLQLQESGPGLVKPSETLSLTCTVSGGSLSSSSYWWGWTRQPPGRGLEWIGTMYYSGNIYYNPSLQSRATISV DTSKNQFSLKLSSVTAADTAVYYCARHVGYSYGRRFWYFDLWGRGTLVTVSS Light chain sequence (GP5B83) (SEO ID NO: 65) EIVLTQSPATLSSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTI SSLEPEDFAVYYCQQRSNWPPTFGQGTKVEIK HCDR1 (GC5B680) (SEO ID NO: 66) GFSLTNIRM HCDR2 (GC5B680) (SEO ID NO: 67) FSNDE HCDR3 (GC5B680) (SEO ID NO: 68) MRLPYGMDV LCDR1 (GC5B680) (SEO ID NO: 69) RSSQSLVHSDGNTYLS LCDR2 (GC5B680) (SEO ID NO: 70) KISNRFF LCDR3 (GC5B680) (SEO ID NO: 71) MQATQFPHT Heavy chain sequence (GC5B680) (SEO ID NO: 72) QVTLKESGPVLVKPTETLTLTCTVSGFSLTNIRMSVSWIRQPPGKALEWLAHIFSNDEKSYSSSLKSRLTISRDT SKSQWLTLTNVDPVDTATYYCARMRLPYGMDVWGQGTTVTVSS MA / t / ZUZI / U / 4400 108 Light chain sequence (GC5B680) (SEO ID NO: 73) DIVMTQTPLSSPVTLGQPASISCRSSQSLVHSDGNTYLSWLQQRPGQPPRLLIYKISNRFFGVPDRFSGSGAGT DFTLKISRVEAEDVGVYYCMQATQFPHTFGQGTKLEIK Linker polypeptide sequence (SEO ID NO: 74) GGSEGKSSGSGSSESKSTGGS scFv sequence (GP5B83-HL) (SEO ID NO: 75) QLQLQESGPGLVKPSETLSLTCTVSGGSSLSSSSYWWGWTRQPPGRGLEWIGTMYYSGNIYYNPSLQSRATISV DTSKNQFSLKLSSVTAADTAVYYCARHVGYSYGRRFWYFDLWGRGTLVTVSSGGSEGKSSGSGSESKSTGGSE IVLTQSPATLSLSPGERATLSCRASQSVSSYLAW YQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTIS SLEPEDFAVYYCQQRSNWPPTFGQGTKVEIK scFv sequence (GP5B83-LH) (SEO ID NO: 76) EIVLTQSPATLSSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTI SSLEPEDFAVYYCQQRSNWPPTFGQGTKVEIKGGSEGKSSGSGSESKSTGGSQLQLQESGPGLVKPSETLSLTC TVSGGSSLSSSYWWGWTRQPPGRGLEWIGTMYYSG NIYYNPSLQSRATISVDTSKNQFSLKLSSVTAADTAV YYCARHVGYSYGRRFWYFDLWGRGTLVTVSS scFv sequence (GC5B680-HL) (SEO ID NO: 77) QVTLKESGPVLVKPTETLTLTCTVSGFSLTNIRMSVSWIRQPPGKALEWLAHIFSNDEKSYSSSLKSRLTISRDT SKSQWLTLTNVDPVDTATYYCARMRLPYGMDVWGQGTTVTVSSGGSEGKSSGSGSESKSTGGSDIVMTQTP LSSPVTLGQPASISCRSSQSLVHSDGNTYLSWLQQRPGQ PPRLLIYKISNRFFGVPDRFSGSGAGTDFTLKISRV EAEDVGVYYCMQATQFPHTFGQGTKLEIK scFv sequence (GC5B680-LH) (SEO ID NO: 78) DIVMTQTPLSSPVTLGQPASISCRSSQSLVHSDGNTYLSWLQQRPGQPPRLLIYKISNRFFGVPDRFSGSGAGT DFTLKISRVEAEDVGVYYCMQATQFPHTFGQGTKLEIKGGSEGKSSGSGSESKSTGGSQVTLKESGPVLVKPTE TLTLTCTVSGFSLTNIRMSVSWIRQPPGKALEW LAHIFSNDEKSYSSSLKSRLTISRDTSKSQVVLTLTNVDPVD TATYYCARMRLPYGMDVWGQGTTVTVSS Extracellular binding domain (GP5B83-HL) (SEO ID NO: 79) MAWVWTLFLMAAAQSIQAQLQLQESGPGLVKPSETLSLTCTVSGGSLSSSSYWWGWTRQPPGRGLEWIGT MYYSGNIYYNPSLQSRATISVDTSKNQFSLKLSSVTAADTAVYYCARHVGYSYGRRFWYFDLWGRGTLVTVSS GGSEGKSSGSGSESKSTGGSEIVLTQSPATLS LSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNR MA / t / ZUZI / U / 4400 109 ATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPPTFGQGTKVEIK Extracellular binding domain (GP5B83-LH) (SEO ID NO: 80) MAWVWTLFLMAAAQSIQAEIVLTQSPATLSSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNR ATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQRSNWPPTFGQGTKVEIKGGSEGKSSGSGSESKSTGGSQ LQLQESGPGLVKPSETLSLTCTVSGGSLSSSSYWW GWTRQPPGRGLEWIGTMYYSGNIYYNPSLQSRATISVD TSKNQFSLKLSSVTAADTAVYYCARHVGYSYGRRFWYFDLWGRGTLVTVSS Extracellular binding domain (GC5B680-HL) (SEO ID NO: 81) MAWVWTLFLMAAAQSIQAQVTLKESGPVLVKPTETLTLTCTVSGFSLTNIRMSVSWIRQPPGKALEWLAHIFS NDEKSYSSSLKSRLTISRDTSKSQWLTLTNVDPVDTATYYCARMRLPYGMDVWGQGTTVTVSSGGSEGKSSG SGSESKSTGGSDIVMTQTPLSSPVTLGQPASISCRSSQSL VHSDGNTYLSWLQQRPGQPPRLLIYKISNRFFGV PDRFSGSGAGTDFTLKISRVEAEDVGVYYCMQATQFPHTFGQGTKLEIK Extracellular binding domain (GC5B680-LH) (SEO ID NO: 82) MAWVWTLFLMAAAQSIQADIVMTQTPLSSPVTLGQPASISCRSSQSLVHSDGNTYLSWLQQRPGQPPRLLIY KISNRFFGVPDRFSGSGAGTDFTLKISRVEAEDVGVYYCMQATQFPHTFGQGTKLEIKGGSEGKSSGSGSESKS TGGSQVTLKESGPVLVKPTETLTLTCTVSGFSLTNI RMSVSWIRQPPGKALEWLAHIFSNDEKSYSSSLKSRLTI SRDTSKSQVVLTLTNVDPVDTATYYCARMRLPYGMDVWGQGTTVTVSS Sequence of GP5B83-HL-CAR (SEO ID NO: 83) QLQLQESGPGLVKPSETLSLTCTVSGGSSLSSSSYWWGWTRQPPGRGLEWIGTMYYSGNIYYNPSLQSRATISV DTSKNQFSLKLSSVTAADTAVYYCARHVGYSYGRRFWYFDLWGRGTLVTVSSGGSEGKSSGSGSESKSTGGSE IVLTQSPATLSLSPGERATLSCRASQSVSSYLAW YQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTIS SLEPEDFAVYYCQQRSNWPPTFGQGTKVEIKTSTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFA CDIYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCELRVKFSRS ADAPAY KQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEIGMKGE RRRGKGHHDGLYQGLSTATKDTYDALHMQALPPR Sequence of GP5B83-LH-CAR (SEO ID NO: 84) EIVLTQSPATLSSLSPGERATLSCRASQSVSSYLAWYQQKPGQAPRLLIYDASNRATGIPARFSGSGSGTDFTLTI SSLEPEDFAVYYCQQRSNWPPTFGQGTKVEIKGGSEGKSSGSGSESKSTGGSQLQLQESGPGLVKPSETLSLTC TVSGGSSLSSSYWWGWTRQPPGRGLEWIGTMYYSG SADAPAY KQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEIGMKG ΜΛ / t / ZUZ I / U / 4400 110 ERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR Sequence of GC5B680-HL-CAR (SEO ID NO: 85) QVTLKESGPVLVKPTETLTLTCTVSGFSLTNIRMSVSWIRQPPGKALEWLAHIFSNDEKSYSSSLKSRLTISRDT SKSQWLTLTNVDPVDTATYYCARMRLPYGMDVWGQGTTVTVSSGGSEGKSSGSGSESKSTGGSDIVMTQTP LSSPVTLGQPASISCRSSQSLVHSDGNTYLSWLQQRPGQ PPRLLIYKISNRFFGVPDRFSGSGAGTDFTLKISRV EAEDVGVYYCMQATQFPHTFGQGTKLEIKTSTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACD IYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCELRVKFSRSAD APAYKQG QNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEIGMKGERR RGKGHHDGLYQGLSTATKDTYDALHMQALPPR Sequence of GC5B680-LH-CAR(SEQ ID NO: 86) DIVMTQTPLSSPVTLGQPASISCRSSQSLVHSDGNTYLSWLQQRPGQPPRLLIYKISNRFFGVPDRFSGSGAGT DFTLKISRVEAEDVGVYYCMQATQFPHTFGQGTKLEIKGGSEGKSSGSGSESKSTGGSQVTLKESGPVLVKPTE TLTLTCTVSGFSLTNIRMSVSWIRQPPGKALEW LAHIFSNDEKSYSSSLKSRLTISRDTSKSQVVLTLTNVDPVD TATYYCARMRLPYGMDVWGQGTTVTVSSTSTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACD IYIWAPLAGTCGVLLLSLVITLYCKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCELRVKFSRSAD APAYK QGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPRRKNPQEGLYNELQKDKMAEAYSEIGMKGERR RGKGHHDGLYQGLSTATKDTYDALHMQALPPR DNA sequence for Sequence of GP5B83-HL from dDR000084454 (SEO ID NO: 87) ATGGCTTGGGTGTGGACCTTGCTATTCCTGATGGCAGCTGCCCAAAGTATACAGGCCCAACTCCAGCTGCAAGAA TCTGGTCCTGGACTCGTAAAACCATCAGAAACCCTCTCATTGACCTGCACAGTGAGTGGTGGATCATTGTCTTCC AGCAGCTATTGGTGGGGGTGGACTCGACAGCCACCAGGTC GCGGTCTCGAGTGGATAGGTACAATGTATTACAG TGGTAACATTTATTACAACCCTAGCCTCCAAAGCCGGGCAACCATCrCTGTTGACACATCCAAGAATCAATTTAGC CTGAAATTGTCTAGTGTGACTGCTGCTGATACAGCTGTTTATTATTGCGCTAGGCATGTCGGATACTCTTATGGT CGTAGATTCTGGTACT TCGATTTGTGGGGTCGCGGGACCTTGGTAACAGTCTCCTCCGGAGGATCAGAGGGGAA ATCTTCCGGTAGCGGCAGTGAATCAAAGTCAACTGGTGGTTCCGAAATCGTGCTGACTCAGTCACCCGCAACTCT TTCACTGAGTCCTGGAGAACGTGCTACrCTGTCATGTCGGGCTTCTCAGTCAGTAAGTTCTTATTTG GCATGGTA CCAGCAAAAGCCCGGCCAAGCCCCCCGACTCTTGATATACGATGCATCAAACCGTGCCACTGGAATCCCAGCACGTTTTTCCGGAAGTGGTTCCGGAACCGACTTCACCCTCACCATATCCAGTTTGGAGCCCGAGGACTTCGCAGTTTA CTATTGTCAACAACGGTCCAACTGGCCCCCCACATTTGGACAAGGCACCAAAGTCGAAATA AAGACTAGTACCCCA GCCCCACGCCCTCCCACCCCTGCTCCTACAATAGCATCCCAGCCCTTGTCACrTCGCCCCGAAGCATGCAGACCAG CCGCAGGCGGTGCTGTGCATACCCGAGGACTGGACTTCGCCTGCGAACATCTACATCTGGGCCCCACTGGCCGGC 111 ACCTGCGGCGTGCTGCTGCTGAGCCTGGTGATCACCCTGTACTGCAAGCGCGGCCGCAAGAAGCTGCTGTACAT CTTCAAGCAGCCATTCATGCGCCCAGTGCAGACCACCCAGGAGGAGGACGGCTGCAGCTGCCGCTTCCCAGAGG AGGAGGAGGGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCCGA CGCCCCAGCCTACAAGCAGGGCCA GAACCAGCTGTACAACGAGCTGAACGTGGGCCGCCGCGAGGAGTACGACGTGCTGGACAAGCGCCGCGGCCGCG ACCCAGAGATGGGCGGCAAGCCACGCCGCAAGAACCCACAGGAGGGCCTGTACAACGAGCrGCAGAAGGACAAG ATGGCCGAGGCCTACAGCGAGATCGGC ATGAAGGGCGAGCGCCGCCGCGGCAAGGGCCACGACGGCCTGTACCA GGGCCTGAGCACCGCCACCAAGGACACCTACGACGCCCTGCACATGCAGGCCCTGCCACCACGCTGA DNA sequence for Sequence of GP5B83-LH (SEO ID NO: 88) ATGGCTTGGGTGTGGACCTTGCTATTCCTGATGGCAGCTGCCCAAAGTATACAGGCCGAAATCGTACTGACTCAA AGTCCCGCTACTCTCAGTCTGTCACCCGGCGAGAGCCACACTGTCATGCCGCGCCAGCCAATCAGTCAGnTCC TACCTTGCTTGGTATCAGCAGAAACCTGGCCAAGCACCTCGGCTGCT TATCTACGACGCCAGCAATCGCGCCACT GGTATCCCAGCTCGGTTTTCAGGTAGCGGCAGTGGGACAGACTTTTACCTTGACTATTAGCTTCTCTTGAACCCGAA GACTTTGCCGTTTATTACTGCCAGCAACGGTCAAACTGGCCTCCCACTTTTGGCCAAGGAACCAAAGTAGAGATA AAAGGTGGTTCAGAAGGTAAATCAAGTGGGTC CGGTTCCGAAAGTAAGTCCACCGGAGGCTCTCAACTCCAGTTG CAGGAAAGTGGGCCTGGGCTTGTAAAACCAAGCGAGACATTGTCTCTCACATGCACTGTATCAGGGGGATCTCTT TCAAGTTCCTCTTATTGGTGGGGGTGGACTCGTCAACCCCCCGGTAGGGGTCTCGAATGGATCGGTACCATGTAT TATT CTGGGAATATATACTATAATCCAAGCCTTCAAAGTAGAGCTACTATATCCGTGGACACATCCAAGAATCAGT TCTCCTTGAAACTTTCTAGCGTGACCGCCGCCGATACTGCTGTCTACTACTGCGCACGGCATGTGGGATACTCCT ACGGGAGACGGrrCTGCTATTTCGACTTCTGGGCTCGCGGTACACTCGTTACACTGTCCTCTACTAGTACCCC AG CCCCACGCCCTCCCACCCCTGCTCCTACAATAGCATCCCAGCCCTTGTCACTTCGCCCCGAAGCATGCAGACCAGC CGCAGGCGGTGCTGTGCATACCCGAGGACTGGACTTCGCCTGCGAACATCTACATCTGGGCCCCACTGGCCGGCA CCTGCGGCGTGCTGCTGCTGAGCCTGGTGATCACCCTGTACTGCAAGCGCG GCCGCAAGAAGCTGCTGTACATC TTCAAGCAGCCATTCATGCGCCCAGTGCAGACCACCCAGGAGGAGGACGGCTGCAGCTGCCGCTTCCCAGAGGA GGAGGAGGGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCCGACGCCCCAGCCTACAAGCAGGGCCAG AACCAGCTGTACAACGAGCTGAACCTGGGCCGCC GCGAGGAGTACGACGTGCTGGACAAGCGCCGCGGCCGCGA CCCAGAGATGGGCGGCAAGCCACGCCGCAAGAACCCACAGGAGGGCCTGTACAACGAGCTGCAGAAGGACAAGA TGGCCGAGGCCTACAGCGAGATCGGCATGAAGGGCGACGCCGCCGCGGCAAGGGCCACGACGGCCTGTACCA GGGCCTGAG CACCGCCACCAAGGACACCTACGACGCCCTGCACATGCAGGCCCTGCCACCACGCTGA DNA sequence for Sequence of GC5B680-HL (SEO ID NO: 89) ATGGCTTGGGTGTGGACCTTGCTATTCCTGATGGCAGCTGCCCAAAGTATACAGGCCCAAGTAACACTCAAGGAG AGCGGACCAGTCTTGGTGAAACCAACTGAGACCTTGACTTTGACATGTACTGTAAGTGGCTTCAGCCTTACCAAC 112 ATCAGGATCTCAGTATCTTGGATAAGGCAACCACCTGGCAAGGCACTCGAATGGCTGGCACACATCTTTTCTAAC GACGAAAAATCCTATTCTTCCAGTCTCAAAAGTCGCCTTACCATCAGCCGAGATACCAGTAAGAGTCAAGTAGTTC TTACATTGACCAATGTAGATCCAGTTGATACAGCCACATACTACTGCGCACGAATGCGGCTTCCATA CGGCATGG ATGTATGGGGACAGGGAACTACTGTTACCGTTAGTTCCGGCGGCTCCGAGGGCAAGAGCAGCGGCAGCGGCAGC GAGAGCAAGAGCACCGGCGGCAGCGACATTGTGATGACCCAAACACCTCTTAGTAGTCCTGTAACTCTCGGACAG CCAGCTTCAATATCTTGTCGCTCAAGTCAATCCCTCGTCCATTCCGACGG CAACACCTACCTTCTCTTGGCTCCAAC AGAGACCCGGCCAGCCTCCCAGACTTCTCATCTACAAAATCAGTAACAGGTTCTTCGGCGTCCCTGACAGGTTCA GTGGATCTGGAGCAGGTACAGATTTCACCTTGAAGATAAGTAGAGTGGAGGCTGAGGACGTAGGCGTCTATTAT TGTATGCAAGCTACCCAATTCCCACATACATTCGGCCAAG GCACTAAATTGGAAATAAAAACTAGTACCCCAGCCC CACGCCCTCCCACCCCTGCTCCTACAATAGCATCCCAGCCCTTGTCACTTCGCCCCGAAGCATGCAGACCAGCCGC AGGCGGTGCTGTGCATACCCGAGGACTGGACTTCGCCTGCGACATCTACATCTGGGCCCCACTGGCCGGCACCT GCGGCGTGCTGCTGCTGAGC CTGGTGATCACCCTGTACTGCAAGCGCGGCCGCAAGAAGCTGCTGTACATCTTC AAGCAGCCATTCATGCGCCCAGTGCAGACCACCCAGGAGGAGGACGGCTGCAGCTGCCGCTTCCCAGAGGAGGA GGAGGGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCCGACGCCCCAGCCTACAAGCAGGGCCAGAACC AG CTGTACAACGAGCTGAACCTGGGCCGCCGCGAGGAGTACGACGTGCTGGACAAGCGCCGCGGCCGCGACCCA GAGATGGGCGGCAAGCCACGCCGCAAGAACCCACAGGAGGGCCTGTACAACGAGCTGCAGAAGGACAAGATGGC CGAGGCCTACAGCGAGATCGGCATGAAGGGCGACGCCGCCGCGGCAAGGGCC ACGACGGCCTGTACCAGGGC CTGAGCACCGCCACCAAGGACACCTACGACGCCCTGCACATGCAGGCCCTGCCACCACGCTGA DNA sequence for Sequence of GC5B680-LH (SEO ID NO: 90) ATGGCTTGGGTGTGGACCTTGCTATTCCTGATGGCAGCTGCCCAAAGTATACAGGCCGACATTGTGATGACCCAA ACACCTCTTAGTAGTCCTGTAACTCTCGGACAGCCAGCTTCAATATCTTGTCGCTCAAGTCAATCCCTCGTCCATT CCGACGGCAACACCTACTCTCTTGGCrCCAACAGAGACCCGGCCAGCCTCCCAG ACTTCTCATCTACAAAATCAG TAACAGGTTCTTCGGCGTCCCTGACAGGTTCAgrGGATCTGGAGCAGGTACAGATTTCACCTTGAAGATAAGrAG AGTGGAGGCTGAGGACGTAGGCGTCTATTATTGTATGCAAGCTACCCAATTCCCACATACATTCGGCCAAGGCAC TAAATTGGAAATAAAAGGCGGCTCCGAGGGCAAG AGCAGCGGCAGCGGCAGCGAGAGCAAGAGCACCGGCGGCA GCCAAGTAACACTCAAGGAGAGCGGACCAGTCTTGGTGAAACCAACTGAGACCTTGACTTTGACATGTACTGTAA GTGGCTTCAGCCTTACCAACATCAGGATGTCAGTATCTTGGATAAGGCAACCACCTGGCAAGGCACTCGAATGGC TGGCACACATCTTTTCTAACG ACGAAAAATCCTATTCTTCCAGTCTCAAAAAGTCGCCTTACCATCAGCCGAGATAC CAGTAAGAGTCAAGTAGTTCTrACATTGACCAATGTAGATCCAGiTTGATACAGCCACATACTACTGCGCACGAAT GCGGCTTCCATACGGCATGGATGTATGGGGACAGGGAACTACTGTTACCGTTAGTTCCACTAGTACCCCAGCCCC ACGCCCTCCCACCC CTGCTCCTACAATAGCATCCCAGCCCTTGTCACTTCGCCCCGAAGCATGCAGACCAGCCGCA GGCGGTGCTGTGCATACCCGAGGACTGGACTTCGCCTGCGAACATCTACATCTGGGCCCCACTGGCCGGCACCTG CGGCGTGCTGCTGCTGAGCCTGGTGATCACCCTGTACTGCAAGCGCGGCCGCAAGAAGCTGCTG TACATCTTCAA GCAGCCATTCATGCGCCCAGTGCAGACCACCCAGGAGGAGGACGGCTGCAGCTGCCGCTTCCCAGAGGAGGAGG 113 AGGGCGGCTGCGAGCTGCGCGTGAAGTTCAGCCGCAGCGCCGACGCCCCAGCCTACAAGCAGGGCCAGAACCAG CTGTACAACGAGCTGAACCTGGGCCGCCGCGAGGAGTACGACGTGCTGGACAAGCGCCGCGGCCGCGACCCAGA GATGGGCGGCAAGCCACGCCGCAAGAACCCACAGGAGGGCCTGTACAACGA GCTGCAGAAGGACAAGATGGCCG AGGCCTACAGCGAGATCGGCATGAAGGGCGAGCGCCGCCGCGGCAAGGGCCACGACGGCCTGTACCAGGGCCT GAGCACCGCCACCAAGGACACCTACGACGCCCTGCACATGCAGGCCCTGCCACCACGCTGA Linker sequence (SEO ID NO: 91) GGSEGKSSGSGSSESKSTGGS Linker sequence (SEO ID NO: 92) GGGSGGGS Linker sequence (SEO ID NO: 93) GGGSGGGSGGGS Linker sequence (SEO ID NO: 94) GGGSGGGSGGGSGGGS Linker sequence (SEO ID NO: 95) GGGSGGGSGGGSGGGSGGGS Linker sequence (SEO ID NO: 96) GGGGSGGGGSGGGGS Linker sequence (SEO ID NO: 97) GGGGSGGGGSGGGGSGGGGS Linker sequence (SEO ID NO: 98) GGGGSGGGGSGGGGSGGGGSGGGGS Linker sequence (SEO ID NO: 99) GSTSGSGKPGSGEGSTKG Linker sequence (SEO ID NO: 100) IRPRAIGGSKPRVA ΜΛ / t / ZUZ I / U / 4400 114 Linker sequence (SEO ID NO: 101) GKGGSGKGGSGKGGS Linker sequence (SEO ID NO: 102) GGKGSGGKGSGGKGS Linker sequence (SEO ID NO: 103) GGGKSGGGKSGGGKS Linker sequence (SEO ID NO: 104) GKGKSGKGKSGKGKS Linker sequence (SEO ID NO: 105) GGGKSGGKGSGKGGS Linker sequence (SEO ID NO: 106) GKPGSGKPGSGKPGS Linker sequence (SEO ID NO: 107) GKPGSGKPGSGKPGSGKPGS Linker sequence (SEO ID NO: 108) GKGKSGKGKSGKGKSGKGKS Linker sequence (SEO ID NO: 109) STAGDTHLGGEDFD Linker sequence (SEO ID NO: 110) GEGGSGEGGSGEGGS Linker sequence (SEO ID NO: 111) GGEGSGGEGSGGEGS Linker sequence (SEO ID NO: 112) GEGESGEGESGEGES 115 Linker sequence (SEO ID NO: 113) GGGESGGEGSGEGGS Linker sequence (SEO ID NO: 114) GEGESGEGESGEGESGEGES Linker sequence (SEO ID NO: 115) GSTSGSGKPGSGEGSTKG Linker sequence (SEO ID NO: 116) PRGASKSGSASQTGSAPGS Linker sequence (SEO ID NO: 117) GTAAAGAGAAGGAAAGAAG Linker sequence (SEO ID NO: 118) GTSGSSGSGSGGSGSGGGG Linker sequence (SEO ID NO: 119) GKPGSGKPGSGKPGSGKPGS Linker sequence (SEO ID NO: 120) GSGS Linker sequence (SEO ID NO: 121) APAPAPAPAP Linker sequence (SEO ID NO: 122) PAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAPAD Linker sequence (SEO ID NO: 123) AEAAAKEAAAAKEAAAAAKEAAAAAKEAAAAAKAAA Hinge sequence (SEO ID NO: 124) EPKSCDKTHTCPPCP / U / 4400 116 Hinge sequence (SEO ID NO: 125) ERKCCVECPPCP Hinge sequence (SEO ID NO: 126) ELKTPLGDTTHTCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCP Hinge sequence (SEO ID NO: 127) ESKYGPPCPSCP MA / t / ZUZI / U / 4400

Claims

CLAIMS 1. A chimeric antigen receptor (CAR), comprising an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain, wherein the extracellular antigen-binding domain comprises: a heavy-chain complementarity-determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 66, a heavy-chain CDR2 having the amino acid sequence of SEQ ID NO: 67, and a heavy-chain CDR3 having the amino acid sequence of SEQ ID NO: 68; a heavy-chain complementarity-determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 58, a heavy-chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and a heavy-chain CDR3 having the amino acid sequence of SEQ ID NO: 60;a heavy chain complementarity-determining region 1 (CDR1) having the amino acid sequence of SEQ ID NO: 39, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 41; a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 43, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 44; or a heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 45, a heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and a heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 47; where the extracellular antigen-binding domain binds to the antigen of the group 5 family C anti-G protein receptor member D (GPRC5D).; 2. The CAR according to claim 1, further characterized in that the extracellular antigen-binding domain comprises the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 66, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 67, and the heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 68, and further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 69, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 70, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 71;The extracellular antigen-binding domain comprises the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 58, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 59, and the heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 60, and further comprises a light chain / U / 4400 118 CDR1 having the amino acid sequence of SEQ ID NO: 61, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 62, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 63;The extracellular antigen-binding domain comprises the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 39, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 40, and the heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 41, and further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 48, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 49, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 50;The extracellular antigen-binding domain comprises the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 42, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 43, and the heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 44, and further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 51, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 52, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 53;or the extracellular antigen-binding domain comprises the heavy chain CDR1 having the amino acid sequence of SEQ ID NO: 45, the heavy chain CDR2 having the amino acid sequence of SEQ ID NO: 46, and the heavy chain CDR3 having the amino acid sequence of SEQ ID NO: 47, and further comprises a light chain CDR1 having the amino acid sequence of SEQ ID NO: 54, a light chain CDR2 having the amino acid sequence of SEQ ID NO: 55, and a light chain CDR3 having the amino acid sequence of SEQ ID NO: 56.; 3. The CAR according to claim 1 or 2, further characterized in that the extracellular antigen-binding domain comprises a light chain variable region (LCVR) comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 73, 65, 1, 3 and 5, or a heavy chain variable region (HCVR) comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 72, 64, 2, 4, and 6, or a combination of an LCVR comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 73, 65, 1, 3 and 5, and an HCVR comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 72, 64, 2, 4, and 6.

4. The CAR according to claims 1 to 3, further characterized in that the extracellular antigen-binding domain comprises: a light chain variable region comprising an amino acid sequence of SEQ ID NO: 73 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 72; a light chain variable region comprising an amino acid sequence of SEQ ID NO: 65 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 64; a light chain variable region comprising an amino acid sequence of SEQ ID NO: 1 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 2; a light chain variable region comprising an amino acid sequence of SEQ ID NO: 3 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 4;or a light chain variable region comprising an amino acid sequence of SEQ ID NO: 5 and a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 6.; 5. The CAR according to any of claims 1 to 4, further characterized in that the extracellular antigen-binding domain comprises a single-chain variable fragment (scFv).

6. The CAR according to claim 5, characterized in that the scFv comprises a linking polypeptide between the light chain variable region and the heavy chain variable region. 7.- The CAR according to claim 6, further characterized in that the linking polypeptide comprises an amino acid sequence of SEQ ID NO:

7.

8. The CAR according to any of claims 5 to 7, further characterized in that the scFv comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 78, 77, 75, 76, 8, 9, 10, 24, 25, and 26.

9. The CAR in accordance with any of claims 1 to 8, further characterized in that the extracellular antigen-binding domain comprises a signal polypeptide.

10. The CAR according to claim 9, further characterized in that the signal polypeptide comprises an amino acid sequence of SEQ ID NO:

11. 11.- The CAR according to any of claims 1 to 10, further characterized in that the intracellular signaling domain comprises a polypeptide component selected from the group consisting of a TNF receptor superfamily member 9 (CD137) component, a CD3 (CD3z) T cell surface glycoprotein zeta chain component, a differentiation component (CD27) cluster, a differentiation superfamily member component cluster, and a combination thereof. 12.- The CAR according to claim 11, further characterized in that the CD137 component comprises an amino acid sequence of SEQ ID NO:

12. 13.- The CAR according to claim 11, further characterized in that the CD3z component comprises an amino acid sequence of SEQ ID NO:

13. 14.- The CAR according to claim 11, further characterized in that the MA / t / ZUZI / U / 4400 120 intercellular signaling domain comprises an amino acid sequence of SEQ ID NO:

14.

15. The CAR according to any of claims 1 to 14, further characterized in that the transmembrane domain comprises a polypeptide of the CD8a transmembrane region (CD8a-TM).

16. The CAR according to claim 15, further characterized in that the CD8a-TM polypeptide comprises an amino acid sequence of SEQ ID NO:

15.

17. The CAR according to any of claims 1 to 16, further characterized in that it additionally comprises a hinge region connecting the transmembrane domain to the extracellular antigen-binding domain. 18.- The CAR according to claim 17, further characterized in that the hinge region is a hinge region CD8a.

19. The CAR according to claim 18, further characterized in that the hinge region CD8a comprises an amino acid sequence of SEQ ID NO:

16.

20. The CAR according to any of claims 1 to 19, further characterized in that the extracellular antigen-binding domain comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 82, 81, 80, 79, 17, 18, 19, 20, 21, and 22.

21. The CAR according to any of claims 1 to 20, further characterized in that the CAR comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 86, 85, 83, 84, 27, 28, 29, 30, 31 and 32. 22 - An isolated lymphocyte expressing the CAR in accordance with any of claims 1 to 21.

23. The isolated lymphocyte according to claim 22, further characterized in that the lymphocyte is a T lymphocyte.

24. The isolated lymphocyte according to claim 23, further characterized in that the T lymphocyte is a naive T cell.

25. The isolated lymphocyte according to claim 23, further characterized in that the T lymphocyte is a memory stem T cell.

26. The isolated lymphocyte according to claim 23, further characterized in that the T lymphocyte is a central memory T cell.

27. The isolated lymphocyte in accordance with any of claims 23 to 26, further characterized in that the T lymphocyte is CD4+.

28. The isolated lymphocyte in accordance with any of claims 23 to 26, further characterized in that the T lymphocyte is CD8+.

29. The isolated lymphocyte in accordance with any of claims 23 to MA / t / ZUZI / U / 4400 121 26, further characterized in that the T lymphocyte is CD4+ and CD8+.

30. An isolated nucleic acid molecule encoding the CAR in accordance with any of claims 1 to 29.

31. The isolated nucleic acid molecule according to claim 30, further characterized in that the nucleic acid molecule comprises a nucleic acid sequence selected from the group consisting of SEQ ID NO: 90, 89, 87, 88, 33, 34, 35, 36, 37, and 38.

32. The isolated nucleic acid molecule according to claim 30, further characterized in that the nucleic acid molecule comprises a nucleotide sequence that is at least approximately 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identical to a nucleotide sequence of SEQ ID NO: 90, 89, 87, 88, 33, 34, 35, 36, 37, and 38. 33.- A vector comprising the nucleic acid molecule in accordance with any of claims 30 to 32. 34.- A cell expressing the nucleic acid molecule in accordance with any of claims 30 to 32.

35. A pharmaceutical composition comprising an effective amount of lymphocyte according to any of claims 22 to 29.

36. A pharmaceutical composition comprising an effective amount of lymphocyte according to any of claims 22 to 29 and a pharmaceutically acceptable excipient.

37. The CAR according to any of claims 1 to 21 or the pharmaceutical composition according to claims 35 or 36 for use in treating a subject having cancer.

38. The use of the CAR according to any of claims 1 to 21 or the pharmaceutical composition according to claim 36 or 36 for the preparation of a medicament for treating a subject having cancer.

39. The lymphocyte according to any of claims 22 to 29, for use in treating a subject having cancer in a therapeutically effective quantity, wherein the lymphocyte induces the death of cancer cells in the subject.

40. The use of the lymphocyte according to any of claims 22 to 29 for the preparation of a medicament to treat a subject having cancer in a therapeutically effective amount, wherein the lymphocyte induces the death of cancer cells in the subject.

41. The CAR or the pharmaceutical composition for use according to claim 37 or the lymphocyte for use according to claim 39, wherein the cancer IVIA / t / ZUZI / U / 4400 122 is selected from the group consisting of lung cancer, gastric cancer, colon cancer, hepatocellular carcinoma, renal cell carcinoma, urothelial carcinoma of the bladder, metastatic melanoma, breast cancer, ovarian cancer, cervical cancer, head and neck cancer, pancreatic cancer, glioma, glioblastoma, and non-Hodgkin lymphoma (NHL), acute lymphocytic leukemia (ALL), chronic lymphocytic leukemia (CLL), chronic myelogenous leukemia (CML), latent multiple myeloma (SMM), multiple myeloma (MM), acute myeloid leukemia (AML), and combinations thereof.

42. Use in accordance with claim 38 or claim 40, wherein the cancer is selected from the group consisting of lung cancer, gastric cancer, colon cancer, hepatocellular carcinoma, renal cell carcinoma, urothelial carcinoma of the bladder, metastatic melanoma, breast cancer, ovarian cancer, cervical cancer, head and neck cancer, pancreatic cancer, glioma, glioblastoma, and non-Hodgkin lymphoma (NHL), acute lymphocytic leukemia (ALL), chronic lymphocytic leukemia (CLL), chronic myeloid leukemia (CML), latent multiple myeloma (SMM), multiple myeloma (MM), acute myeloid leukemia (AML), and combinations thereof.

43. The CAR or the pharmaceutical composition for use according to claim 37 and the lymphocyte for use according to claim 39, wherein the cancer is multiple myeloma. 44.- Use in accordance with claim 38 or claim 40, wherein the cancer is multiple myeloma.

45. The lymphocyte according to any of claims 22 to 29 for use in the targeted elimination of a cancer cell, wherein the lymphocyte is adapted to be administered by bringing it into contact with the cancer cell, whereby the lymphocyte induces the elimination of the cancer cell.

46. ​​The use of the lymphocyte according to any of claims 22 to 29 for the preparation of a medicament for the targeted elimination of a cancer cell, wherein the medicament is adapted to be administered by bringing it into contact with the cancer cell, whereby the lymphocyte induces the elimination of the cancer cell.

47. The lymphocyte for use according to claim 45, wherein the cancer is selected from the group consisting of lung cancer, gastric cancer, colon cancer, hepatocellular carcinoma, renal cell carcinoma, urothelial carcinoma of the bladder, metastatic melanoma, breast cancer, ovarian cancer, cervical cancer, head and neck cancer, pancreatic cancer, glioma, glioblastoma, and non-Hodgkin lymphoma (NHL), acute lymphocytic leukemia (ALL), chronic lymphocytic leukemia (CLL), chronic myelogenous leukemia (CML), latent multiple myeloma (SMM), multiple myeloma (MM), acute myeloid leukemia (AML), and combinations thereof.

48. Use according to claim 46, wherein the cancer cell is selected from the group consisting of lung cancer, gastric cancer, colon cancer, hepatocellular carcinoma, renal cell carcinoma, urothelial carcinoma of the bladder, metastatic melanoma, breast cancer, ovarian cancer, cervical cancer, head and neck cancer, pancreatic cancer, glioma, glioblastoma, and non-Hodgkin lymphoma (NHL), acute lymphocytic leukemia (ALL), chronic lymphocytic leukemia (CLL), chronic myelogenous leukemia (CML), latent multiple myeloma (SMM), multiple myeloma (MM), acute myeloid leukemia (AML), and combinations thereof.

49. The lymphocyte for use in accordance with claim 45, wherein the cancer cell is a multiple myeloma cell.

50. Use in accordance with claim 46, wherein the cancer cell is a multiple myeloma cell.

51. The CAR-cell complex according to claim 1 for use in detecting the presence of cancer in a subject, wherein the CAR-cell complex is adapted to be administered to a subject in need by: (a) contacting a cell sample obtained from the subject with the CAR of claim 1, thereby forming a CAR-cell complex, and (b) detecting the complex, wherein detection of the complex is indicative of the presence of cancer in the subject. 52.- The use of the CAR-cell complex according to claim 1 for the preparation of a medicament for detecting the presence of cancer in a subject, wherein the medicament is adapted to be administered to the subject in need by: (a) contacting a cell sample obtained from the subject with the medicament comprising the CAR of claim 1, thereby forming a CAR-cell complex, and (b) detecting the complex, wherein the detection of the complex is indicative of the presence of cancer in the subject.