WO2023200873A2

WO2023200873A2 - Chimeric antigen receptor compositions and methods of using the same

Info

Publication number: WO2023200873A2
Application number: PCT/US2023/018345
Authority: WO
Inventors: John DIPERSIO; Julie O'NEAL; Julie RITCHEY; Ramzi ABBOUD
Original assignee: Washington University
Priority date: 2022-04-12
Filing date: 2023-04-12
Publication date: 2023-10-19
Also published as: WO2023200873A3

Abstract

This application generally relates to immune cellular therapy. In particular, the disclosure relates to chimeric antigen receptor (CAR) constructs, cells comprising the same, and methods of treating subjects in need thereof.

Description

CHIMERIC ANTIGEN RECEPTOR COMPOSITIONS AND METHODS OF USING THE SAME CROSS-REFERENCE TO RELATED APPLICATIONS [0001] The present application claims the benefit of U.S. Provisional Patent Application No.63/330,088, entitled, “Chimeric antigen receptor compositions and methods of using the same” filed April 12, 2022, the content of which is hereby incorporated by reference in its entirety. FIELD OF THE TECHNOLOGY [0002] This application generally relates to immune cellular therapy. In particular, the disclosure relates to chimeric antigen receptor (CAR) constructs, cells comprising the same, and methods of treating subjects in need thereof. REFERENCE TO SEQUENCE LISTING [0003] A paper copy of the sequence listing and a computer readable form of the same sequence listing are appended below and herein incorporated by reference. The information recorded in computer readable form is identical to the written sequence listing, according to 37 C.F.R.1.821(f). BACKGROUND [0004] Despite improvement in treatment options for myeloma patients, multiple myeloma remains incurable. Expression of chimeric antigen receptor (CAR) on T-cells targeting BCMA (BCMA-CAR-T) has been successful in extending patient survival in some patients, by more than two years. However, relapse is inevitable, suggesting targeting alternative proteins may improve CAR-T therapy for myeloma. [0005] Thus, there is a need to identify new and efficient targets for CAR-T therapy for treating multiple myeloma, and other B cell and/or plasma cell malignancies. SUMMARY [0006] In some aspects, the disclosure provides an immune effector cell comprising a chimeric antigen receptor (CAR-immune effector cell), wherein the antigen recognition domain of the chimeric antigen receptor specifically binds to FCRL5. [0007] In some aspects, the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising an amino acid sequence with at least 80% identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [0008] In some aspects, the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VL comprising an amino acid sequence with at least 80% identity to the sequence of any one of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [0009] In some aspects, the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises: a VH comprising an amino acid sequence with at least 80% identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80; and a VL comprising an amino acid sequence with at least 80% identity to the sequence of any one of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [0010] In some aspects, the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising an amino acid sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [0011] In some aspects, the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VL comprising an amino acid sequence of any one of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [0012] In some aspects, the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises: a VH comprising an amino acid sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80; and a VL comprising an amino acid sequence of any one of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [0013] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLQESGPGLVKPSQTLSLTCTVSGGSISSGGYFWSWIRQHPGKGLEWIGFIYYSG NTYYNPSLKSRVTISVDTSKSQFSLELSSVTAADTAVYYCAREGAAAGTFHYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIK. [0014] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLIQPGGSLRLSCAASGLTVSSNYMSWVRQAPGKGLEWVSLIYTGGST YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGWVAFDIWGQGTMVTVS S and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSLTFGGGTKVDIK. [0015] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLIQPGGSLRLSCAASGFTVSRNYMTWVRQAPGKGLEWVSVIYSGGTT YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGVVAFDIWGQGTMVTVS S and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPPLTFGGGTKVEIK. [0016] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLIQPGGSLRLSCAASGFTVSRNYMTWVRQAPGKGLEWVSVIYTGGST YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGGVAFDIWGQGTMVTVS S and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFALYYCQQYGNSPMSTFGQGTRLEIK. [0017] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLIQPGGSLRLSCAASGFTVSRNYMTWVRQAPGKGLEWVSVIYSGGST YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGVIAFDYWGQGILVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPITFGQGTRLEIK. [0018] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMHWVRQAPGQGLEWMGWINPNS GGTKYAQKFQGRVTMTRDTSISTAYMELRRLTSDDTAVYYCVREGGSYYYASSGYDY VPFEYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSMYTFGQGTKVEIK. [0019] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFNGYYMHWVRQAPGQGLEWMGWISAYN GNTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCVREGGSYYYASSGYDY VPFEYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKLEIK. [0020] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKTSGYTFTGYYIHWVRQAPGQGLEWMGWISAYNG NTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCAREGGSYYYANGGYDY VPFEYWGQGTLVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSFLSASVGDRVTITCRASQGISSYLAWYQQKPGKAPKLLIYAASSLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPITFGQGTRLEIK. [0021] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMTPNS VNTGYAQKFQGRVTMTTDTSTSTAYMELSRLRSDDTAVYYCARGPSIMITFGGVIVTP FDYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKVDIK. [0022] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMNPNS GNTGYAQKFQGRVTMTRNTSISTAYMELSSLRSEDTAVYYCARGPSILITFGGVIVTPF DYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPYTFGQGTKVDIK. [0023] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMTPNS GNTGYAQKFQGRVTMTRNTSISTAYMELSSLRSEDTAVYYCARGPSILITFGGVIVTPF DYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPATLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASNRATGI PARFSGSGSGTDFTLTISSLQPEDFAVYYCQQYGSSPYTFGQGTRLEIK. [0024] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYVHWVRQAPGQGLEWMGWINPNS GGTVSAQKFQGRVTMTRDTSISTAYMELSGLKSDDTAVYSCARFCSITSCYMRGFDY WGQGTLVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSASVGDRVTITCRASQSISSWLAWYQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPLTFGGGTKVDIK. [0025] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLEWMGWINPNSG GTDSAQKFQGRVTMTRDTSISTAYMELSRLRSDDTAVYYCAREGGSYYYANGGYYYL PFDFWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYNNWPPTFGQGTKVDIK. [0026] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMQWVRQAPGQGLEWMGWINPNS GDTNYAQKFQGRVTMTRDTSINTVYMELSRLRSDDTAVYYCAREGGSYYYAGGGYY YLPFDYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSLFTFGPGTKLEIK. [0027] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLEWMGLINPNSG GTNYAQKFQGRVTMTRDTSIGTAYMELSRLRSDDSAIYYCTREGGSYYYANGGYYYL PFDFWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKVDIK. [0028] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYLYWVRQAPGQGLEWMGWINPNS GDTSYVQKFQGRVTMTRDTSTSTVYMELSRLRSDDTAVYYCARRYSGYLDYWGQGT LVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPVTFGGGTKVEIK. [0029] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMYWVRQAPGQGLEWMGLINPNS GDTSYAQKFQGRVTMTRDTSISTVYMELSGLTSDDTAVYYCARRYSGYLDYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPITFGQGTRLEIK. [0030] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMEWVRQAPGQGLEWMGLINPNS GGTNYEENFKGRVTMTRDTSISTAYMELSRLRSDDTAVYYCARRDSGFLDYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKAGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPLTFGGGTKVEIK. [0031] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLQESGPGLVKPSETLSLTCTVSGGSVSSGSYYWSWIRQPPGKGLEWIGFIYYSG STYYNPSLKSRVTISVDTSKNQFSLKLTSVTAADTAVYYCARDGGAAAGTLDYWGQGT LVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIK. [0032] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLVKPGGSLRLSCAASGFTFSSYDMHWVRQAPGKGLVWVSRIDSYGT YTNYADSVKGRFTISRDNAKNTLYLQMNNLRAEDTAVYYCARIAATASGYWGQGTPVT VSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQRISNYLNWYQQKPGKAPKPLIYAASRLQSGV PSRFSGSGSVTDFTLTISSLQPEDFASYYCQQSYSTPYTFGQGTKVEIK. [0033] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QITLKESGPTLVKPTQTLTLTCTFSGFSLSTSGVGVGWIRQPPGKALEWLALIYWNDDK RYSPSLKSRLTITKDTSKNQVVLTMTNVDPVDTATYYCAHRRNSRWYPFDYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIQLTQSPSFLSASVGDRVTITCRASQGISSYLAWYRQKPGKAPKLLIYAVSILQSGVPS RFSGSGSGTDFTLTISSLQPEDFATYYCQQLNSYPITFGQGTRLEIK. [0034] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGADVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLEWMGWINPNSG GTNYEQKFQGRVTMTRDTSITTAYMEVSRLRSDDTAVYYCARRWNYGIDYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIVMTQTPLSSPVTLGQPASISCRSSQSLVYSDGNTYLSWLQQRPGQPPRLLIYKISNR FSGVPDRFSGSGAGTDFTLKISRVEAEDVGVYYCMQAIQFPYTFGQGTKLEIK. [0035] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYDG SNKYYVDSVKGRVTISRDNSKNTLYLQMNSLRAEDTAVYYCARGGFDYLPLMDVWGK GTTVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLAVSLGERAIINCKSSQSVLHSSDNKNYLAWYQQKPGQPPKLLIHWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPWTFGQGTKVEIK. [0036] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLQESGPGLVKPSQTLSLTCTVSGGSISSGGYYWSWIRQHPGKGLEWIGYIYYSG STYYNPSLKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCARDGHYDSIGYYFDYWGQ GTLVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQNPGKAPKLLIFTASSLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPRTFGQGTKVEIK. [0037] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMNPTS GNTGYAQKFQGRVTMTKNTSISTAYMELSNLRSEDTAVYFCARGLYKWNYWGQGTL VTVSS and/or a VL comprising the amino acid sequence EIVMTQSPATLSVSPGERATLSCRASQSVSRNLAWYQQKPGQAPRLLIYGASTRATGI PARFSGSGSGTEFTLTISSLQSEDFAVYSCQQYTNWPALTFGGGTKVEIK. [0038] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGVLVQPGGSLRLSCAASGFTFSSYWMHWVRQAPGKGLMWVSRIDSDGT TTNYADSVKGRFTISRDNAKNTLNLQMNSLRAEDTAVYYCARIAATASGYWGQGTLVT VSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSTSVGDRVTITCRASQSISSYLNWYQQKPGKAPNLLIYAASSLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPITFGQGTRLEIK. [0039] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QLQLQESGPGLVKPSETLSLICTVSGGSISSSNYYWGWIRQPPGKGLEWIGSIYYSGS TYYNPSLKSRVTISVDTSNNQFSLRLNSVTAADTAVYYCAREGELKYWFFDLWGRGTL VTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSTLSASVGDRVTITCRASQSIISWLAWYQEKPGKAPKVLIYKASSLESGVP SRFSGSGSGTEFTLTISSLQPDDFATYYCQQYNSYSRTFGQGTKVEIK. [0040] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLDWMGWINPNSG VTNYAQKFQGRVTMTRDTSISTAYMDLSRLRSDDTAVYSCARDRGGDSPDAFDLWG QGTMVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLTVSLGERATINCKSSQSVLYSSKNKNYLAWYQQKPGQPPKLLIYWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVFYCQQYYSTPWTFGHGTKVEIK. [0041] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTNYGITWVRQAPGQGLEWMGWISAYDG YTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARDYDFWSGLDPWGQG TLVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPLSLPVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKPGQSPQLLIYLGSN RASGVPDRFSGSGSGTDFTLKISRVEAEDVGIYYCMQALQTPWTFGRGTKVEIK. [0042] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLVQPGGSLRLSCAASGFILSSYDMHWVRQATGKGLEWVSGIGTAGET YYSGSVKGRFTISRENAKNSLYLQMNSLRAGDTAVYYCAREDYFYYMDVWGKGTTVT VSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQSIRSYLNWYQQKPGKAPKLLIYAASTLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTRTFGQGTKVEIK. [0043] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGDLVKPGGSLRLSCAASGFTFNNAWMSWVRQAPGKGLEWVGRIQSKTD GGTTDYAAPVKGRFTISRDDSKNTLYMQMNSLKAEDTAVYYCTSILTGYYYYYYMDV WGRGTTVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQGISIYLAWYQQKPGKVPKLLIYAASSLQSGVP SRFSGSKSGTDFTLTISSLQPEDVATYYCQKYDSAPFTFGPGTKVDIK. [0044] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVANIKQDGI KKYYVDSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDQYCTNGVCYGGWF DPWGQGTLVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSTLSASVGDRVTITCRASQSISSWLAWYQQKPGKAPKVLIYKASSLESGV PSRFSGSGSGTDFTLTISSMQPDDFATYYCQQYNGYSRTFGQGTKVEIK. [0045] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLVQPGGSLRLSCAASGFTFNSYAMSWVRQAPGKGLEWVSAISGSGD TTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYHCVKGWKHLWSDYFDHWG PGTLVTVSS and/or a VL comprising the amino acid sequence EIVMTQSPATQSVSPGERATLSCRASQSVNNNLAWYQQKPGQAPRLLIYGASTRATGI PARFSGSGSGTEFTLTISSLQSEDFAVYYCQQYNNWPIAFGQGTRLEIK. [0046] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYVMHWVRQAPGKGLEWVSTINWNGD YIGYADSVKGRFTISRDNAKNSLYLQMNSLRAEDTALYYCAKASYMDVWGKGTTVTVS S and/or a VL comprising the amino acid sequence DVVMTQSPLSLPVTLGQPASVSCRSSQSLVYSDGNTYLNWFQQRPGQSPRRLIYKVS NRDSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGTHWTWTFGQGTKLEIK. [0047] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVESGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTT NYAQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCARDELYSSSWYGVYWGQGT LVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPLSLPVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKPGQSPQLLIYLGSN RASGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQALQTPWTFGQGTKLEIK. [0048] In some aspect, the immune effector cell comprises an anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYYMYWVRQAPGPGLEWMGIINPSGG RTTYAQKFQGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCARRDDYGALDYWGQGT LVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQSIRNYLNWYQQKPGKAPKLLIYDTSNLQSGV PSRFSGSGSGTDLTLTISSLQPDDFATYYCQQSYSIPITFGQGTRLEIK. [0049] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLQQSGPGLVKPSQTLSLTCAISGDSVSSNSAAWNWIRQSPSRGLEWLGRTYYRS KWYNDYAASVKSRITINPDTSKNQFSLQLNSVTPEDTAVYYCARDDWYFDLWGRGTL VTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQQPGLPPKLLIFWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSSPYTFGQGTKVEIK. [0050] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYEG SNKYFADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARDRGTMVRGLHYFDY WGQGTLVTVSS and/or a VL comprising the amino acid sequence AIQMTQSPSSLSASVGDRVTITCRASQDIRNDLGWYQQKPGKAPKLLIYGASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCLQDYNYPWTFGQGTKVEIK. [0051] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGVVVQPGGSLRLSCAASGFTFDDYTMHWVRQAPGKGLEWVSLITWDGG RTYYADSVKGRFTISRDNSKNSLYLQMNSLRTEDTALYYCAKDISLDYWGQGTLVTVS S and/or a VL comprising the amino acid sequence DVVMTQSPLSLSVTLGQPASISCRSSQSLVYSDGNTYLNWFQQRPGQSPRRLIYKVS NRDSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGIHWPLTFGGGTKVEIK. [0052] In some aspects, the immune effector cell comprises an anti- FCRL5 antigen recognition domain of the chimeric antigen receptor comprising a VH comprising the amino acid sequence EVQLVESGGGLVKPGGSLRLSCAASGFTFSNAWMSWVRQAPGKGLEWVGRIKSKTD GGTTDYAAPVKGRFTISRDDSKNTLYLQMNSLRTEDTAVYYCSTTSLSYYDILTGYYKD YYYYYMDVWGKGTTVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSTSVGDRVTITCRASQGISSWLAWFQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPLTFGGGTKVEIK. [0053] In some aspects, the CAR-T cell further comprises a suicide gene. In some aspects, the suicide gene encodes a modified Human-Herpes Simplex Virus-1- thymidine kinase (TK) gene fused in-frame to the extracellular and transmembrane domains of the human CD34 cDNA. [0054] In further aspects, the disclosure encompasses a method of killing a malignant cell in a subject in need thereof, the method comprising administering an disclosed immune effector cell. [0055] In some aspects of the method, the malignant cell is a malignant B cell or a malignant plasma cell. In some aspects, the malignant cell is a Burkitt lymphoma, chronic lymphocytic leukemia/small lymphocytic lymphoma (CLL/SLL), diffuse large B-cell lymphoma, follicular lymphoma, or mantle cell lymphoma, Monoclonal gammopathy of undetermined significance, Lymphoplasmacytic lymphoma, Plasmacytoma, or myeloma. In some aspects, the malignant cell is a myeloma cell. [0056] In some aspects, a method of treating a mammal having a cell malignancy, the method comprising administering to the mammal a plurality of disclosed chimeric antigen receptor immune effector cells, is further provided. BRIEF DESCRIPTION OF THE FIGURES [0057] The application file contains at least one drawing executed in color. Copies of this patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee. [0058] Fig.1 is a schematic of method of generation of FCRL5 antibodies. [0059] Fig.2 shows binding of FCRL5 antibodies to MOLP-2 cells. Fig.1A shows assessment of binding of FCRL5 antibodies to the MOLP-2 myeloma cell line using flow cytometry. Fig.1B shows ranked mean fluorescence intensity (MFI) of antibody binding of FCRL5 antibodies to MOLP-2 cells. [0060] Fig.3 illustrates specific binding of FCRL5 antibodies to high expressing FCRL5 MM.1S-CG cells. Fig.3A shows assessment of binding of FCRL5 antibodies to MM1S-CG cells engineered to express high levels of FCLR5. Fig 3B shows negligible binding FCRL5 antibodies to parental MM.1S-CG cells, which do not express FCRL5 demonstrating specificity. [0061] Fig.4 shows in vitro killing of FCRL5 low (MOLP-2) and high (OPM2-CG) expressing cells by FCRL5-CAR-T. Fig.4A shows high FCRL5 expressing cells, generated by adding human FCRL5 to OPM2 cell, which was previously modified to express a GFP-luciferase fusion protein. Fig.4B shows comparison of FCRL5 expression levels on MOLP-2 and OPM2-CG-FCRL5. Fig.4C-4D shows efficient killing of FCRL5-CAR-T generated with scFv sequences from two clones (ATX-942; 942 and ATX-947, 947) in vitro of both MOLP2 (modified to express GFP and luciferase; MOLP2-CG) (Fig.4C) and OPM2-CG-FCRL5 (Fig.4D) target cells. Killing assays were run by incubating effector (E) CAR-T with target (T) cells at a range of E:T ratios. Bioluminescent imaging (BLI) was used to assess cell death. Fig.4E shows cell death in OPM2-CG-FCRL5 target cells incubated with FCRL5-CAR-T cells made using scFv sequences from seven different antibody clones for 24 hours (left) and 48 hours (right) at a range of E:T ratios. Bioluminescent imaging (BLI) was used to assess cell death. Fig.4F shows cell death of MOLP2 target cells incubated with FCRL5-CAR-T cells. FCRL5 CAR-T generated with the same seven scFv as in (Fig.4E) were used in 48 hour killing assays with MOLP2 target cells at the E:T ratios indicated. Flow cytometry was used to assess MOLP2 killing in two separate experiments. [0062] Fig.5 shows efficacy of FCRL5 CAR-T tested in a xenograft mouse model of myeloma. Fig.5A shows survival assessed using Kaplan Meier analysis in mice.2x10⁶ OPM2-CG-FCRL5 were injected i.v. into tail veins of NSG mice. Eighteen days later (avg. BLI signal 4.4x10⁸), mice were treated with 2x10⁶ FCRL5-CAR-T-970 injected i.v., non-transduced T cells or were left untreated. Fig.5B shows tumor burden measured over time via longitudinal live mouse bioluminescent imaging (BLI). Each line represents one mouse Fig.5C shows Kaplan Meier analysis of mice engrafted with 2x10⁶ OPM2-CG-FCRL5 cells and treated on day 18 with FCRL5-CAR-T (948, 951, 957 970 or controls). Average BLI signal at time of treatment was 1.8x10⁹. Fig.5D shows tumor burden assessed using BLI. Each line represents one mouse Fig.5E shows normalized BLI mouse images. NT represents no treatment. DETAILED DESCRIPTION [0063] The present disclosure is based, in part, on the identification of antigen binding proteins which specifically target FCRL5 and are useful for incorporation into chimeric antigen receptor (CAR) constructs. Thus, the present disclosure provides amino acid and nucleic acid sequences encoding anti-FCRL5 binding molecules. The immune effector cells engineered to express FCRL5-CAR were found to be active and functional against both low and high FCRL5 expressing target cells. The disclosure further relates to compositions and methods for treating cancer including but not limited to B cell and plasma cell malignancies. [0064] Other aspects and iterations of the invention are described more thoroughly below. I. Definitions [0065] So that the present disclosure may be more readily understood, certain terms are first defined. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which aspects of the disclosure pertain. Many methods and materials similar, modified, or equivalent to those described herein can be used in the practice of the various aspects of the present disclosure without undue experimentation, the preferred materials and methods are described herein. In describing and claiming the aspects of the present disclosure, the following terminology will be used in accordance with the definitions set out below. [0066] Concentrations, amounts, and other numerical data may be expressed or presented herein in a range format. It is to be understood that such a range format is used merely for convenience and brevity and should be interpreted flexibly to include not only the numerical values explicitly recited as the limits of the range, but also to include all the individual numerical values or sub-ranges encompassed within that range as if each numerical value and sub-range is explicitly recited. As an illustration, a numerical range of “about 2 to about 50” should be interpreted to include not only the explicitly recited values of 2 to 50, but also include all individual values and sub-ranges within the indicated range. Thus, included in this numerical range are individual values such as 2, 2.4, 3, 3.7, 4, 5.5, 10, 10.1, 14, 15, 15.98, 20, 20.13, 23, 25.06, 30, 35.1, 38.0, 40, 44, 44.6, 45, 48, and sub-ranges such as from 1-3, from 2-4, from 5-10, from 5-20, from 5-25, from 5-30, from 5-35, from 5-40, from 5-50, from 2-10, from 2-20, from 2-30, from 2-40, from 2-50, etc. This same principle applies to ranges reciting only one numerical value as a minimum or a maximum. Furthermore, such an interpretation should apply regardless of the breadth of the range or the characteristics being described. [0067] The term “about,” as used herein, refers to variation of in the numerical quantity that can occur, for example, through typical measuring techniques and equipment, with respect to any quantifiable variable, including, but not limited to, mass, volume, time, distance, and amount. Further, given solid and liquid handling procedures used in the real world, there is certain inadvertent error and variation that is likely through differences in the manufacture, source, or purity of the ingredients used to make the compositions or carry out the methods and the like. The term “about” also encompasses these variations, which can be up to ± 5%, but can also be ± 4%, 3%, 2%, 1%, etc. Whether or not modified by the term “about,” the claims include equivalents to the quantities. [0068] In this disclosure, “comprises,” “comprising,” “containing,” and “having” and the like can have the meaning ascribed to them in U.S. Patent Law and can mean “includes,” “including,” and the like, and are generally interpreted to be open ended terms. The terms “consisting of” or “consists of” are closed terms, and include only the components, structures, steps, or the like specifically listed in conjunction with such terms, as well as that which is in accordance with U.S. Patent law. “Consisting essentially of” or “consists essentially of” have the meaning generally ascribed to them by U.S. Patent law. In particular, such terms are generally closed terms, with the exception of allowing inclusion of additional items, materials, components, steps, or elements, that do not materially affect the basic and novel characteristics or function of the item(s) used in connection therewith. For example, trace elements present in a composition, but not affecting the composition’s nature or characteristics would be permissible if present under the “consisting essentially of” language, even though not expressly recited in a list of items following such terminology. In this specification when using an open ended term, like “comprising” or “including,” it is understood that direct support should be afforded also to “consisting essentially of” language as well as “consisting of” language as if stated explicitly and vice versa. [0069] As used herein “FCRL5” or “Fc Receptor Like 5” refers to peptides derived from the gene FCRL5 which is located on human chromosome 1q23.1 (chr1:157,513,377-157,552,533 (GRCh38/hg38) Size: 39,157 bases). FCRL5 is also designated as FcRH5, IRTA2 or CD307. This gene encodes a member of the immunoglobulin receptor superfamily and the Fc-receptor like family. This gene and several other Fc receptor-like gene members are clustered on the long arm of chromosome 1. The encoded protein is a single-pass type I membrane protein and contains 8 immunoglobulin-like C2-type domains. This gene is implicated in B cell development and lymphomagenesis. Alternatively spliced transcript variants encoding different isoforms have been identified. The FCRL5 protein is 977 amino acids long and has a molecular mass of 106437 Da. Further, the FCRL5 has a large extracellular domain comprised of nine Ig subunits (referred as “domain 1-9” or “D1-9”) Full-length FCRL5 has an amino acid sequence of SEQ ID NO: 1.

[0070] As used herein “isoform”, refers to any of several different forms of the same protein, arising due to alternative splicing of mRNA encoding the protein, post- translational modification of the protein, proteolytic processing of the protein that occurs in vivo, genetic variations and somatic recombination. The terms “isoform,” “species,” and “variant” are used interchangeably (e.g., the term “FCRL5 isoform” and “FCRL5 species” may be used interchangeably). [0071] Unless expressly stated otherwise, the term “FCRL5” refers to “human FCRL5”, and encompasses all genetically encoded isoforms or variants, as well as species thereof that are C-terminally truncated in vivo, N-terminally truncated in vivo, N-terminally truncated and C-terminally truncated in vivo, post-translationally modified in vivo, or any combination thereof. [0072] As used herein, “individual”, “subject”, “host”, and “patient” can be used interchangeably and may refer to any human or non-human mammalian subject for whom diagnosis, treatment, prophylaxis or therapy is desired, for example, humans, pets, livestock, horses or other animals. In some aspects, the subject is a human. In other aspects, the subject is a human in need of treatment for cancer. [0073] The terms “treat,” "treating," or "treatment" as used herein, refer to both therapeutic treatment and prophylactic or preventative measures, wherein the object is to prevent or slow down (lessen) an undesired physiological change or disease/disorder. Beneficial or desired clinical results include, but are not limited to, alleviation of symptoms, diminishment of extent of disease, stabilized (i.e., not worsening) state of disease, a delay or slowing of disease progression, amelioration or palliation of the disease state, and remission (whether partial or total), whether detectable or undetectable. “Treatment” can also mean prolonging survival as compared to expected survival if not receiving treatment. Those in need of treatment include those already with the disease, condition, or disorder as well as those prone to have the disease, condition, or disorder or those in which the disease, condition or disorder is to be prevented. [0074] As used herein “cancer,” “tumor,” or “malignancy” may refer to one or more neoplasm or cancer. The neoplasm may be malignant or benign, the cancer may be primary or metastatic; the neoplasm or cancer may be early stage or late stage. Non-limiting examples of neoplasms or cancers may include acute lymphoblastic leukemia, acute myeloid leukemia, adrenocortical carcinoma, AIDS-related cancers, AIDS-related lymphoma, anal cancer, appendix cancer, astrocytomas (childhood cerebellar or cerebral), basal cell carcinoma, bile duct cancer, bladder cancer, bone cancer, brainstem glioma, brain tumors (cerebellar astrocytoma, cerebral astrocytoma/malignant glioma, ependymoma, medulloblastoma, supratentorial primitive neuroectodermal tumors, visual pathway and hypothalamic gliomas), breast cancer, bronchial adenomas/carcinoids, Burkitt lymphoma, carcinoid tumors (childhood, gastrointestinal), carcinoma of unknown primary, central nervous system lymphoma (primary), cerebellar astrocytoma, cerebral astrocytoma/malignant glioma, cervical cancer, childhood cancers, chronic lymphocytic leukemia, chronic myelogenous leukemia, chronic myeloproliferative disorders, colon cancer, cutaneous T-cell lymphoma, desmoplastic small round cell tumor, endometrial cancer, ependymoma, esophageal cancer, Ewing's sarcoma in the Ewing family of tumors, extracranial germ cell tumor (childhood), extragonadal germ cell tumor, extrahepatic bile duct cancer, eye cancers (intraocular melanoma, retinoblastoma), gallbladder cancer, gastric (stomach) cancer, gastrointestinal carcinoid tumor, gastrointestinal stromal tumor, germ cell tumors (childhood extracranial, extragonadal, ovarian), gestational trophoblastic tumor, gliomas (adult, childhood brain stem, childhood cerebral astrocytoma, childhood visual pathway and hypothalamic), gastric carcinoid, hairy cell leukemia, head and neck cancer, hepatocellular (liver) cancer, Hodgkin lymphoma, hypopharyngeal cancer, hypothalamic and visual pathway glioma (childhood), intraocular melanoma, islet cell carcinoma, Kaposi sarcoma, kidney cancer (renal cell cancer), laryngeal cancer, leukemias (acute lymphoblastic, acute myeloid, chronic lymphocytic, chronic myelogenous, hairy cell), lip and oral cavity cancer, liver cancer (primary), lung cancers (non-small cell, small cell), lymphomas (AIDS-related, Burkitt, cutaneous T-cell, Hodgkin, non-Hodgkin, primary central nervous system), macroglobulinemia (Waldenström), malignant fibrous histiocytoma of bone/osteosarcoma, medulloblastoma (childhood), melanoma, intraocular melanoma, Merkel cell carcinoma, mesotheliomas (adult malignant, childhood), metastatic squamous neck cancer with occult primary, mouth cancer, multiple endocrine neoplasia syndrome (childhood), multiple myeloma/plasma cell neoplasm, mycosis fungoides, myelodysplastic syndromes, myelodysplastic/myeloproliferative diseases, myelogenous leukemia (chronic), myeloid leukemias (adult acute, childhood acute), multiple myeloma, myeloproliferative disorders (chronic), nasal cavity and paranasal sinus cancer, nasopharyngeal carcinoma, neuroblastoma, non-Hodgkin lymphoma, non-small cell lung cancer, oral cancer, oropharyngeal cancer, osteosarcoma/malignant fibrous histiocytoma of bone, ovarian cancer, ovarian epithelial cancer (surface epithelial-stromal tumor), ovarian germ cell tumor, ovarian low malignant potential tumor, pancreatic cancer, pancreatic cancer (islet cell), paranasal sinus and nasal cavity cancer, parathyroid cancer, penile cancer, pharyngeal cancer, pheochromocytoma, pineal astrocytoma, pineal germinoma, pineoblastoma and supratentorial primitive neuroectodermal tumors (childhood), pituitary adenoma, plasma cell neoplasia, pleuropulmonary blastoma, primary central nervous system lymphoma, prostate cancer, rectal cancer, renal cell carcinoma (kidney cancer), renal pelvis and ureter transitional cell cancer, retinoblastoma, rhabdomyosarcoma (childhood), salivary gland cancer, sarcoma (Ewing family of tumors, Kaposi, soft tissue, uterine), Sézary syndrome, skin cancers (nonmelanoma, melanoma), skin carcinoma (Merkel cell), small cell lung cancer, small intestine cancer, soft tissue sarcoma, squamous cell carcinoma, squamous neck cancer with occult primary (metastatic), stomach cancer, supratentorial primitive neuroectodermal tumor (childhood), T-Cell lymphoma (cutaneous), testicular cancer, throat cancer, thymoma (childhood), thymoma and thymic carcinoma, thyroid cancer, thyroid cancer (childhood), transitional cell cancer of the renal pelvis and ureter, trophoblastic tumor (gestational), unknown primary site (adult, childhood), ureter and renal pelvis transitional cell cancer, urethral cancer, uterine cancer (endometrial), uterine sarcoma, vaginal cancer, visual pathway and hypothalamic glioma (childhood), vulvar cancer, Waldenström macroglobulinemia, and Wilms tumor (childhood). [0075] As used herein, treatment of cancer can comprise increased inhibition of cancer progression and/or metastases, inhibition of an increase in tumor volume, a reduction in tumor volume and/or growth, a reduction in tumor growth rate, an eradication or killing of a tumor and/or cancer cell, or any combination thereof. In some aspects, the treatment can also prolong the survival of a subject, improve the prognosis and/or improve the quality of life of the subject. [0076] As used herein “control sample” or “control cell” can be procured from a healthy subject and/or a subject with cancer procured prior to the start of treatment (baseline). A control subject is a healthy subject, or a subject not receiving treatment. In some aspects, the parameters measured during treatment can be an average of several control subjects, or a population average. In some aspects, the control sample can comprise of non-cancer cells. In some aspects, the non-cancer cells can be from the same tissue type as the cancer cells. For example, if the cancer cells are from breast cancer, then the non-cancer cells can be from healthy breast tissue. In some aspects, the control can comprise of an average levels of the analyte in a sample from a subject before onset of cancer. In some aspects, control sample can be a sample from the subject prior to diagnosis or treatment. In certain aspects, the analyte can be measured in a person or persons other than the subject with cancer. In some aspects, the control a person or persons with similar characteristics to the subject with cancer. In some aspects, the control can be an average of the combination of disclosed analyte levels from different healthy sources (e.g., more than one healthy control subject and/or more than one subject prior to the start of treatment (baseline)). In some aspects, the control sample can be pooled sample. [0077] As used herein, a biological sample may be of any biological tissue, fluid, or cell from the subject. The sample can be solid or fluid. The sample can be a heterogeneous cell population. Non-limiting examples of suitable biological samples include sputum, serum, blood, blood cells (e.g., white cells), a biopsy, urine, peritoneal fluid, pleural fluid, or cells derived therefrom. The biopsy can be a fine needle aspirate biopsy, a core needle biopsy, a vacuum assisted biopsy, an open surgical biopsy, a shave biopsy, a punch biopsy, an incisional biopsy, a curettage biopsy, or a deep shave biopsy. Biological samples may also include sections of tissues, such as frozen sections or formalin fixed sections taken for histological purposes. A sample can be a tumor tissue, tissue surrounding a tumor, or non-tumor tissue. Methods of procuring a biological sample from a subject are well known in the art. [0078] As used herein “antibody” is used in the broadest sense and encompasses various antibody and antibody-like structures, including but not limited to full-length monoclonal, polyclonal, and multispecific (e.g., bispecific, trispecific, etc.) antibodies, as well as heavy chain antibodies and antibody fragments provided they exhibit the desired antigen-binding activity. The domain(s) of an antibody that is involved in binding an antigen is referred to as a “variable region” or “variable domain,” and is described in further detail below. A single variable domain may be sufficient to confer antigen-binding specificity. Preferably, but not necessarily, antibodies useful in the discovery are produced recombinantly. Antibodies may or may not be glycosylated, though glycosylated antibodies may be preferred. An “isolated” antibody is one which has been separated from a component of its natural environment. In some aspects, an antibody is purified to greater than 95% or 99% purity as determined by methods known in the art. [0079] As used herein “full length antibody” and “intact antibody” are interchangeable, and refer to an antibody having a structure substantially similar to a native antibody structure or having heavy chains that contain an Fc region as defined herein. The basic structural unit of a native antibody comprises a tetramer. Each tetramer is composed of two identical pairs of polypeptide chains, each pair having one "light” chain (about 25 kDa) and one "heavy" chain (about 50-70 kDa). Light chains are classified as gamma, mu, alpha, and lambda. Heavy chains are classified as gamma, mu, alpha, delta, or epsilon, and define the antibody's isotype as IgG, IgM, IgA, IgD and IgE, respectively. The amino-terminal portion of each light and heavy chain includes a variable region of about 100 to 110 or more amino acid sequences primarily responsible for antigen recognition (VL and VH, respectively). The carboxy-terminal portion of each chain defines a constant region primarily responsible for effector function. Within light and heavy chains, the variable and constant regions are joined by a "J" region of about 12 or more amino acid sequences, with the heavy chain also including a "D" region of about 10 more amino acid sequences. Intact antibodies are properly cross-linked via disulfide bonds, as is known in the art. [0080] The variable domains of the heavy chain and light chain of an antibody generally have similar structures, with each domain comprising four conserved framework regions (FRs) and three hypervariable regions (HVRs). (See, e.g., Kindt et al. Kuby Immunology, 6^th ed., W.H. Freeman and Co., page 91 (2007)). A single VH or VL domain may be sufficient to confer antigen-binding specificity. Furthermore, antibodies that bind a particular antigen may be isolated using a VH or VL domain from an antibody that binds the antigen to screen a library of complementary VL or VH domains, respectively. See, e.g., Portolano et al., J. Immunol.150:880-887 (1993); Clarkson et al., Nature 352:624-628 (1991). [0081] As used herein “Framework region” or “FR” refers to variable domain residues other than hypervariable region (HVR) residues. The FR of a variable domain generally consists of four FR domains: FR1, FR2, FR3, and FR4. Accordingly, the HVR and FR sequences generally appear in the following sequence: FR1-HVR1- FR2-HVR2-FR3-HVR3-FR4. The FR domains of a heavy chain and a light chain may differ, as is known in the art. [0082] As used herein “hypervariable region” or “HVR” refers to each of the regions of a variable domain which are hypervariable in sequence (also commonly referred to as “complementarity determining regions” or “CDR”) and/or form structurally defined loops (“hypervariable loops”) and/or contain the antigen-contacting residues (“antigen contacts”). Generally, antibodies comprise six HVRs: three in the VH (H1, H2, H3), and three in the VL (L1, L2, L3). As used herein, “an HVR derived from a variable region” refers to an HVR that has no more than two amino acid substitutions, as compared to the corresponding HVR from the original variable region. Exemplary HVRs herein include: (a) hypervariable loops occurring at amino acid residues 26-32 (L1), 50- 52 (L2), 91-96 (L3), 26-32 (H1), 53-55 (H2), and 96-101 (H3) (Chothia and Lesk, J. Mol. Biol.196:901-917 (1987)); (b) CDRs occurring at amino acid residues 24-34 (L1), 50-56 (L2), 89-97 (L3), 31-35b (H1), 50-65 (H2), and 95-102 (H3) (Kabat et al.,Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, MD (1991)); (c) antigen contacts occurring at amino acid residues 27c-36 (L1), 46-55 (L2), 89-96 (L3), 30-35b (H1), 47-58 (H2), and 93-101 (H3) (MacCallum et al. J. Mol. Biol.262: 732-745 (1996)); (d) CDR1-IMGT (positions 27-38), CDR2-IMGT (positions 56-65), and CDR3-IMGT regions (positions 105-116 or 105- 117), which are based on IMGT unique numbering (Lefranc, “The IMGT unique numbering for Immunoglobulins, T cell receptors and Ig-like domains,” The Immunologist, 1999, 7: 132-136; Lefranc et al., Nucleic Acids Research, 2009, 37(Database issue): D1006-D1012; Ehrenmann et al., “Chapter 2: Standardized Sequence and Structure Analysis of Antibody Using IMGT,” in Antibody Engineering Volume 2, Eds. Roland E. Kontermann and Stefan Dubel, 2010, Springer-Verlag Berlin Heidelberg, doi: 10.1007/978-3-642-01147-4; www.imgt.org/IMGTScientificChart/Nomenclature/IMGT-FRCDRdefinition.html), and (e) combinations of (a), (b), (c), and/or (d), as defined below for various antibodies of this disclosure. Unless otherwise indicated, HVR residues and other residues in the variable domain (e.g., FR residues) that are assigned sequence identification numbers are numbered based on IMGT unique numbering, supra. [0083] As used herein “Fc region” define a C-terminal region of an immunoglobulin heavy chain that contains at least a portion of the constant region. The term includes native sequence Fc regions and variant Fc regions. In one embodiment, a human IgG heavy chain Fc region extends from Cys226, or from Pro230, to the carboxyl-terminus of the heavy chain. However, the C-terminal lysine (Lys447) of the Fc region may or may not be present. Unless otherwise specified herein, numbering of amino acid residues in the Fc region or constant region is according to the EU numbering system, also called the EU index, as described in Kabat et al., Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md., 1991. [0084] A “variant Fc region” comprises an amino acid sequence that can differ from that of a native Fc region by virtue of one or more amino acid substitution(s) and/or by virtue of a modified glycosylation pattern, as compared to a native Fc region or to the Fc region of a parent polypeptide. In an example, a variant Fc region can have from about one to about ten amino acid substitutions, or from about one to about five amino acid substitutions in a native sequence Fc region or in the Fc region of the parent polypeptide. The variant Fc region herein may possess at least about 80% homology, at least about 90% homology, or at least about 95% homology with a native sequence Fc region and/or with an Fc region of a parent polypeptide. [0085] As used herein “antibody fragment” refers to a molecule other than an intact antibody that comprises a portion of an intact antibody that binds the antigen to which the intact antibody binds. Non-limiting examples of antibody fragments include but are not limited to Fv, Fab, Fab′, Fab′-SH, F(ab′)2; single-chain forms of antibodies and higher order variants thereof; single-domain antibodies, and multispecific antibodies formed from antibody fragments. [0086] Single-chain forms of antibodies, and their higher order forms, may include, but are not limited to, single-domain antibodies, single chain variant fragments (scFvs), divalent scFvs (di-scFvs), trivalent scFvs (tri-scFvs), tetravalent scFvs (tetra- scFvs), diabodies, and triabodies and tetrabodies. ScFv’s are comprised of heavy and light chain variable regions connected by a linker. In most instances, but not all, the linker may be a peptide. A linker peptide is preferably from about 5 to 30 amino acids in length, or from about 10 to 25 amino acids in length. Typically, the linker allows for stabilization of the variable domains without interfering with the proper folding and creation of an active binding site. In preferred embodiments, a linker peptide is rich in glycine, as well as serine or threonine. ScFvs can be used to facilitate phage display or can be used for flow cytometry, immunohistochemistry, or as targeting domains. Methods of making and using scFvs are known in the art. ScFvs may also be conjugated to a human constant domain (e.g. a heavy constant domain is derived from an IgG domain, such as lgG1, lgG2, lgG3, or lgG4, or a heavy chain constant domain derived from IgA, IgM, or IgE). Diabodies, triabodies, and tetrabodies and higher order variants are typically created by varying the length of the linker peptide from zero to several amino acids. Alternatively, it is also well known in the art that multivalent binding antibody variants can be generated using self-assembling units linked to the variable domain. [0087] As used herein “single-domain antibody” refers to an antibody fragment consisting of a single, monomeric variable antibody domain. [0088] As used herein “Multispecific antibodies” include bi-specific antibodies, tri-specific, or antibodies of four or more specificities. Multispecific antibodies may be created by combining the heavy and light chains of one antibody with the heavy and light chains of one or more other antibodies. These chains can be covalently linked. [0089] As used herein "Monoclonal antibody" refers to an antibody that is derived from a single copy or clone, including e.g., any eukaryotic, prokaryotic, or phage clone. "Monoclonal antibody" is not limited to antibodies produced through hybridoma technology. Monoclonal antibodies can be produced using hybridoma techniques well known in the art, as well as recombinant technologies, phage display technologies, synthetic technologies or combinations of such technologies and other technologies readily known in the art. Furthermore, the monoclonal antibody may be labeled with a detectable label, immobilized on a solid phase and/or conjugated with a heterologous compound (e.g., an enzyme or toxin) according to methods known in the art. [0090] As used herein “heavy chain antibody” refers to an antibody that consists of two heavy chains. A heavy chain antibody may be an IgG-like antibody from camels, llamas, alpacas, sharks, etc., or an IgNAR from a cartiliaginous fish. [0091] As used herein "humanized antibody" refers to a non-human antibody that has been modified to reduce the risk of the non-human antibody eliciting an immune response in humans following administration but retains similar binding specificity and affinity as the starting non-human antibody. A humanized antibody binds to the same or similar epitope as the non-human antibody. The term “humanized antibody” includes an antibody that is composed partially or fully of amino acid sequences derived from a human antibody germline by altering the sequence of an antibody having non-human hypervariable regions (“HVR”). The simplest such alteration may consist simply of substituting the constant region of a human antibody for the murine constant region, thus resulting in a human/murine chimera which may have sufficiently low immunogenicity to be acceptable for pharmaceutical use. Preferably, the variable region of the antibody is also humanized by techniques that are by now well known in the art. For example, the framework regions of a variable region can be substituted by the corresponding human framework regions, while retaining one, several, or all six non-human HVRs. Some framework residues can be substituted with corresponding residues from a non-human VL domain or VH domain (e.g., the non- human antibody from which the HVR residues are derived), e.g., to restore or improve specificity or affinity of the humanized antibody. Substantially human framework regions have at least about 75% homology with a known human framework sequence (i.e. at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, or at least about 99% sequence identity). HVRs may also be randomly mutated such that binding activity and affinity for the antigen is maintained or enhanced in the context of fully human germline framework regions or framework regions that are substantially human. As mentioned above, it is sufficient for use in the methods of this discovery to employ an antibody fragment. Further, as used herein, the term "humanized antibody" refers to an antibody comprising a substantially human framework region, at least one HVR from a nonhuman antibody, and in which any constant region present is substantially human. Substantially human constant regions have at least about 90% with a known human constant sequence (i.e. about 90%, about 95%, or about 99% sequence identity). Hence, all parts of a humanized antibody, except possibly the HVRs, are substantially identical to corresponding pairs of one or more germline human immunoglobulin sequences. [0092] If desired, the design of humanized immunoglobulins may be carried out as follows, or using similar methods familiar to those with skill in the art (for example, see Almagro, et al. Front. Biosci.2008, 13(5):1619-33). A murine antibody variable region is aligned to the most similar human germline sequences (e.g. by using BLAST or similar algorithm). The CDR residues from the murine antibody sequence are grafted into the similar human “acceptor” germline. Subsequently, one or more positions near the CDRs or within the framework (e.g., Vernier positions) may be reverted to the original murine amino acid in order to achieve a humanized antibody with similar binding affinity to the original murine antibody. Typically, several versions of humanized antibodies with different reversion mutations are generated and empirically tested for activity. The humanized antibody variant with properties most similar to the parent murine antibody and the fewest murine framework reversions is selected as the final humanized antibody candidate. [0093] As used herein, the term "fusion protein" refers to proteins created through the joining of two or more genes that originally coded for separate proteins. Translation of this fusion gene results in a single polypeptide or multiple polypeptides with functional properties derived from each of the original proteins. In some embodiments, the two or more genes may comprise a substitution, a deletion, and / or an addition in its nucleotide sequence. [0094] As used herein “expression” or “expression level” or “level of expression” refers to amount of a particular analyte (e.g., FCRL5) present in the sample. The amount may be a concentration, number, ratio, proportion, or a percentage of the analyte compared to the control sample or determined using a standard curve. The amount may be an absolute amount or a relative amount. [0095] As used herein "combination therapy" refers to the administration of two or more therapeutic agents to treat a therapeutic condition or disorder described in the present disclosure. Such administration encompasses co-administration of these therapeutic agents in a substantially simultaneous manner, such as in a single capsule having a fixed ratio of active ingredients or in multiple, separate capsules for each active ingredient. In addition, such administration also encompasses use of each type of therapeutic agent in a sequential manner. In either case, the treatment regimen will provide beneficial effects of the drug combination in treating the conditions or disorders described herein. [0096] The term "composition" or “pharmaceutical composition” as used herein refers to an immunotherapeutic cell population combination with one or more therapeutically acceptable carriers. [0097] The term "deglycosylation" as used herein refers to an Fc region in which sugars are removed enzymatically from an Fc fragment. Additionally, the term "aglycosylation" means that an Fc fragment is produced in an unglycosylated form by a prokaryote, and preferably in E. coli. [0098] As used herein, the term "dimer" is an oligomer consisting of two monomers joined by bonds that can be either strong or weak, covalent, or intermolecular. The term "homodimer" is used when the two molecules are identical, e.g. A-A, and "heterodimer" when they are not, e.g. A-B. [0099] The term "disease" as used herein is intended to be generally synonymous, and is used interchangeably with, the terms "disorder," "syndrome," and "condition" (as in medical condition), in that all reflect an abnormal condition of the human or animal body or of one of its parts that impairs normal functioning, is typically manifested by distinguishing signs and symptoms, and causes the human or animal to have a reduced duration or quality of life. [00100] The term "effector function" refers to a specialized function of a differentiated cell. An effector function of a T cell, for example, may be cytolytic activity or helper activity including the secretion of cytokines. An effector function in a naive, memory, or memory-type T cell may also include antigen-dependent proliferation. [00101] The term "fratricide" as used herein means a process which occurs when a CAR-T cell becomes the target of, and is killed by, another CAR-T cell comprising the same chimeric antigen receptor as the target of CAR-T cell, because the targeted cell expresses the antigen specifically recognized by the chimeric antigen receptor on both cells. CAR-T cells comprising a chimeric antigen receptor which are deficient in an antigen to which the chimeric antigen receptor specifically binds will be "fratricide-resistant." [00102] As used herein, the term "gene expression" or "expression" of an IL-7 protein is understood to refer to transcription of a DNA sequence, translation of an mRNA transcript, and secretion of a fusion protein product, or an antibody, or an antibody fragment thereof. [00103] The term "genome-edited" as used herein means having a gene added, deleted, or modified to be non-functional. Thus, in certain aspects, a "gene- edited T cell" or a “modified T cell” is a T cell that has had a gene such as a CAR recognizing at least one antigen added; and/or has had a gene such as the gene(s) to the antigen(s) that are recognized by the CAR deleted. [00104] A "healthy donor," as used herein, is one who does not have a malignancy (e.g., a plasma-cell malignancy). [00105] As used herein, the term "host cell" refers to a prokaryotic cell and/or a eukaryotic cell into which a recombinant expression vector can be introduced. [00106] Unless otherwise specified, the terms "protein", "polypeptide", and "peptide" may be used as an interchangeable concept. [00107] The term "immune checkpoint inhibitor" refers to a type of drug that blocks certain proteins made by some types of immune system cells, such as T cells, and some cancer cells. [00108] The term "immune effector cell," as used herein, are cells that are actively involved in the destruction of tumor cells, e.g., possess anti-tumor activity. These cells may include, but are not limited to, natural killer (NK) cells, cytotoxic T cells, and memory T cells. [00109] The term "chimeric antigen receptor (CAR)-bearing immune effector cells” or “chimeric antigen receptor (CAR) modified immune effector cells” are immune effector cells that express a chimeric antigen receptor. These cells may include, but are not limited to, CAR-T cells or CAR-bearing NK cells. [00110] The term "CAR-T cell" means a CAR-T cell that expresses a chimeric antigen receptor. [00111] A dual CAR-T cell (equivalently, dCAR-T) is a CAR-T cell that expresses two distinct chimeric antigen receptor polypeptides with affinity to different target antigens expressed within the same effector cell or separate epitopes within the same target protein, wherein each CAR functions independently. The CAR may be expressed from a single polynucleotide sequence or multiple polynucleotide sequences. [00112] A tandem CAR-T cell (equivalently, tCAR-T) is a CAR-T cell with a single chimeric antigen polypeptide containing two distinct antigen recognition domains with affinity to different targets or separate epitopes within the same target protein, wherein the antigen recognition domains are linked through a peptide linker and share common costimulatory domain(s), and wherein binding of either antigen recognition domain will signal though a common costimulatory domains(s) and signaling domain. [00113] The term "patient" is generally synonymous with the term "subject" and includes all mammals including humans. [00114] As used herein, the term "signal sequence," or equivalently, "signal peptide," refers to a fragment directing the secretion of a biologically active molecule drug and a fusion protein, and it is cut off after being translated in a host cell. The signal sequence as used herein is a polynucleotide encoding an amino acid sequence initiating the movement of the protein penetrating the endoplasmic reticulum (ER) membrane. Useful signal sequences include an antibody light chain signal sequence, e.g., antibody 14.18 (Gillies et al.., J. Immunol. Meth 1989.125:191-202), an antibody heavy chain signal sequence, e.g., MOPC141 an antibody heavy chain signal sequence (Sakano et al., Nature, 1980.286: 676-683), and other signal sequences know in the art (e.g., see Watson et al., Nucleic Acid Research, 1984.12:5145-5164). The characteristics of signal peptides are well known in the art, and the signal peptides conventionally having 16 to 30 amino acids, but they may include more or less number of amino acid residues. Conventional signal peptides consist of three regions of the basic N-terminal region, a central hydrophobic region, and a more polar C-terminal region. [00115] The term "therapeutically acceptable" refers to substances which are suitable for use in contact with the tissues of patients without undue toxicity, irritation, and allergic response, are commensurate with a reasonable benefit/risk ratio, and/or are effective for their intended use. [00116] The term "therapeutically effective" is intended to qualify the amount of active ingredients used in the treatment of a disease or disorder or on the effecting of a clinical endpoint. [00117] As used herein, the terms "transduced", "transformed", and "transfected" refer to the introduction of a nucleic acid (e.g., a vector) into a cell using a technology known in the art. [00118] As used herein, the term "vector" is understood as a nucleic acid means which includes a nucleotide sequence that can be introduced into a host cell to be recombined and inserted into the genome of the host cell, or spontaneously replicated as an episome. The vector may include linear nucleic acids, plasmids, phagemids, cosmids, RNA vectors, virus vectors, and analogs thereof. Examples of the virus vectors may include retroviruses, adenoviruses, and adeno-associated viruses, but are not limited thereto. [00119] Each amino acid sequence described herein by virtue of its identity or similarity percentage with a given amino acid sequence respectively has in a further preferred aspect an identity or a similarity of at least 60%, at least 61%, at least 62%, at least 63%, at least 64%, at least 65%, at least 66%, at least 67%, at least 68%, at least 69%, at least 70%, at least 71%, at least 72%, at least 73%, at least 74%, at least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% with the given nucleotide or amino acid sequence, respectively. The terms “homology”, “sequence identity” and the like are used interchangeably herein. Sequence identity is described herein as a relationship between two or more amino acid (polypeptide or protein) sequences or two or more nucleic acid (polynucleotide) sequences, as determined by comparing the sequences. In a preferred aspect, sequence identity is calculated based on the full length (in amino acids or nucleotides) of two given SEQ ID NOS or based on a portion thereof. A portion of a full-length sequence may be referred to as a fragment, and preferably means at least 50%, 60%, 70%, 80%, 90%, or 100% of the length (in amino acids or nucleotides) of a reference sequence. "Identity" also refers to the degree of sequence relatedness between two amino acid sequences, or between two nucleic acid sequences, as the case may be, as determined by the match between strings of such sequences. The degree of sequence identity between two sequences can be determined, for example, by comparing the two sequences using computer programs commonly employed for this purpose, such as global or local alignment algorithms. Non- limiting examples include BLASTp, BLASTn, Clustal W, MAFFT, Clustal Omega, AlignMe, Praline, GAP, BESTFIT, or another suitable method or algorithm. A Needleman and Wunsch global alignment algorithm can be used to align two sequences over their entire length or part thereof (part thereof may mean at least 50%, 60%, 70%, 80%, 90% of the length of ths sequence), maximizing the number of matches and minimizes the number of gaps. Default settings can be used and preferred program is Needle for pairwise alignment (in an aspect, EMBOSS Needle 6.6.0.0, gap open penalty 10, gap extent penalty: 0.5, end gap penalty: false, end gap open penalty: 10 , end gap extent penalty: 0.5 is used) and MAFFT for multiple sequence alignment ( in an aspect, MAFFT v7Default value is: BLOSUM62 [bl62], Gap Open: 1.53, Gap extension: 0.123, Order: aligned , Tree rebuilding number: 2, Guide tree output: ON [true], Max iterate: 2 , Perform FFTS: none is used). [00120] "Similarity" between two amino acid sequences is determined, for example, by comparing the amino acid sequence and its conserved amino acid substitutes of one polypeptide to the sequence of a second polypeptide. Similar algorithms used for determination of sequence identity may be used for determination of sequence similarity. Optionally, in determining the degree of amino acid similarity, the skilled person may also take into account so-called conservative amino acid substitutions. As used herein, “conservative” amino acid substitutions refer to the interchangeability of residues having similar side chains. Examples of classes of amino acid residues for conservative substitutions are given in the Tables below:

Alternative conservative amino acid residue substitution classes :

Alternative physical and functional classifications of amino acid residues:

[00121] For example, a group of amino acids having aliphatic side chains is glycine, alanine, valine, leucine, and isoleucine; a group of amino acids having aliphatic- hydroxyl side chains is serine and threonine; a group of amino acids having amide- containing side chains is asparagine and glutamine; a group of amino acids having aromatic side chains is phenylalanine, tyrosine, and tryptophan; a group of amino acids having basic side chains is lysine, arginine, and histidine; and a group of amino acids having sulphur-containing side chains is cysteine and methionine. Preferred conservative amino acids substitution groups are: valine-leucine-isoleucine, phenylalanine-tyrosine, lysine-arginine, alanine-valine, and asparagine-glutamine. Substitutional variants of the amino acid sequence disclosed herein are those in which at least one residue in the disclosed sequences has been removed and a different residue inserted in its place. Preferably, the amino acid change is conservative. Preferred conservative substitutions for each of the naturally occurring amino acids are as follows: Ala to Ser; Arg to Lys; Asn to Gln or His; Asp to Glu; Cys to Ser or Ala; Gln to Asn; Glu to Asp; Gly to Pro; His to Asn or Gln; Ile to Leu or Val; Leu to Ile or Val; Lys to Arg; Gln or Glu; Met to Leu or Ile; Phe to Met, Leu or Tyr; Ser to Thr; Thr to Ser; Trp to Tyr; Tyr to Trp or Phe; and, Val to Ile or Leu. [00122] As used herein “binds”, refers to a polypeptide (including antibodies) or receptor, binding reaction which is determinative of the presence of the protein or polypeptide or receptor in a heterogeneous population of proteins and other biologics. Thus, under designated conditions (e.g. immunoassay conditions in the case of an antibody), a specified ligand or antibody “specifically binds” to its particular “target” (e.g. an antibody specifically binds to an antigen) when it does not bind in a significant amount to other proteins present in the sample or to other proteins to which the ligand or antibody may come in contact in an organism. II. CAR Expressing Cells [00123] The disclosure provides chimeric antigen receptor (CAR) compositions, methods of making and using the same. [00124] The phrase "chimeric antigen receptor (CAR)," as used herein, refers to a recombinant fusion protein that has an extracellular domain, i.e. an antigen recognition domain or target element, coupled to an intracellular domain comprising co- stimulatory and signaling domains, which directs the cell to perform a specialized function upon binding of an antigen. The terms "artificial T cell receptor," "chimeric T- cell receptor," and "chimeric immunoreceptor'' may each be used interchangeably herein with the term "chimeric antigen receptor." Chimeric antigen receptors are distinguished from other antigen binding agents by their ability to both bind MHC- independent antigen and transduce activation signals via the components of the intracellular domain. [00125] A chimeric antigen receptor (CAR) polypeptide includes a signal peptide, an antigen recognition domain, a hinge region, a transmembrane domain, at least one co-stimulatory domain, and a signaling domain. The hinge region and the antigen recognition domain may be collectively referred to as the extracellular domain. The at least one co-stimulatory domain and signaling domain may be collectively referred to as the intracellular domain. The extracellular and intracellular domains of a CAR are discussed in more detail below. [00126] First-generation CARs include CD3 ζ as a signaling domain, whereas second-generation CARs include at least one single co-stimulatory domain, which can be derived from various proteins. Examples of co-stimulatory domains include, but are not limited to, CD28, CD2, 4-1BB (CD137), and OX-40 (CD134). Third generation CARs include two co-stimulatory domains selected from, but not limited to, CD28, 4-1BB (CD137), OX-40 (CD134), and CD2. [00127] The signal peptide includes a peptide sequence that directs the transport and localization of the peptide and any attached polypeptide within a cell, e.g. to a certain cell organelle (such as the endoplasmic reticulum) and/or the cell surface. The terms "signal peptide" and "leader sequence" are used interchangeably. [00128] The signal peptide directs the transport of any secreted or transmembrane protein to the cell membrane and cell surface allowing correct localization of the polypeptide. In particular, the signal peptide of the present disclosure directs the polypeptide to the cellular membrane, wherein the extracellular portion, i.e. antigen recognition domain or target element of the polypeptide is displayed on the cell surface, the transmembrane portion spans the plasma membrane, and the signaling domain is in the cytoplasmic portion, or interior of the cell. [00129] In some aspects, the signal peptide includes the signal peptide from human CD8a. In some aspects, the signal peptide may be a functional fragment of the CD8a signal peptide. A functional fragment includes a fragment of at least 10 amino acids of the CD8a signal peptide that directs the appended polypeptide to the cell membrane and cell surface. [00130] The antigen recognition domain or target element of a chimeric antigen receptor includes a polypeptide that is selective for or targets an antigen, receptor, peptide ligand, protein ligand of the target, or a polypeptide of the target. [00131] The antigen recognition domain of a chimeric antigen receptor recognizes and specifically binds an antigen, typically a surface-expressed antigen of a malignancy. An antigen recognition domain specifically binds an antigen when, for example, it binds the antigen with an affinity constant or affinity of interaction (KD) between about 0.1 pM to about 10 pM, preferably about 0.1 pM to about 1 pM, more preferably about 0.1 pM to about 100 nM. Methods for determining the affinity of interaction are well-known in the art. An antigen-specific extracellular domain suitable for use in a CAR of the present disclosure may be any antigen-binding polypeptide, a wide variety of which are well-known in the art. In some instances, the antigen-binding domain is a single chain Fv (scFv). The single-chain variable fragment (scFv) is expressed on the surface of a CAR-immune effector cell and confers antigen specificity. The scFv is derived from the portion of an antibody that specifically recognizes a target protein. Other antibody-based recognition domains (cAb VHH (camelid antibody variable domains) and humanized versions thereof, lgNAR VH (shark antibody variable domains) and humanized versions thereof, sdAb VH (single domain antibody variable domains) and "camelized" antibody variable domains are suitable for use. In some instances, T-cell receptor (TCR) based recognition domains such as single chain TCR (scTv, single chain two-domain TCR containing VαVβ) are also suitable for use. [00132] In some aspects, an antigen specifically bound by the chimeric antigen receptor of a CAR-immune effector cell, and optionally the antigen for which the CAR-immune effector cell is deficient, is an antigen expressed on a malignant cell, more preferably an antigen that is overexpressed on malignant cell in comparison to a non- malignant cell. A "malignant cell" is a cell derived from a cell malignancy. The term "T- cell malignancy" refers to a broad, highly heterogeneous grouping of malignancies derived from T-cell precursors, mature T cells, or natural killer cells. Non-limiting examples of T-cell malignancies include T-cell acute lymphoblastic leukemia/lymphoma (T-ALL), T-cell large granular lymphocyte (LGL) leukemia, human T-cell leukemia virus type 1-positive (HTLV-1 +) adult T-cell leukemia/lymphoma (ATL), T-cell prolymphocytic leukemia (T-PLL), and various peripheral T-cell lymphomas (PTCLs), including but not limited to angioimmunoblastic T-cell lymphoma (AITL), ALK positive anaplastic large cell lymphoma, and ALK-negative anaplastic large cell lymphoma. Suitable CAR targeted antigens may include antigens found on the surface of abnormal myeloblast, a red blood cell, or platelet, i.e., acute myeloid leukemia (AML). Leukemia may affect red blood cells, white blood cells, and platelets. Suitable CAR targeted antigens can also include antigens found on the surface of a multiple myeloma cell, i.e., a malignant plasma cell. [00133] For instance, in one aspect, FCRL5 is a suitable CAR targeted antigen expressed on a malignant cell. In some aspects, a CAR-immune effector cell of the present disclosure comprises an antigen recognition domain of a chimeric antigen receptor that specifically binds to FCRL5. [00134] In one aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLQESGPGLVKPSQTLSLTCTVSGGSISSGGYFWSWIRQHPGKGLEWIGFIYYSG NTYYNPSLKSRVTISVDTSKSQFSLELSSVTAADTAVYYCAREGAAAGTFHYWGQGTL VTVSS (SEQ ID NO: 2) and/or a VL comprising the amino acid sequence: DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIK (SEQ ID NO: 3). [00135] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLIQPGGSLRLSCAASGLTVSSNYMSWVRQAPGKGLEWVSLIYTGGST YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGWVAFDIWGQGTMVTVS S (SEQ ID NO: 4) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSLTFGGGTKVDIK (SEQ ID NO: 5). [00136] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLIQPGGSLRLSCAASGFTVSRNYMTWVRQAPGKGLEWVSVIYSGGTT YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGVVAFDIWGQGTMVTVS S (SEQ ID NO: 6) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPPLTFGGGTKVEIK (SEQ ID NO: 7). [00137] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLIQPGGSLRLSCAASGFTVSRNYMTWVRQAPGKGLEWVSVIYTGGST YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGGVAFDIWGQGTMVTVS S (SEQ ID NO: 8) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFALYYCQQYGNSPMSTFGQGTRLEIK (SEQ ID NO: 9). [00138] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLIQPGGSLRLSCAASGFTVSRNYMTWVRQAPGKGLEWVSVIYSGGST YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGVIAFDYWGQGILVTVSS (SEQ ID NO: 10) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPITFGQGTRLEIK (SEQ ID NO: 11). [00139] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMHWVRQAPGQGLEWMGWINPNS GGTKYAQKFQGRVTMTRDTSISTAYMELRRLTSDDTAVYYCVREGGSYYYASSGYDY VPFEYWGQGTLVTVSS (SEQ ID NO: 12) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSMYTFGQGTKVEIK (SEQ ID NO: 13). [00140] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFNGYYMHWVRQAPGQGLEWMGWISAYN GNTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCVREGGSYYYASSGYDY VPFEYWGQGTLVTVSS (SEQ ID NO: 14) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKLEIK (SEQ ID NO: 15) [00141] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKTSGYTFTGYYIHWVRQAPGQGLEWMGWISAYNG NTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCAREGGSYYYANGGYDY VPFEYWGQGTLVTVSS (SEQ ID NO: 16) and/or a VL comprising the amino acid sequence: DIQMTQSPSFLSASVGDRVTITCRASQGISSYLAWYQQKPGKAPKLLIYAASSLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPITFGQGTRLEIK (SEQ ID NO: 17). [00142] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMTPNS VNTGYAQKFQGRVTMTTDTSTSTAYMELSRLRSDDTAVYYCARGPSIMITFGGVIVTP FDYWGQGTLVTVSS (SEQ ID NO: 18) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKVDIK (SEQ ID NO: 19). [00143] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMNPNS GNTGYAQKFQGRVTMTRNTSISTAYMELSSLRSEDTAVYYCARGPSILITFGGVIVTPF DYWGQGTLVTVSS (SEQ ID NO: 20) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPYTFGQGTKVDIK (SEQ ID NO: 21). [00144] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMTPNS GNTGYAQKFQGRVTMTRNTSISTAYMELSSLRSEDTAVYYCARGPSILITFGGVIVTPF DYWGQGTLVTVSS (SEQ ID NO: 22) and/or a VL comprising the amino acid sequence: EIVLTQSPATLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASNRATGI PARFSGSGSGTDFTLTISSLQPEDFAVYYCQQYGSSPYTFGQGTRLEIK (SEQ ID NO: 23). [00145] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYVHWVRQAPGQGLEWMGWINPNS GGTVSAQKFQGRVTMTRDTSISTAYMELSGLKSDDTAVYSCARFCSITSCYMRGFDY WGQGTLVTVSS (SEQ ID NO: 24) and/or a VL comprising the amino acid sequence: DIQMTQSPSSVSASVGDRVTITCRASQSISSWLAWYQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPLTFGGGTKVDIK (SEQ ID NO: 25). [00146] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLEWMGWINPNSG GTDSAQKFQGRVTMTRDTSISTAYMELSRLRSDDTAVYYCAREGGSYYYANGGYYYL PFDFWGQGTLVTVSS (SEQ ID NO: 26) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYNNWPPTFGQGTKVDIK (SEQ ID NO: 27). [00147] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMQWVRQAPGQGLEWMGWINPNS GDTNYAQKFQGRVTMTRDTSINTVYMELSRLRSDDTAVYYCAREGGSYYYAGGGYY YLPFDYWGQGTLVTVSS (SEQ ID NO: 28) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSLFTFGPGTKLEIK (SEQ ID NO: 29). [00148] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLEWMGLINPNSG GTNYAQKFQGRVTMTRDTSIGTAYMELSRLRSDDSAIYYCTREGGSYYYANGGYYYL PFDFWGQGTLVTVSS (SEQ ID NO: 30) and/or a VL comprising the amino acid sequence: EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKVDIK (SEQ ID NO: 31). [00149] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYLYWVRQAPGQGLEWMGWINPNS GDTSYVQKFQGRVTMTRDTSTSTVYMELSRLRSDDTAVYYCARRYSGYLDYWGQGT LVTVSS (SEQ ID NO: 32) and/or a VL comprising the amino acid sequence: DIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPVTFGGGTKVEIK (SEQ ID NO: 33). [00150] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMYWVRQAPGQGLEWMGLINPNS GDTSYAQKFQGRVTMTRDTSISTVYMELSGLTSDDTAVYYCARRYSGYLDYWGQGTL VTVSS (SEQ ID NO: 34) and/or a VL comprising the amino acid sequence: DIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPITFGQGTRLEIK (SEQ ID NO: 35). [00151] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMEWVRQAPGQGLEWMGLINPNS GGTNYEENFKGRVTMTRDTSISTAYMELSRLRSDDTAVYYCARRDSGFLDYWGQGTL VTVSS (SEQ ID NO: 36) and/or a VL comprising the amino acid sequence: DIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKAGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPLTFGGGTKVEIK (SEQ ID NO: 37). [00152] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLQESGPGLVKPSETLSLTCTVSGGSVSSGSYYWSWIRQPPGKGLEWIGFIYYSG STYYNPSLKSRVTISVDTSKNQFSLKLTSVTAADTAVYYCARDGGAAAGTLDYWGQGT LVTVSS (SEQ ID NO: 38) and/or a VL comprising the amino acid sequence: DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIK (SEQ ID NO: 39). [00153] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLVKPGGSLRLSCAASGFTFSSYDMHWVRQAPGKGLVWVSRIDSYGT YTNYADSVKGRFTISRDNAKNTLYLQMNNLRAEDTAVYYCARIAATASGYWGQGTPVT VSS (SEQ ID NO: 40) and/or a VL comprising the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQRISNYLNWYQQKPGKAPKPLIYAASRLQSGV PSRFSGSGSVTDFTLTISSLQPEDFASYYCQQSYSTPYTFGQGTKVEIK (SEQ ID NO: 41). [00154] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QITLKESGPTLVKPTQTLTLTCTFSGFSLSTSGVGVGWIRQPPGKALEWLALIYWNDDK RYSPSLKSRLTITKDTSKNQVVLTMTNVDPVDTATYYCAHRRNSRWYPFDYWGQGTL VTVSS (SEQ ID NO: 42) and/or a VL comprising the amino acid sequence: DIQLTQSPSFLSASVGDRVTITCRASQGISSYLAWYRQKPGKAPKLLIYAVSILQSGVPS RFSGSGSGTDFTLTISSLQPEDFATYYCQQLNSYPITFGQGTRLEIK (SEQ ID NO: 43). [00155] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGADVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLEWMGWINPNSG GTNYEQKFQGRVTMTRDTSITTAYMEVSRLRSDDTAVYYCARRWNYGIDYWGQGTL VTVSS (SEQ ID NO: 44) and/or a VL comprising the amino acid sequence: DIVMTQTPLSSPVTLGQPASISCRSSQSLVYSDGNTYLSWLQQRPGQPPRLLIYKISNR FSGVPDRFSGSGAGTDFTLKISRVEAEDVGVYYCMQAIQFPYTFGQGTKLEIK (SEQ ID NO: 45). [00156] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYDG SNKYYVDSVKGRVTISRDNSKNTLYLQMNSLRAEDTAVYYCARGGFDYLPLMDVWGK GTTVTVSS (SEQ ID NO: 46) and/or a VL comprising the amino acid sequence: DIVMTQSPDSLAVSLGERAIINCKSSQSVLHSSDNKNYLAWYQQKPGQPPKLLIHWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPWTFGQGTKVEIK (SEQ ID NO: 47). [00157] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLQESGPGLVKPSQTLSLTCTVSGGSISSGGYYWSWIRQHPGKGLEWIGYIYYSG STYYNPSLKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCARDGHYDSIGYYFDYWGQ GTLVTVSS (SEQ ID NO: 48) and/or a VL comprising the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQNPGKAPKLLIFTASSLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPRTFGQGTKVEIK (SEQ ID NO: 49). [00158] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMNPTS GNTGYAQKFQGRVTMTKNTSISTAYMELSNLRSEDTAVYFCARGLYKWNYWGQGTL VTVSS (SEQ ID NO: 50) and/or a VL comprising the amino acid sequence: EIVMTQSPATLSVSPGERATLSCRASQSVSRNLAWYQQKPGQAPRLLIYGASTRATGI PARFSGSGSGTEFTLTISSLQSEDFAVYSCQQYTNWPALTFGGGTKVEIK (SEQ ID NO: 51). [00159] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGVLVQPGGSLRLSCAASGFTFSSYWMHWVRQAPGKGLMWVSRIDSDGT TTNYADSVKGRFTISRDNAKNTLNLQMNSLRAEDTAVYYCARIAATASGYWGQGTLVT VSS (SEQ ID NO: 52) and/or a VL comprising the amino acid sequence: DIQMTQSPSSLSTSVGDRVTITCRASQSISSYLNWYQQKPGKAPNLLIYAASSLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPITFGQGTRLEIK (SEQ ID NO: 53). [00160] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QLQLQESGPGLVKPSETLSLICTVSGGSISSSNYYWGWIRQPPGKGLEWIGSIYYSGS TYYNPSLKSRVTISVDTSNNQFSLRLNSVTAADTAVYYCAREGELKYWFFDLWGRGTL VTVSS (SEQ ID NO: 54) and/or a VL comprising the amino acid sequence: DIQMTQSPSTLSASVGDRVTITCRASQSIISWLAWYQEKPGKAPKVLIYKASSLESGVP SRFSGSGSGTEFTLTISSLQPDDFATYYCQQYNSYSRTFGQGTKVEIK (SEQ ID NO: 55). [00161] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLDWMGWINPNSG VTNYAQKFQGRVTMTRDTSISTAYMDLSRLRSDDTAVYSCARDRGGDSPDAFDLWG QGTMVTVSS (SEQ ID NO: 56) and/or a VL comprising the amino acid sequence: DIVMTQSPDSLTVSLGERATINCKSSQSVLYSSKNKNYLAWYQQKPGQPPKLLIYWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVFYCQQYYSTPWTFGHGTKVEIK (SEQ ID NO: 57). [00162] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTNYGITWVRQAPGQGLEWMGWISAYDG YTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARDYDFWSGLDPWGQG TLVTVSS (SEQ ID NO: 58) and/or a VL comprising the amino acid sequence: DIVMTQSPLSLPVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKPGQSPQLLIYLGSN RASGVPDRFSGSGSGTDFTLKISRVEAEDVGIYYCMQALQTPWTFGRGTKVEIK (SEQ ID NO: 59). [00163] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLVQPGGSLRLSCAASGFILSSYDMHWVRQATGKGLEWVSGIGTAGET YYSGSVKGRFTISRENAKNSLYLQMNSLRAGDTAVYYCAREDYFYYMDVWGKGTTVT VSS (SEQ ID NO: 60) and/or a VL comprising the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQSIRSYLNWYQQKPGKAPKLLIYAASTLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTRTFGQGTKVEIK (SEQ ID NO: 61). [00164] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGDLVKPGGSLRLSCAASGFTFNNAWMSWVRQAPGKGLEWVGRIQSKTD GGTTDYAAPVKGRFTISRDDSKNTLYMQMNSLKAEDTAVYYCTSILTGYYYYYYMDV WGRGTTVTVSS (SEQ ID NO: 62) and/or a VL comprising the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQGISIYLAWYQQKPGKVPKLLIYAASSLQSGVP SRFSGSKSGTDFTLTISSLQPEDVATYYCQKYDSAPFTFGPGTKVDIK (SEQ ID NO: 63). [00165] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVANIKQDGI KKYYVDSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDQYCTNGVCYGGWF DPWGQGTLVTVSS (SEQ ID NO: 64) and/or a VL comprising the amino acid sequence: DIQMTQSPSTLSASVGDRVTITCRASQSISSWLAWYQQKPGKAPKVLIYKASSLESGV PSRFSGSGSGTDFTLTISSMQPDDFATYYCQQYNGYSRTFGQGTKVEIK (SEQ ID NO: 65). [00166] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLVQPGGSLRLSCAASGFTFNSYAMSWVRQAPGKGLEWVSAISGSGD TTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYHCVKGWKHLWSDYFDHWG PGTLVTVSS (SEQ ID NO: 66) and/or a VL comprising the amino acid sequence: EIVMTQSPATQSVSPGERATLSCRASQSVNNNLAWYQQKPGQAPRLLIYGASTRATGI PARFSGSGSGTEFTLTISSLQSEDFAVYYCQQYNNWPIAFGQGTRLEIK (SEQ ID NO: 67). [00167] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYVMHWVRQAPGKGLEWVSTINWNGD YIGYADSVKGRFTISRDNAKNSLYLQMNSLRAEDTALYYCAKASYMDVWGKGTTVTVS S (SEQ ID NO: 68) and/or a VL comprising the amino acid sequence: DVVMTQSPLSLPVTLGQPASVSCRSSQSLVYSDGNTYLNWFQQRPGQSPRRLIYKVS NRDSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGTHWTWTFGQGTKLEIK (SEQ ID NO: 69). [00168] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVESGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTT NYAQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCARDELYSSSWYGVYWGQGT LVTVSS (SEQ ID NO: 70) and/or a VL comprising the amino acid sequence: DIVMTQSPLSLPVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKPGQSPQLLIYLGSN RASGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQALQTPWTFGQGTKLEIK (SEQ ID NO: 71). [00169] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYYMYWVRQAPGPGLEWMGIINPSGG RTTYAQKFQGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCARRDDYGALDYWGQGT LVTVSS (SEQ ID NO: 72) and/or a VL comprising the amino acid sequence: DIQMTQSPSSLSASVGDRVTITCRASQSIRNYLNWYQQKPGKAPKLLIYDTSNLQSGV PSRFSGSGSGTDLTLTISSLQPDDFATYYCQQSYSIPITFGQGTRLEIK (SEQ ID NO: 73). [00170] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLQQSGPGLVKPSQTLSLTCAISGDSVSSNSAAWNWIRQSPSRGLEWLGRTYYRS KWYNDYAASVKSRITINPDTSKNQFSLQLNSVTPEDTAVYYCARDDWYFDLWGRGTL VTVSS (SEQ ID NO: 74) and/or a VL comprising the amino acid sequence: DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQQPGLPPKLLIFWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSSPYTFGQGTKVEIK (SEQ ID NO: 75). [00171] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYEG SNKYFADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARDRGTMVRGLHYFDY WGQGTLVTVSS (SEQ ID NO: 76) and/or a VL comprising the amino acid sequence: AIQMTQSPSSLSASVGDRVTITCRASQDIRNDLGWYQQKPGKAPKLLIYGASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCLQDYNYPWTFGQGTKVEIK (SEQ ID NO: 77). [00172] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGVVVQPGGSLRLSCAASGFTFDDYTMHWVRQAPGKGLEWVSLITWDGG RTYYADSVKGRFTISRDNSKNSLYLQMNSLRTEDTALYYCAKDISLDYWGQGTLVTVS S (SEQ ID NO: 78) and/or a VL comprising the amino acid sequence: DVVMTQSPLSLSVTLGQPASISCRSSQSLVYSDGNTYLNWFQQRPGQSPRRLIYKVS NRDSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGIHWPLTFGGGTKVEIK (SEQ ID NO: 79). [00173] In another exemplary aspect, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence: EVQLVESGGGLVKPGGSLRLSCAASGFTFSNAWMSWVRQAPGKGLEWVGRIKSKTD GGTTDYAAPVKGRFTISRDDSKNTLYLQMNSLRTEDTAVYYCSTTSLSYYDILTGYYKD YYYYYMDVWGKGTTVTVSS (SEQ ID NO: 80) and/or a VL comprising the amino acid sequence: DIQMTQSPSSVSTSVGDRVTITCRASQGISSWLAWFQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPLTFGGGTKVEIK (SEQ ID NO: 81). [00174] In some aspects, an anti-FCRL5 antigen recognition domain of a chimeric antigen receptor of the disclosure comprises a VH and/or VL, comprising one or more amino acid sequences of SEQ ID NO: 2-81, wherein the said amino acid sequence comprises at least 60% sequence identity or similarity with one or more of amino acid sequence SEQ ID NOS: 2-81. In some aspect, the identity or similarity is of at least 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%. [00175] In some aspects, disclosed CAR comprises an anti-FCRL5 antigen recognition domain comprising a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [00176] In some aspects, disclosed CAR comprises an anti-FCRL5 antigen recognition domain comprising a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00177] In some aspects, disclosed CAR comprises an anti-FCRL5 antigen recognition domain comprising a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, and a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00178] In some aspects, disclosed CAR comprises an anti-FCRL5 antigen recognition domain comprising a VH with 100% identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [00179] In some aspects, disclosed CAR comprises an anti-FCRL5 antigen recognition domain comprising a VL with 100% identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00180] In some aspects, disclosed CAR comprises an anti-FCRL5 antigen recognition domain comprising a VH with 100 identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, and a VL with 100% identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00181] The hinge domain is a structure between the antigen recognition domain and the cell plasma membrane; these sequences are generally derived from IgG subclasses (such as IgG1 and IgG4), IgD and CD8 domains, of which IgG1 has been the most extensively used for CAR construction. Currently, studies of the hinge domain mainly focus on the following four aspects: 1) reducing binding affinity to the Fcγ receptor, thereby eliminating off-target activation; 2) enhancing the single-chain variable fragment (scFv) flexibility, thereby relieving the spatial constraints between tumor antigens and CARs, and in turn promoting synapse formation between the CAR- immune effector cells and target cells; 3) reducing the distance between an scFv and the target epitope; and 4) facilitating the detection of CAR expression using anti-Fc reagents. [00182] In one aspect, the hinge domain includes a hinge domain of a human protein selected from CD28, 4-1BB (CD137), OX-40 (CD134), CD3ζ, T cell receptor α or β chain, CD45, CD4, CD5, CD8, CD8α, CD9, CD16, CD22, CD33, CD37, CD64, CD80, CD86, ICOS, CD154, functional derivatives and/or combinations thereof. [00183] Typically, the extracellular domain, i.e. an antigen recognition domain or target element is linked to the intracellular domain, i.e., the co-stimulatory and signaling domain(s) of the chimeric antigen receptor by a transmembrane domain. A transmembrane domain traverses the cell membrane, anchors the CAR to the immune effector cell surface, and connects the extracellular domain to the intracellular domain, thus impacting expression of the CAR on the immune effector cell surface. [00184] The transmembrane domain includes a hydrophobic polypeptide that spans the cellular membrane. In particular, the transmembrane domain spans from one side of a cell membrane (extracellular) through to the other side of the cell membrane (intracellular or cytoplasmic). [00185] The transmembrane domain may be in the form of an alpha helix or a beta barrel, or combinations thereof. The transmembrane domain may include a polytopic protein, which has many transmembrane segments, each alpha-helical, beta sheets, or combinations thereof. [00186] In one aspect, the transmembrane domain that is naturally associated with one of the domains in the CAR is used. In another aspect, the transmembrane domain is 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. [00187] For example, the transmembrane domain is selected from a transmembrane domain of a T-cell receptor α or β chain, a CD3ζ chain, CD28, CD3s, CD45, CD4, CD5, CD7, CD8, CD9, CD16, CD22, CD33, CD37, CD64, CD80, CD86, CD68, OX-40 (CD134), 4-1BB (CD137), ICOS, CD41, CD154, functional derivatives and/or combinations thereof. [00188] A chimeric antigen receptor of the present disclosure may comprise one or more costimulatory domain and/or one or more spacers. A costimulatory domain is derived from costimulatory proteins that enhance cytokine production, proliferation, cytotoxicity, and/or persistence in vivo. [00189] In one embodiment, the co-stimulatory domain is selected from OX- 40 (CD134), CD27, CD28, CD30, CD40, PD-1, CD2, CD7, CD258, Natural killer Group 2 member C (NKG2C), Natural killer Group 2 member D (NKG2D), B7-H3, a ligand that binds to at least one of CD83, ICAM-1, LFA-1 (CD1 la/CD18), ICOS, and 4-1BB (CD137), CDS, ICAM-1, LFA-1 (CDla/CD18), CD40, CD27, active fragments thereof, functional derivatives thereof, and combinations thereof. [00190] A chimeric antigen receptor of the present disclosure also comprises a signaling domain that provides an intracellular signal to the immune effector cell upon antigen binding to the antigen recognition domain. The signaling domain of a chimeric antigen receptor of the present disclosure is responsible for activation of at least one of the effector functions of the immune effector cell in which the chimeric receptor is expressed. The term "effector function" refers to a specialized function of a differentiated cell. An effector function of an immune cell, for example, may be cytolytic activity or helper activity including the secretion of cytokines. An effector function in a naive, memory, or memory-type immune cell may also include antigen-dependent proliferation. Thus, the term "intracellular domain" refers to the intracellular portion of a CAR that transduces the effector function signal upon binding of an antigen to the extracellular domain and directs the immune cell to perform a specialized function. Non-limiting examples of suitable signaling domains include the zeta chain of the immune-cell receptor or any of its homologs (e.g., eta, delta, gamma, or epsilon), MB-1 chain, 829, FcRIII, FcRI, and combinations of signaling molecules, such as CD3ζ and CD28, CD27, 4-1BB (CD137), DNAX-activating protein 10 (DAP10), OX-40 (CD134), and combinations thereof, as well as other similar molecules and fragments. Signaling domains of other activating proteins may be used, such as FcγRIII and FcεRI. While usually the entire signaling domain will be employed, in many cases it will not be necessary to use the entire intracellular polypeptide. To that extent, a truncated portion of the signaling domain may be used as long as it still transduces the effector function signal. The term intracellular domain is also meant to include any truncated portion of the intracellular domain sufficient to transduce the effector function signal. Alternatively, or in addition, CAR-immune effector cells encompassed by the present disclosure may further comprise one or more suicide genes. As used herein, "suicide gene" refers to a nucleic acid sequence introduced to a CAR-immune effector cell by standard methods known in the art that, when activated, results in the death of the CAR-immune effector cell. Suicide genes may facilitate effective tracking and elimination of the CAR-immune effector cells in vivo if required. Facilitated killing by activating the suicide gene may occur by methods known in the art. Suitable suicide gene therapy systems known in the art include, but are not limited to, various the herpes simplex virus thymidine kinase (HSVtk)/ganciclovir (GCV) suicide gene therapy systems or inducible caspase 9 protein. In an exemplary embodiment, a suicide gene is a CD34/thymidine kinase chimeric suicide gene. [00191] Methods for CAR design, delivery and expression in immune cells, and the manufacturing of clinical-grade CAR-immune effector cell populations are known in the art. See, for example, Lee et al., Clin. Cancer Res., 2012, 18(10): 2780-90, hereby incorporated by reference in its entirety. For example, the engineered CARs may be introduced into immune effector cells using retroviruses, which efficiently and stably integrate a nucleic acid sequence encoding the chimeric antigen receptor into the target cell genome. An exemplary method for the viral vector production is described in the Methods to the Examples. Other methods known in the art include, but are not limited to, lentiviral transduction, transposon-based systems, direct RNA transfection, and CRISPR/Cas systems (e.g., type I, type II, or type III systems using a suitable Cas protein such Cas3, Cas4, Cas5, Cas5e (or CasD), Cas6, Cas6e, Cas6f, Cas7, Cas8a1 , Cas8a2, Cas8b, Cas8c, Cas9, Cas10, Casl Od, CasF, CasG, CasH, Csy1 , Csy2, Csy3, Cse1 (or CasA), Cse2 (or CasB), Cse3 (or CasE), Cse4 (or CasC), Csc1 , Csc2, Csa5, Csn2, Csm2, Csm3, Csm4, Csm5, Csm6, Cmr1 , Cmr3, Cmr4, Cmr5, Cmr6, Csb1 , Csb2, Csb3,Csx17, Csx14, Csx10, Csx16, CsaX, Csx3, Csz1 , Csx15, Csf1 , Csf2, Csf3, Csf4, and Cu1966, etc.). [00192] In some aspects, an immune effector cell is selected from the group consisting of a T cell, a Natural Killer (NK) cell, a cytotoxic T lymphocyte (CTL), and a regulatory T cell. [00193] In some aspects, the immune effector cells comprise any leukocyte involved in defending the body against infectious disease and foreign materials. For example, the immune effector cells can comprise lymphocytes, monocytes, macrophages, dendritic cells, mast cells, neutrophils, basophils, eosinophils, or any combinations thereof. In some aspects, the immune effector cells comprise T lymphocytes. [00194] As disclosed herein, T cells can be T cell of any subset, non-limiting examples can include T helper cells (TH cells), Cytotoxic T cells (TC cells, or CTLs), Memory T cells, Regulatory T cells (Treg cells), or Natural killer T (NKT) cells. [00195] T helper cells (TH cells) assist other white blood cells in immunologic processes, including maturation of B cells into plasma cells and memory B cells, and activation of cytotoxic T cells and macrophages. These cells are also known as CD4+ T cells because they express the CD4 glycoprotein on their surface. Helper T cells become activated when they are presented with peptide antigens by MHC class II molecules, which are expressed on the surface of antigen-presenting cells (APCs). Once activated, they divide rapidly and secrete small proteins called cytokines that regulate or assist in the active immune response. These cells can differentiate into one of several subtypes, including TH1, TH2, TH3, TH17, TH9, or TFH, which secrete different cytokines to facilitate a different type of immune response. [00196] Cytotoxic T cells (TC cells, or CTLs) destroy virally infected cells and tumor cells, and are also implicated in transplant rejection. These cells are also known as CD8+ T cells since they express the CD8 glycoprotein at their surface. These cells recognize their targets by binding to antigen associated with MHC class I molecules, which are present on the surface of all nucleated cells. Through IL-10, adenosine and other molecules secreted by regulatory T cells, the CD8+ cells can be inactivated to an anergic state, which prevents autoimmune diseases. [00197] Memory T cells are a subset of antigen-specific T cells that persist long-term after an infection has resolved. They quickly expand to large numbers of effector T cells upon re-exposure to their cognate antigen, thus providing the immune system with “memory” against past infections. Memory cells may be either CD4+ or CD8+. Memory T cells typically express the cell surface protein CD45RO. [00198] Regulatory T cells (Treg cells), formerly known as suppressor T cells, are crucial for the maintenance of immunological tolerance. Their major role is to shut down T cell-mediated immunity toward the end of an immune reaction and to suppress auto-reactive T cells that escaped the process of negative selection in the thymus. Two major classes of CD4+ Treg cells have been described—naturally occurring Treg cells and adaptive Treg cells. [00199] Natural killer T (NKT) cells, not to be confused with natural killer (NK) cells) bridge the adaptive immune system with the innate immune system. Unlike conventional T cells that recognize peptide antigens presented by major histocompatibility complex (MHC) molecules, NKT cells recognize glycolipid antigen presented by an MHC like I, CD1d. In some aspects, NKT cells are invariant natural killer T (iNKT) cells. iNKT cells recognize CD1d and are restricted by their T-cell Receptor (TCR) which in humans is Vα24Jα18 and typically paired with Vβ11. iNKT cells, further reduce graft-versus-host disease (GVHD). [00200] In some aspects, the T cells comprise a mixture of CD4+ cells. In other aspects, the T cells are enriched for one or more subsets based on cell surface expression. For example, in some cases, the T comprise are cytotoxic CD8+ T lymphocytes. In some embodiments, the T cells comprise γδ T cells, which possess a distinct T-cell receptor (TCR) having one γ chain and one δ chain instead of α and β chains. [00201] Natural-killer (NK) cells are CD56+CD3− large granular lymphocytes that can kill virally infected and transformed cells, and constitute a critical cellular subset of the innate immune system. Unlike cytotoxic CD8+ T lymphocytes, NK cells launch cytotoxicity against tumor cells without the requirement for prior sensitization, and can also eradicate MHC-I-negative cells. [00202] In some aspects, immune effector cells can be obtained from the subject to be treated (i.e. are autologous) and can be administered after genetic modification to express CAR with the disclosed anti-FCRL5 antigen recognition domain, as adoptive transfer. In such aspects, adoptive transfer comprises procuring subject’s immune effector cells, followed by genetically modifying the cells to express the disclosed CARs with anti-FCRL5 antigen recognition domain, and infusing the modified cells back into the subject. In some aspects, immune effector cell lines or donor effector cells (allogeneic) are used. The immune effector cells for allogeneic therapy may be collected from a single subject or multiple subjects. Immune effector cells can be obtained from a number of sources, including peripheral blood mononuclear cells, bone marrow, lymph node tissue, cord blood, thymus tissue, tissue from a site of infection, ascites, pleural effusion, spleen tissue, and tumors. Immune effector cells can be obtained from blood collected from a subject using any number of techniques known to the skilled artisan, such as Ficoll™ separation. For example, cells from the circulating blood of an individual may be obtained by apheresis. In some aspects, immune effector cells can be isolated from peripheral blood lymphocytes by lysing the red blood cells and depleting the monocytes, for example, by centrifugation through a PERCOLL™ gradient or by counterflow centrifugal elutriation. A specific subpopulation of immune effector cells can be further isolated by positive or negative selection techniques. For example, immune effector cells can be isolated using a combination of antibodies directed to surface markers unique to the positively selected cells, e.g., by incubation with antibody-conjugated beads for a time period sufficient for positive selection of the desired immune effector cells. Alternatively, enrichment of immune effector cells population can be accomplished by negative selection using a combination of antibodies directed to surface markers unique to the negatively selected cells. [00203] In some aspects, the expression of nucleic acids encoding CARs can be achieved by operably linking a nucleic acid encoding the CAR polypeptide comprising the disclosed anti-FCRL5 antigen recognition domains, to a promoter, and incorporating the construct into an expression vector. Typical cloning vectors contain transcription and translation terminators, initiation sequences, and promoters useful for regulation of the expression of the desired nucleic acid sequence. In some aspects, immune effector cells are further comprises a modification of the endogenous T-cell Receptor Alpha Chain (TRAC) such that endogenous T cell receptor mediated signaling is blocked in the CAR-T cell. [00204] In some aspects, the CAR comprising the disclosed anti-FCRL5 antigen recognition domains, can be cloned into a number of types of vectors. For example, the CAR comprising the disclosed anti-FCRL5 antigen recognition domains can be cloned into a vector including, but not limited to a plasmid, a phagemid, a phage derivative, an animal virus, and a cosmid. In some aspects, non-limiting examples of vectors include expression vectors, replication vectors, probe generation vectors, and sequencing vectors. [00205] Further, the expression vector may be provided to a cell in the form of a viral vector. Viral vector technology is well known in the art. Viruses, which are useful as vectors include, but are not limited to, retroviruses, adenoviruses, adeno- associated viruses, herpes viruses, and lentiviruses. In general, a suitable vector contains an origin of replication functional in at least one organism, a promoter sequence, convenient restriction endonuclease sites, and one or more selectable markers. In some aspects, the polynucleotide vectors are lentiviral or retroviral vectors. [00206] A number of viral based systems have been developed for gene transfer into mammalian cells. For example, the CAR comprising the disclosed anti- FCRL5 antigen recognition domain can be inserted into a vector and packaged in retroviral particles using techniques known in the art. The recombinant virus can then be isolated and delivered to cells of the subject either in vivo or ex vivo. [00207] In some aspects, promoters used herein comprise a strong constitutive promoter sequence. Non-limiting examples of constitutive promoter sequences include cytomegalovirus (CMV), Elongation Growth Factor-1α (EF-1α), simian virus 40 (SV40) early promoter, MND (a synthetic promoter that contains the U3 region of a modified MoMuLV LTR with myeloproliferative sarcoma virus enhancer), mouse mammary tumor virus (MMTV), human immunodeficiency virus (HIV) long terminal repeat (LTR) promoter, MoMuLV promoter, an avian leukemia virus promoter, an Epstein-Barr virus immediate early promoter, a Rous sarcoma virus promoter, as well as human gene promoters such as, but not limited to, the actin promoter, the myosin promoter, the hemoglobin promoter, and the creatine kinase promoter. In some aspects, the promoter can be an inducible promoter. Examples of inducible promoters include, but are not limited to a metallothionine promoter, a glucocorticoid promoter, a progesterone promoter, and a tetracycline promoter. [00208] In order to assess the expression of a CAR polypeptide or portions thereof, the expression vector to be introduced into a cell can also contain either a selectable marker gene or a reporter gene or both to facilitate identification and selection of expressing cells from the population of cells sought to be transfected or infected through viral vectors. In other aspects, the selectable marker may be carried on a separate piece of DNA and used in a co-transfection procedure. Both selectable markers and reporter genes may be flanked with appropriate regulatory sequences to enable expression in the host cells. Non-limiting examples of selectable markers include, antibiotic-resistance genes. Examples of reporter genes may include, but not limited to genes encoding luciferase, beta-galactosidase, chloramphenicol acetyl transferase, secreted alkaline phosphatase, or the green fluorescent protein gene. [00209] Methods of introducing and expressing genes into a cell are known in the art. In the context of an expression vector, the vector can be readily introduced into a host cell, e.g., mammalian, bacterial, yeast, or insect cell by any method in the art. For example, the expression vector can be transferred into a host cell by physical, chemical, or biological means. [00210] Physical methods for introducing a polynucleotide into a host cell include calcium phosphate precipitation, lipofection, particle bombardment, microinjection, electroporation, and the like. Methods for producing cells comprising vectors and/or exogenous nucleic acids are well-known in the art. [00211] Biological methods for introducing a polynucleotide of interest into a host cell include the use of DNA and RNA vectors. Viral vectors, and especially retroviral vectors, have become the most widely used method for inserting genes into mammalian, e.g., human cells. [00212] Chemical means for introducing a polynucleotide into a host cell include colloidal dispersion systems, such as macromolecule complexes, nanocapsules, microspheres, beads, and lipid-based systems including oil-in-water emulsions, micelles, mixed micelles, and liposomes. An exemplary colloidal system for use as a delivery vehicle in vitro and in vivo is a liposome (e.g., an artificial membrane vesicle). [00213] In some aspects, a non-viral delivery system is utilized, wherein the delivery vehicle is a liposome. In another aspect, the nucleic acid may be associated with a lipid. The nucleic acid associated with a lipid may be encapsulated in the aqueous interior of a liposome, interspersed within the lipid bilayer of a liposome, attached to a liposome via a linking molecule that is associated with both the liposome and the oligonucleotide, entrapped in a liposome, complexed with a liposome, dispersed in a solution containing a lipid, mixed with a lipid, combined with a lipid, contained as a suspension in a lipid, contained or complexed with a micelle, or otherwise associated with a lipid. Lipid, lipid/DNA or lipid/expression vector associated compositions are not limited to any particular structure in solution. For example, they may be present in a bilayer structure, as micelles, or with a “collapsed” structure. They may also simply be interspersed in a solution, possibly forming aggregates that are not uniform in size or shape. Lipids are fatty substances which may be naturally occurring or synthetic lipids. For example, lipids include the fatty droplets that naturally occur in the cytoplasm as well as the class of compounds which contain long-chain aliphatic hydrocarbons and their derivatives, such as fatty acids, alcohols, amines, amino alcohols, and aldehydes. Lipids suitable for use can be obtained from commercial sources. For example, dimyristyl phosphatidylcholine (“DMPC”) can be obtained from Sigma, dicetyl phosphate (“DCP”) can be obtained from K & K Laboratories; cholesterol (“Choi”) can be obtained from Calbiochem-Behring; dimyristyl phosphatidylglycerol (“DMPG”) and other lipids may be obtained from Avanti Polar Lipids, Inc. [00214] In some aspects, the chimeric antigen receptor of the disclosure comprises anti-FCRL5 antigen recognition domain comprising an scFv, which comprise a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, or 80, and/or a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, or 81. [00215] In some aspects, the chimeric antigen receptor of the disclosure comprises anti-FCRL5 antigen recognition domain comprising at least two scFv, wherein each scFV comprises a distinct anti-FCRL5 antigen recognition domain. In such aspects, scFV comprises one or more VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, or 80, and/or one or more VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, or 81. [00216] In some aspects, the chimeric antigen receptor of the disclosure is a bispecific chimeric antigen receptor. In such aspects, the chimeric antigen receptor comprises a first antigen recognition domain comprising an anti-FCRL5 antigen recognition domain disclosed herein and a second antigen recognition domain comprising antibodies or antigen-binding antibody fragments that bind to an antigen expressed by B cell and/or plasma cell tumor cells. In such aspects, the second antigen recognition domain comprises antibody or antigen-binding antibody fragment that binds to one or more of BCMA, CS1, ROR1, BAFF, CD19, CD38, ICAM-1 (CD54), CD40, CD45, CD20, syndecan 1, transferrin receptor protein 1 (TfR1), or DKK1. [00217] In some aspects, the bispecific chimeric antigen receptor of the disclosure comprises a first antigen recognition domain comprising an anti-FCRL5 antigen recognition domain comprising one or more VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, or 80, and/or one or more VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, or 81. III. Antibodies [00218] In some aspects, further provided herein is an anti-FCRL5 antibody. In some aspects, anti-FCRL5 antibody comprises a VH and/or VL described herein. [00219] In some aspects, disclosed anti-FCRL5 antibody comprises a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [00220] In some aspects, disclosed anti-FCRL5 antibody comprises a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00221] In some aspects, disclosed anti-FCRL5 antibody comprises a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, and a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00222] In some aspects, disclosed anti-FCRL5 antibody comprises a VH with amino acid sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [00223] In some aspects, disclosed anti-FCRL5 antibody comprises a VL with amino acid sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00224] In some aspects, disclosed anti-FCRL5 antibody comprises a VH with amino acid sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, and a VL with amino acid sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00225] In some aspects, the present disclosure further encompasses a bispecific antibody, a multi-specific antibody, or a hybrid antibody having at least two distinct binding domains with different specificities, with at least one domain comprising a FCRL5 VH and/or FCRL5 VL disclosed herein. In some aspects, a bispecific antibody, a multi-specific antibody, or a hybrid antibody comprises a FCRL5 VH and/or FCRL5 VL disclosed herein, and at least one of an immune cell engager (e.g., a T cell engager, an NK cell engager, an iNKT cell engager, a B cell engager, a dendritic cell engager, or a macrophage cell engager). Such antibody constructs are recombinant protein constructs made from two flexibly linked antibody derived binding domains, with one binding domain specific for a selected tumor antigen on target tumor cells and the second binding domain that binds to and/or activates T cells, NK cells, iNKT cells, B cells, dendritic cells, or macrophage cells. In some aspects, the disclosed antibodies can transiently direct immune cells to the target tumor cells and/or activate the inherent cytolytic potential of immune cells against target tumor cells. In some aspects, a bispecific antibody, a multi-specific antibody, or a hybrid antibody comprises with at least one domain comprising a FCRL5 VH and/or FCRL5 VL disclosed herein, and a second domain comprising a binding domain specific for an antigen expressed by B cell and/or plasma cell tumor cells. A bispecific antibody, a multi-specific antibody, or a hybrid antibody construct can be produced by a variety of methods, including fusion of hybridomas, linking of Fab' fragments, or any other known method in the art. [00226] In some aspects, the bispecific antibody, the multi-specific antibody, or the hybrid antibody comprises a T-cell engager (e.g., bispecific T cell engager (BiTE)) comprising first antigen recognition domain comprising FCRL5 VH and/or FCRL5 VL disclosed herein, and a second antigen recognition domain comprising an antibody or antigen-binding antibody fragment that bind to or activate T cells. In such aspects, a second antigen recognition domain comprising antibody or antigen-binding antibody fragment binds to one or more of CD2, CD3, CD4, CD5, CD6, CD8, CD25, CD27, CD28, CD30, CD40, CD40L, CD44, CD45, CD69, CD90, CRa, TCRp, TCRy, TCRC, ICOS, HVEM, LIGHT, 4-lBB, OX40, DR3, GITR, TIMl, SLAM, or CD226 [00227] In some aspects, the bispecific antibody, the multi-specific antibody, or the hybrid antibody has a binding domain that engages NK cells. In such aspects, the bispecific antibody comprises a first antigen recognition domain comprising FCRL5 VH and FCRL5 VL disclosed herein, and a second antigen recognition domain comprising an antibody or antigen-binding antibody fragments that bind to or activate NK cells. In such aspects, a second antigen recognition domain comprising an antibody or antigen-binding antibody fragment binds to one or more of CD16 (e.g., CD16a, CD16b, or both), NKp30, NKp40, NKp44, NKp46, NKG2D, DNAMl, DAP10, CRTAM, CD27, PSGL1, CD96, CD100 (SEMA4D), NKp80, CD244 (also known as SLAMF4 or 2B4), SLAMF6, SLAMF7, KIR2DS2, KIR2DS4, KIR3DS 1, KIR2DS3, KIR2DS5, KIR2DS 1, CD94, NKG2C, NKG2E, or CD160. [00228] In some aspects, the bispecific antibody, the multi-specific antibody, or the hybrid antibody has a binding domain that engages iNKT cells. In such aspects, the bispecific antibody comprises a first antigen recognition domain comprising FCRL5 VH and FCRL5 VL disclosed herein, and a second antigen recognition domain comprising an antibody or antigen-binding antibody fragments that bind to or activate iNKT cells. In such aspects, a second antigen recognition domain comprising an antibody or antigen-binding antibody fragment binds to CD3. [00229] In some aspects, the bispecific antibody, the multi-specific antibody, or the hybrid antibody has a binding domain that engages B cells. In such aspects, the bispecific antibody comprises a first antigen recognition domain comprising FCRL5 VH and FCRL5 VL disclosed herein, and a second antigen recognition domain comprising an antibody or antigen-binding antibody fragments that bind to or activate B cells. In such aspects, a second antigen recognition domain comprising an antibody or antigen-binding antibody fragment binds to one or more of OX40, CD40 or CD70. [00230] In some aspects, the bispecific antibody, the multi-specific antibody, or the hybrid antibody has a binding domain that engages dendritic cells. In such aspects, the bispecific antibody comprises a first antigen recognition domain comprising FCRL5 VH and FCRL5 VL disclosed herein, and a second antigen recognition domain comprising an antibody or antigen-binding antibody fragments that bind to or activate dendritic cells. In such aspects, a second antigen recognition domain comprising an antibody or antigen-binding antibody fragment binds to one or more of CD2, OX40, 4-IBB, TLR4, CD47, or STING. [00231] In some aspects, the bispecific antibody, the multi-specific antibody, or the hybrid antibody has a binding domain that engages macrophage cell. In such aspects, the bispecific antibody comprises a first antigen recognition domain comprising FCRL5 VH and FCRL5 VL disclosed herein, and a second antigen recognition domain comprising an antibody or antigen-binding antibody fragments that bind to or activate macrophage cells. In such aspects, a second antigen recognition domain comprising an antibody or antigen-binding antibody fragment binds to one or more of OX40, CD40, CD70, TLR4, TLR9, CD47 or STING agonist. [00232] In some aspects, a bispecific antibody, a multi-specific antibody, or a hybrid antibody comprises a first antigen recognition domain comprising FCRL5 VH and FCRL5 VL disclosed herein, and a second antigen recognition domain comprising an antibody or antigen-binding antibody fragments that bind to an antigen expressed by B cell and/or plasma cell tumor cells. In such aspects, a second antigen recognition domain comprising an antibody or antigen-binding antibody fragment binds to one or more of BCMA, CS1, ROR1, BAFF, CD19, CD38, ICAM-1 (CD54), CD40, CD45, CD20, syndecan 1, transferrin receptor protein 1 (TfR1), or DKK1. [00233] In some aspects, the disclosed bispecific antibody, a multi-specific antibody, or a hybrid antibody comprises an anti-FCRL5 antigen recognition domain comprising a VH and/or a VL, comprising one or more amino acid sequences of SEQ ID NO: 2-81, wherein the said amino acid sequence comprises at least 60% sequence identity or similarity with one or more of amino acid sequence SEQ ID NOs: 2-81. In some aspect, the identity or similarity is of at least 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100%. [00234] In some aspects, the disclosed bispecific antibody, a multi-specific antibody, or a hybrid antibody comprises an anti-FCRL5 antigen recognition domain comprising a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, or 80, and a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, or 81. [00235] In some aspects, the disclosed bispecific antibody, a multi-specific antibody, or a hybrid antibody comprises an anti-FCRL5 antigen recognition domain comprising a VH with 100% identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, or 80, and a VL with 100% identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, or 81. IV. Methods Of Using CAR-expressing Cells and Antibodies [00236] The current disclosure further encompasses treatment of cancer. In some aspects, the present disclosure provides a method of killing a malignant cell, the method comprising contacting the malignant cell with an effective amount of an immune effector cell comprising a chimeric antigen receptor (CAR-immune effector cell), wherein the CAR-immune effector cell is deficient in an antigen to which the chimeric antigen receptor specifically binds, and wherein the chimeric antigen receptor specifically binds an antigen expressed on a malignant cell. In various aspects, the malignant cell is a Burkitt lymphoma, chronic lymphocytic leukemia/small lymphocytic lymphoma (CLL/SLL), diffuse large B-cell lymphoma, follicular lymphoma, or mantle cell lymphoma, Monoclonal gammopathy of undetermined significance, Lymphoplasmacytic lymphoma, Plasmacytoma, or myeloma. In further aspects, the antigen is FCRL5. Suitable CAR-immune effector cells are described in detail in Section II. [00237] Contacting a malignant cell with an effective amount of a CAR- immune effector cell generally involves admixing the CAR-immune effector cell and the malignant cell for a period of time sufficient to allow the chimeric antigen receptor of the CAR-immune effector cell to bind its cognate antigen on the surface of the malignant cell. This may occur in vitro or ex vivo. The term "effective amount", as used herein, means an amount that leads to measurable effect, e.g., antigen-dependent cell proliferation, cytokine secretion, cytotoxic killing, etc. The effective amount may be determined by using the methods known in the art and/or described in further detail in the examples. [00238] In another aspect, the present disclosure provides a method for treating a subject having a B cell malignancy. In some aspects, the B cell malignancy is a Burkitt lymphoma, chronic lymphocytic leukemia/small lymphocytic lymphoma (CLL/SLL), diffuse large B-cell lymphoma, follicular lymphoma, or mantle cell lymphoma. The method comprises administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, optionally wherein the CAR- immune effector cells are deficient in an antigen specifically recognized by the chimeric antigen receptor, and wherein the chimeric antigen receptor specifically binds an antigen expressed on a malignant B cell. In some aspects, the antigen expressed on the malignant B cell is FCRL5. In some aspects, the method for treating a subject having a B cell malignancy comprises administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor specifically binds to FCRL5. In some aspects, the method for treating a subject having a B cell malignancy, comprises administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor comprises an anti-FCRL5 antigen recognition domain disclosed herein. [00239] In some aspects, the present disclosure provides a method for treating a subject having a plasma cell malignancy. In some aspects, the plasma cell malignancy is Monoclonal gammopathy of undetermined significance (MGUS), Lymphoplasmacytic lymphoma, Plasmacytoma, or multiple myeloma. The method comprises administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, optionally wherein the CAR-immune effector cells are deficient in an antigen specifically recognized by the chimeric antigen receptor, and wherein the chimeric antigen receptor specifically binds an antigen expressed on a malignant plasma cell. In some aspects, the antigen expressed on the malignant plasma cell is FCRL5. In some aspects, the method for treating a subject having a plasma cell malignancy comprises administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor specifically binds to FCRL5. In some aspects, the method for treating a subject having a plasma cell malignancy comprises, administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR- immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor comprises an anti-FCRL5 antigen recognition domain disclosed herein. [00240] In certain aspects, the present disclosure provides a method for treating a subject having multiple myeloma. The method comprises administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, optionally wherein the CAR-immune effector cells are deficient in an antigen specifically recognized by the chimeric antigen receptor, and wherein the chimeric antigen receptor specifically binds an antigen expressed on multiple myeloma cells. In some aspects, the antigen expressed on the multiple myeloma cell is FCRL5. In some aspects, the method of treating a subject having multiple myeloma comprises administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR- immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor specifically binds to FCRL5. In some aspects, the method of treating a subject having multiple myeloma comprises, administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR- immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor comprises an anti-FCRL5 antigen recognition domain disclosed herein. [00241] In some aspects, the present disclosure provides a method for treating a subject having a malignant cell that express FCRL5. The method comprises administering to the subject a therapeutically effective amount of plurality of CAR- immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, optionally wherein the CAR-immune effector cells are deficient in an antigen specifically recognized by the chimeric antigen receptor, and wherein the chimeric antigen receptor specifically binds FCRL5. In some aspects, the method of treating a subject having a malignant cell that express FCRL5 comprises administering to the subject a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor comprises an anti-FCRL5 antigen recognition domain disclosed herein. [00242] Further provided in the disclosure is a method for treating a subject having a malignancy, wherein the malignancy comprises a malignant cell that express FCRL5 at low levels. Such cells express FCRL5 at similar or lower levels than normal cells (e.g., control plasma cells or control B cells) or similar or lower than malignant cells, when compared to malignant cells across patient samples. In some aspects, the malignant cells express FCRL5 at levels at least 10% lower, for e.g., 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, or more, lower than normal cells (e.g., control plasma cells or control B cells) or lower than malignant cells, when compared to malignant cells across patient samples. In such aspects, the method comprises administering to the subject having a malignant cell that express FCRL5 at low levels, a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor comprises an anti-FCRL5 antigen recognition domain disclosed herein. [00243] In some aspects, the disclosure further provides a method for treating a subject having a malignancy, wherein the malignancy comprises a malignant cell that express FCRL5 at high levels. Such malignant cells express FCRL5 at high higher levels than normal cells (e.g., control plasma cells or control B cells) or malignant cells, when compared to malignant cells across patient samples. Such cells express FCRL5 at levels higher than average levels expressed by a population of malignant cells (e.g., average levels of FCRL5 expression in myeloma cells). In some aspects, the malignant cells express FCRL5 at levels at least 10% higher, for e.g., 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, or more, higher than normal cells (e.g., control plasma cells or control B cells) or higher than malignant cells, when compared to malignant cells across patient samples. In such aspects, the method comprises administering to the subject having a malignant cell that express FCRL5 at high levels, a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor comprises an anti-FCRL5 antigen recognition domain disclosed herein. [00244] The disclosure further encompasses, a method for treating a subject having multiple myeloma, wherein the myeloma cells express FCRL5 at low levels. Myeloma cells which express FCRL5 at low levels comprise cells which express FCRL5 at levels lower than average levels expressed by a population of myeloma cells or similar or lower levels than FCRL5 in normal plasma cells. In some aspects, the myeloma cells express FCRL5 at levels at least 10% lower, for e.g., 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, or more, lower than the average level of FCRL5 expression in a population of myeloma cells. In such aspects, the method comprises administering to the subject having a myeloma cell that express FCRL5 at low levels, a therapeutically effective amount of plurality of CAR-immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor comprises an anti-FCRL5 antigen recognition domain disclosed herein. [00245] In further aspects, the disclosure encompasses, a method for treating a subject having multiple myeloma, wherein the myeloma cells express FCRL5 at high levels. Myeloma cells which express FCRL5 at high levels comprise cells which express FCRL5 at levels higher than average levels expressed by a population of myeloma cells and/or at higher levels than FCRL5 in normal plasma cells. In some aspects, the myeloma cells express FCRL5 at levels at least 10% higher, for e.g., 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, or more, higher than the average level of FCRL5 expression in a population of myeloma cells. In such aspects, the method comprises administering to the subject having a myeloma cell that express FCRL5 at high levels, a therapeutically effective amount of plurality of CAR- immune effector cells, each CAR-immune effector cell comprising the same chimeric antigen receptor, and wherein the chimeric antigen receptor comprises an anti-FCRL5 antigen recognition domain disclosed herein [00246] The CAR-immune effector cells may be administered in effective doses. The effective dose may be either one or multiple doses, and are sufficient to produce the desired therapeutic effect. In some aspects, the dosage of CAR-immune effector cells may range from about 1x10⁴ to 5x10⁹ cells/Kg body weight of subject receiving therapy. In some aspects, a pharmaceutical composition comprising the immune effector cells described herein may be administered at a dosage of 1x10⁴ to 2x10⁹ cells/kg body weight, such as 1x10⁵ to 2x10⁶ cells/kg body weight. Immune effector cells compositions may also be administered multiple times at these dosages. The immune effector cells can be administered by using infusion techniques that are commonly known in immunotherapy. The optimal dosage and treatment regime for a particular subject can readily be determined by one skilled in the art of medicine by monitoring the subject for signs of disease and adjusting the treatment accordingly. Further, the effective dose may be calculated based on the stage of the malignancy, the health of the subject, and the type of malignancy. In the situation where multiple doses are administered, that dose and the interval between the doses may be determined based on the subject’s response to therapy. [00247] In some aspects, treatment with disclosed CAR-immune effector cells reduces tumor burden in a subject. In some aspects, reduction in tumor burden in a subject, comprises reduction in number of malignant cells, reduction in tumor size, and/or reduction in the tumor growth. Tumor burden in a subject can be assessed using any conventional methods known in the art, non-limiting examples of which include, diagnostic techniques such as X ray, CT scan, bone marrow biopsy, serum protein electrophoresis (SPEP), or MRI. In some aspects, administration of disclosed CAR- immune effector cells reduces number of malignant cells, tumor size, and/or tumor growth in the subject, by at least 10%, e.g., 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or above, as compared to number of malignant cells, tumor size, and/or tumor growth before administration of the inhibitor (baseline) or a control subject not receiving the treatment. [00248] In some aspects, treatment with disclosed CAR-immune effector cells enhances survival and prolongs life of a subject. Survival of the subject can be determined using known methods in the art, non-limiting examples of which include Kaplan Meier analysis, Gleason score, Log-rank (Mantel-Cox) test, and Cox hazard analysis. In some aspects, administration of disclosed CAR-immune effector cells in the subject enhances survival, by at least 10%, e.g., 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or above, as compared to survival of a control subject not receiving the treatment, or expected survival of the subject before the treatment. [00249] In some aspects, treatment disclosed CAR-immune effector cells enhances the death of a malignant cell. Tumor cell death may be determined using any known methods in the art for measuring cell apoptosis or cell viability, including bioluminescent imaging or flow cytometry. In some aspects, administration of disclosed CAR-immune effector cells enhances death of malignant cells in the subject, by at least 10%, e.g., 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or above, as compared to malignant cells, before administration of the inhibitor (baseline) or a control subject not receiving the treatment. [00250] The administration of the disclosed immune effector cells, or compositions thereof, may be carried out in any convenient manner, including by injection, transfusion, or implantation. The compositions described herein may be administered to a patient subcutaneously, intradermally, intratumorally, intranodally, intramedullary, intramuscularly, by intravenous (i.v.) injection, or intraperitoneally. In some aspects, the disclosed immune effector cells, or compositions thereof, are administered to a patient by intradermal or subcutaneous injection. In some aspects, the disclosed compositions are administered by i.v. injection. The immune effector cells, or compositions thereof, may also be injected directly into a tumor, lymph node, or site of infection. In some aspects of the method, compositions disclosed herein are formulated for intravenous administration. [00251] The methods described herein, encompasses allogenic CAR- immune effector cell therapy or autologous CAR- immune effector cell therapy. In some aspects, the method comprise adoptive transfer of disclosed CAR-immune effector cells. Immune effector cells procured from the subject in need of the treatment, are genetically modified to express the CARs comprising disclosed anti-FCRL5 antigen recognition domain, and are administered back into the subject. In some aspects, allogenic immune effector cells are used in the methods described herein. Allogenic sources can comprise of immune effector cell lines or donor effector cells. Once procured, allogenic immune effector cells are genetically modified to express the CARs comprising disclosed anti-FCRL5 antigen recognition domain, and are administered into a subject in need thereof. [00252] Further provided herein, is a method of treating a B cell malignancy, or a plasma cell malignancy, in a subject in need thereof, using one or more of the disclosed anti-FCRL5. In some aspects, the B cell malignancy is a Burkitt lymphoma, chronic lymphocytic leukemia/small lymphocytic lymphoma (CLL/SLL), diffuse large B-cell lymphoma, follicular lymphoma, or mantle cell lymphoma and the method comprises administering to the subject a therapeutically effective amount of one or more of the disclosed anti-FCRL5 antibodies. In some aspects, the plasma cell malignancy is Monoclonal gammopathy of undetermined significance (MGUS), Lymphoplasmacytic lymphoma, Plasmacytoma, or multiple myeloma and the method comprises administering to the subject a therapeutically effective amount of one or more of the disclosed anti-FCRL5 antibodies. In some aspects, the malignancy is multiple myeloma and the method comprises administering to the subject a therapeutically effective amount of one or more of the disclosed anti-FCRL5 antibodies. [00253] In some aspects, the therapeutically effective amount between about 5 mg to about 1000 mg per day with unit doses ranging from about 1 mg to about 250 mg. In some aspects, the effective amount is about 0.001-10 mg/kg, such as about 0.001-5 mg/kg, for example about 0.001-2 mg/kg, such as about 0.001-1 mg/kg, for instance about 0.001, about 0.01, about 0.1, about 1 or about 10 mg/kg. In general, the physician may determine the appropriate dosage depending on the age, weight and any other factors specific to the subject to be treated. [00254] The disclosed compositions comprising anti-FCRL5 antibodies described herein, can be formulated for administration as various formulations including oral, parenteral (e.g. intravenous, intramuscular, intraperinoneal, subcutaneous), intravenously as a bolus or by continuous infusion over a period of time, injected by intramuscular, subcutaneous, intra-articular, intrasynovial, intratumoral, peritumoral, intralesional, or perilesional routes, to exert local as well as systemic therapeutic effects. [00255] In some aspects, administration of therapeutically effective amount of anti-FCRL5 antibodies described herein, can reduces tumor burden in a subject. In some aspects, reduction in tumor burden in a subject, comprises reduction in number of malignant cells, reduction in tumor size, and/or reduction in the tumor growth. Tumor burden in a subject can be assessed using any conventional methods known in the art, non-limiting examples of which include, diagnostic techniques such as X ray, CT scan, bone marrow biopsy, serum protein electrophoresis (SPEP), or MRI. In some aspects, administration of disclosed anti-FCRL5 antibodies reduces number of malignant cells, tumor size, and/or tumor growth in the subject, by at least 10%, e.g., 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or above, as compared to number of malignant cells, tumor size, and/or tumor growth before administration of the inhibitor (baseline) or a control subject not receiving the treatment. [00256] In some aspects, treatment with disclosed anti-FCRL5 antibodies enhances survival and prolongs life of a subject. Survival of the subject can be determined using known methods in the art, non-limiting examples of which include Kaplan Meier analysis, Gleason score, Log-rank (Mantel-Cox) test, and Cox hazard analysis. In some aspects, administration of disclosed anti-FCRL5 antibodies in the subject enhances survival, by at least 10%, e.g., 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or above, as compared to survival of a control subject not receiving the treatment, or expected survival of the subject before the treatment. [00257] In some aspects, treatment disclosed anti-FCRL5 antibodies enhances the death of a malignant cell. Tumor cell death may be determined using any known methods in the art for measuring cell apoptosis or cell viability, including bioluminescent imaging or flow cytometry. In some aspects, administration of disclosed anti-FCRL5 antibodies enhances death of malignant cells in the subject, by at least 10%, e.g., 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or above, as compared to malignant cells, before administration of the inhibitor (baseline) or a control subject not receiving the treatment. [00258] In some aspects, the CAR-immune effector cell therapy may be accompanied by other therapies, including but not limited to immunotherapy, chemotherapy or radiation therapy. Such therapies can be administered before, simultaneously, or following the administration of CAR-immune effector cells. In some aspects, the disclosed CAR- immune effector cells and/or anti-FCRL5 antibodies are administered to a subject in conjunction with any relevant treatments, including but not limited to thalidomide, dexamethasone, bortezomib, and lenalidomide. In further aspects, the CAR- immune effector cells may be used in combination with immunosuppressive agents, such as cyclosporin, azathioprine, methotrexate, mycophenolate, and FK506, antibodies, or other immunoablative agents such as CAM PATH, anti-CD3 antibodies or other antibody therapies, cytoxin, fludaribine, cyclosporin, FK506, rapamycin, mycophenolic acid, steroids, FR901228, cytokines, and irradiation. In some aspects, the CAR-immune effector cells are administered to a subject in conjunction with bone marrow transplantation, T cell ablative therapy using either chemotherapy agents such as, fludarabine, external-beam radiation therapy (XRT), cyclophosphamide, or antibodies such as OKT3 or CAMPATH. In another aspects, the CAR-immune effector cells of the current disclosure are administered following B-cell ablative therapy such as agents that react with CD20, e.g., Rituxan. In some aspects, subjects may undergo standard treatment with high dose chemotherapy followed by peripheral blood stem cell transplantation. In certain aspects, following the transplant, subjects receive an infusion of the disclosed CAR-immune effector cells. In another aspect, CAR-immune effector cells are administered to the subject before or following surgery. [00259] Any mammal can be treated by the CAR-immune effector cells and/or anti-FCRL5 antibodies described herein. Non-limiting examples of mammals include humans, non-human primates (e.g., apes, gibbons, chimpanzees, orangutans, monkeys, macaques, and the like), domestic animals (e.g., dogs and cats), farm animals (e.g., horses, cows, goats, sheep, pigs) and experimental animals (e.g., mouse, rat, rabbit, guinea pig). In certain aspects, a mammal is a human. In certain aspects a mammal is a non-rodent mammal (e.g., human, pig, goat, sheep, horse, dog, or the like). In certain aspects, a non-rodent mammal is a human. A mammal can be any age or at any stage of development (e.g., an adult, teen, child, infant, or a mammal in utero). A mammal can be male or female. In certain aspects a mammal can be an animal disease model. V. Compositions [00260] In some aspects, the disclosure provides compositions comprising disclosed CAR-immune effector cells. In some aspects, the composition can be formulated as a pharmaceutical composition. In some aspects the pharmaceutical composition comprises a vector, a cell, or a population of cells all as defined earlier herein, preferably for use as a medicament. In some aspects, pharmaceutical compositions comprise CAR-immune effector cells disclosed herein, in combination with one or more pharmaceutically or physiologically acceptable carriers, diluents or excipients. Such compositions may comprise buffers such as neutral buffered saline, phosphate buffered saline 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 (e.g., aluminum hydroxide); and preservatives. In certain aspects, compositions of CAR-immune effector cells can further comprise other components such as IL-2, IL-15, IL-7, other cytokines or cell populations, or components that sustain the viability and/or activity of administered CAR-immune effector cells may be included in the composition. The CAR-immune effector cells may be formulated as a single dosage unit or as multiple dosage units. [00261] The compositions comprising CAR-immune effector cells disclosed herein, may be formulated for administration, in any convenient manner, including by compositions for injection, transfusion, or implantation. The compositions described herein may be formulated for subcutaneous, intradermal, intratumoral, intranodal, intramedullar, intramuscular, intravenous (i.v.), or intraperitoneal, injection or adminstration. In some aspects, the disclosed compositions are formulated to be administered by intradermal or subcutaneous injection. In some aspects, the disclosed compositions are formulated to be administered by i.v. injection. The compositions may also be formulated, to be injected directly into a tumor, lymph node, or site of infection. In some aspects, the compositions disclosed herein are formulated for intravenous administration. [00262] In some aspects, the composition can comprise from about 1 x 10⁴ to 5 x 10⁹ disclosed CAR-immune effector cells. In some aspects, the composition comprises 1 x 10⁴, 1 x 10⁵, 1 x 10⁶, 1 x 10⁷, 1 x 10⁸, 1 x 10⁹, 2 x 10⁴, 2 x 10⁵, 2 x 10⁶, 2 x 10⁷, 2 x 10⁸, 2 x 10⁹, 3 x 10⁴, 3 x 10⁵, 3 x 10⁶, 3 x 10⁷, 3 x 10⁸, 3 x 10⁹, 4 x 10⁴, 4 x 10⁵, 4 x 10⁶, 4 x 10⁷, 4 x 10⁸, 4 x 10⁹, 5 x 10⁴, 5 x 10⁵, 5 x 10⁶, 5 x 10⁷, 5 x 10⁸, or 5 x 10⁹ of the disclosed CAR-immune effector cells. [00263] In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [00264] In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00265] In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, and a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00266] In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [00267] In some aspects, disclosed composition comprises a CAR-immune effector cell comprising an anti-FCRL5 antigen recognition domain, comprising a VL with amino acid sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00268] In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, and a VL with amino acid sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00269] In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 2 and/or a VL with amino acid sequence of SEQ ID NO: 3. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 4 and/or a VL with amino acid sequence of SEQ ID NO: 5. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 6 and/or a VL with amino acid sequence of SEQ ID NO: 7. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 8 and/or a VL with amino acid sequence of SEQ ID NO: 9. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 10 and/or a VL with amino acid sequence of SEQ ID NO: 11. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 12 and/or a VL with amino acid sequence of SEQ ID NO: 13. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 14 and/or a VL with amino acid sequence of SEQ ID NO: 15. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 16 and/or a VL with amino acid sequence of SEQ ID NO: 17. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 18 and/or a VL with amino acid sequence of SEQ ID NO: 19. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 20 and/or a VL with amino acid sequence of SEQ ID NO: 21. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 22 and/or a VL with amino acid sequence of SEQ ID NO: 23. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 24 and/or a VL with amino acid sequence of SEQ ID NO: 25. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 26 and/or a VL with amino acid sequence of SEQ ID NO: 27. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 28 and/or a VL with amino acid sequence of SEQ ID NO: 29. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 30 and/or a VL with amino acid sequence of SEQ ID NO: 31. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 32 and/or a VL with amino acid sequence of SEQ ID NO: 33. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 34 and/or a VL with amino acid sequence of SEQ ID NO: 35. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 36 and/or a VL with amino acid sequence of SEQ ID NO: 37. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 38 and/or a VL with amino acid sequence of SEQ ID NO: 39. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 40 and/or a VL with amino acid sequence of SEQ ID NO: 41. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 42 and/or a VL with amino acid sequence of SEQ ID NO: 43. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 44 and/or a VL with amino acid sequence of SEQ ID NO: 45. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 46 and/or a VL with amino acid sequence of SEQ ID NO: 47. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 48 and/or a VL with amino acid sequence of SEQ ID NO: 49. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 50 and/or a VL with amino acid sequence of SEQ ID NO: 51. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 52 and/or a VL with amino acid sequence of SEQ ID NO: 53. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 54 and/or a VL with amino acid sequence of SEQ ID NO: 55. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 56 and/or a VL with amino acid sequence of SEQ ID NO: 57. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 58 and/or a VL with amino acid sequence of SEQ ID NO: 59. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 60 and/or a VL with amino acid sequence of SEQ ID NO: 61. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 62 and/or a VL with amino acid sequence of SEQ ID NO: 63. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 64 and/or a VL with amino acid sequence of SEQ ID NO: 65. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 66 and/or a VL with amino acid sequence of SEQ ID NO: 67. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 68 and/or a VL with amino acid sequence of SEQ ID NO: 69. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 70 and/or a VL with amino acid sequence of SEQ ID NO: 71. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 72 and/or a VL with amino acid sequence of SEQ ID NO: 73. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 74 and/or a VL with amino acid sequence of SEQ ID NO: 75. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 76 and/or a VL with amino acid sequence of SEQ ID NO: 77. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 78 and/or a VL with amino acid sequence of SEQ ID NO: 79. In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises an anti-FCRL5 antigen recognition domain, comprising a VH with amino acid sequence of SEQ ID NO: 80 and/or a VL with amino acid sequence of SEQ ID NO: 81. [00270] In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises anti-FCRL5 antigen recognition domain comprising an scFv, which comprise a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, or 80, and/or a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, or 81. [00271] In some aspects, disclosed composition comprises a CAR-immune effector cell, wherein the CAR comprises anti-FCRL5 antigen recognition domain comprising at least two scFv, wherein each scFV comprises a distinct anti-FCRL5 antigen recognition domain. In such aspects of the composition, scFV comprises one or more VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, or 80, and/or one or more VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, or 81. [00272] In some aspects, further provided is a composition comprising a bispecific chimeric antigen receptor, described herein. In such aspects of the composition, the chimeric antigen receptor comprises a first antigen recognition domain comprising an anti-FCRL5 antigen recognition domain disclosed herein and a second antigen recognition domain comprising antibodies or antigen-binding antibody fragments that bind to an antigen expressed by B cell and/or plasma cell tumor cells. In further aspects, the disclosed second antigen recognition domain comprises an antibody or antigen-binding antibody fragment that binds to one or more of BCMA, CS1, ROR1, BAFF, CD19, CD38, ICAM-1 (CD54), CD40, CD45, CD20, syndecan 1, transferrin receptor protein 1 (TfR1), or DKK1. [00273] In some aspects, the bispecific chimeric antigen receptor of the disclosed compostion comprises a first antigen recognition domain comprising an anti- FCRL5 antigen recognition domain comprising one or more VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, or 80, and/or one or more VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, or 81. [00274] In some aspects, compositions provided herein comprises an anti- FCRL5 antibody comprising a VH and/or VL described herein. [00275] In some aspects, disclosed composition comprises an anti-FCRL5 antibody which comprises a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [00276] In some aspects, disclosed composition comprises an anti-FCRL5 antibody which comprises a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00277] In some aspects, disclosed composition comprises an anti-FCRL5 antibody which comprises a VH with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, and a VL with at least about 80% (e.g., about 85%, about 90%, about 95%, about 98%) identity to the sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00278] In some aspects, disclosed composition comprises an anti-FCRL5 antibody which comprises a VH with amino acid sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. [00279] In some aspects, disclosed composition comprises an anti-FCRL5 antibody which comprises a VL with amino acid sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00280] In some aspects, disclosed composition comprises an anti-FCRL5 antibody which comprises a VH with amino acid sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, and a VL with amino acid sequence of any one of SEQ ID NOs: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. [00281] In further aspects, the disclosed composition comprises a bispecific antibody, a multi-specific antibody, or a hybrid antibody comprising a first antigen recognition domain comprising FCRL5 VH and FCRL5 VL disclosed herein. Pharmaceutically acceptable carriers, excipients and active agents [00282] In some aspects, the compositions, compositions disclosed herein may further compromise one or more pharmaceutically acceptable diluent(s), excipient(s), and/or carrier(s). Pharmaceutically acceptable diluents, carriers, and excipients can include, but are not limited to, physiological saline, Ringer’s solution, phosphate solution or buffer, buffered saline, and other carriers known in the art. Pharmaceutically acceptable carriers include any and all solvents, adjuvants, dispersion media, coatings, surfactants, antioxidants, preservatives (e.g., antibacterial agents, antifungal agents), isotonic agents, absorption delaying agents, salts, drugs, drug stabilizers, gels, binders, excipients, disintegration agents, lubricants, sweetening agents, flavoring agents, dyes, colorants, other medicinal or pharmaceutical agents, wetting agents, emulsifying agents, solution promoters, solubilizers, antifoaming agents, and such like materials and any combinations thereof, as would be known to one of ordinary skill in the art. (See, e.g., Remington’s Pharma. Sci.18th ed.1990). Herein, the term “excipient” refers to an inert substance added to a pharmaceutical composition to further facilitate administration of an active ingredient. Examples, without limitation, of excipients include calcium carbonate, calcium phosphate, various sugars and types of starch, cellulose derivatives, gelatin, vegetable oils and polyethylene glycols. Techniques for formulation and administration of drugs may also be found for example in Remington’s Pharma. Sci.18th ed.1990. Except insofar as any conventional carrier is incompatible with the active ingredient, its use in the therapeutic or pharmaceutical compositions is contemplated. In certain embodiments, a pharmaceutical composition described herein comprising a population of cells described herein, further comprises a suitable amount of an antifungal agent. In some cases, a pharmaceutical composition described herein comprises an antifungal agent in an amount sufficient for the pharmaceutical composition to retain at least 20%, 30%, 40%, 50%, 60%, 70%, 80% or 90% of its desired activity for a period of at least 1 month, 2 months, 3 months, 6 months, 1 year, 1.5 years, 2 years, 2.5 years or 3 years. [00283] In certain aspects, pharmaceutical compositions described herein may be formulated in conventional manner using one or more physiologically acceptable carriers comprising excipients and auxiliaries to facilitate processing of engineered cells or vectors into preparations which can be used pharmaceutically. In some aspects, any of the well-known techniques, carriers, and excipients may be used as suitable and/or as understood in the art. [00284] In certain aspects, pharmaceutical compositions described herein may be an aqueous suspension comprising one or more polymers as suspending agents. In some aspects, polymers that may comprise pharmaceutical compositions described herein include: water-soluble polymers such as cellulosic polymers, e.g., hydroxypropyl methylcellulose; water-insoluble polymers such as cross-linked carboxyl- containing polymers; mucoadhesive polymers, selected from, for example, carboxymethylcellulose, carbomer (acrylic acid polymer), poly(methylmethacrylate), polyacrylamide, polycarbophil, acrylic acid/butyl acrylate copolymer, sodium alginate, and dextran; or a combination thereof. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, or at least 50% total amount of polymers as suspending agent(s) by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of polymers as suspending agent(s) by total weight of the composition. [00285] In certain aspects, pharmaceutical compositions disclosed herein may comprise a viscous formulation. In some aspects, viscosity of composition herein may be increased by the addition of one or more gelling or thickening agents. In some aspects, compositions disclosed herein may comprise one or more gelling or thickening agents in an amount to provide a sufficiently viscous formulation to remain on treated tissue. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, or at least 50% total amount of gelling or thickening agent(s) by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of gelling or thickening agent(s) by total weight of the composition. In some aspects, suitable thickening agents for use herein can be hydroxypropyl methylcellulose, hydroxyethyl cellulose, polyvinylpyrrolidone, carboxymethyl cellulose, polyvinyl alcohol, sodium chondroitin sulfate, sodium hyaluronate. In other aspects, viscosity enhancing agents can be acacia (gum arabic), agar, aluminum magnesium silicate, sodium alginate, sodium stearate, bladderwrack, bentonite, carbomer, carrageenan, Carbopol, xanthan, cellulose, microcrystalline cellulose (MCC), ceratonia, chitin, carboxymethylated chitosan, chondrus, dextrose, furcellaran, gelatin, Ghatti gum, guar gum, hectorite, lactose, sucrose, maltodextrin, mannitol, sorbitol, honey, maize starch, wheat starch, rice starch, potato starch, gelatin, sterculia gum, xanthum gum, gum tragacanth, ethyl cellulose, ethylhydroxyethyl cellulose, ethylmethyl cellulose, methyl cellulose, hydroxyethyl cellulose, hydroxyethylmethyl cellulose, hydroxypropyl cellulose, poly(hydroxyethyl methacrylate), oxypolygelatin, pectin, polygeline, povidone, propylene carbonate, methyl vinyl ether/maleic anhydride copolymer (PVM/MA), poly(methoxyethyl methacrylate), poly(methoxyethoxyethyl methacrylate), hydroxypropyl cellulose, hydroxypropylmethyl- cellulose (HPMC), sodium carboxymethyl-cellulose (CMC), silicon dioxide, polyvinylpyrrolidone (PVP: povidone), Splenda® (dextrose, maltodextrin and sucralose), or any combination thereof. [00286] In certain aspects, pharmaceutical compositions disclosed herein may comprise additional agents or additives selected from a group including surface- active agents, detergents, solvents, acidifying agents, alkalizing agents, buffering agents, tonicity modifying agents, ionic additives effective to increase the ionic strength of the solution, antimicrobial agents, antibiotic agents, antifungal agents, antioxidants, preservatives, electrolytes, antifoaming agents, oils, stabilizers, enhancing agents, and the like. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, or at least 50% total amount of one or more agents by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of one or more agents by total weight of the composition. In some aspects, one or more of these agents may be added to improve the performance, efficacy, safety, shelf-life and/or other property of the muscarinic antagonist composition of the present disclosure. In some aspects, additives may be biocompatible, without being harsh, abrasive, and/or allergenic. [00287] In certain aspects, pharmaceutical compositions disclosed herein may comprise one or more acidifying agents. As used herein, “acidifying agents” refers to compounds used to provide an acidic medium. Such compounds include, by way of example and without limitation, acetic acid, amino acid, citric acid, fumaric acid and other alpha hydroxy acids, such as hydrochloric acid, ascorbic acid, and nitric acid and others known to those of ordinary skill in the art. In some aspects, any pharmaceutically acceptable organic or inorganic acid may be used. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50% total amount of one or more acidifying agents by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of one or more acidifying agents by total weight of the composition. [00288] In certain aspects, pharmaceutical compositions disclosed herein may comprise one or more alkalizing agents. As used herein, “alkalizing agents” are compounds used to provide alkaline medium. Such compounds include, by way of example and without limitation, ammonia solution, ammonium carbonate, diethanolamine, monoethanolamine, potassium hydroxide, sodium borate, sodium carbonate, sodium bicarbonate, sodium hydroxide, triethanolamine, and trolamine and others known to those of ordinary skill in the art. In some aspects, any pharmaceutically acceptable organic or inorganic base can be used. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50% total amount of one or more alkalizing agents by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of one or more alkalizing agents by total weight of the composition. [00289] In certain aspects, pharmaceutical compositions disclosed herein may comprise one or more antioxidants. As used herein, “antioxidants” are agents that inhibit oxidation and thus can be used to prevent the deterioration of preparations by the oxidative process. Such compounds include, by way of example and without limitation, ascorbic acid, ascorbyl palmitate, butylated hydroxyanisole, butylated hydroxytoluene, hypophophorous acid, monothioglycerol, propyl gallate, sodium ascorbate, sodium bisulfite, sodium formaldehyde sulfoxylate, sodium metabisulfite and other materials known to one of ordinary skill in the art. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50% total amount of one or more antioxidants by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of one or more antioxidants by total weight of the composition. [00290] In certain aspects, pharmaceutical compositions disclosed herein may comprise a buffer system. As used herein, a “buffer system” is a composition comprised of one or more buffering agents wherein “buffering agents” are compounds used to resist change in pH upon dilution or addition of acid or alkali. Buffering agents include, by way of example and without limitation, potassium metaphosphate, potassium phosphate, monobasic sodium acetate and sodium citrate anhydrous and dihydrate and other materials known to one of ordinary skill in the art. In some aspects, any pharmaceutically acceptable organic or inorganic buffer can be used. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50% total amount of one or more buffering agents by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of one or more buffering agents by total weight of the composition. [00291] In some aspects, the amount of one or more buffering agents may depend on the desired pH level of a composition. In some aspects, pharmaceutical compositions disclosed herein may have a pH of about 6 to about 9. In some aspects, pharmaceutical compositions disclosed herein may have a pH greater than about 8, greater than about 7.5, greater than about 7, greater than about 6.5, or greater than about 6. [00292] In certain aspects, pharmaceutical compositions disclosed herein may comprise one or more preservatives. As used herein, “preservatives” refers to agents or combination of agents that inhibits, reduces or eliminates bacterial growth in a pharmaceutical dosage form. Non-limiting examples of preservatives include Nipagin, Nipasol, isopropyl alcohol and a combination thereof. In some aspects, any pharmaceutically acceptable preservative can be used. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50% total amount of one or more preservatives by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of one or more preservatives by total weight of the composition. [00293] In certain aspects, pharmaceutical compositions disclosed herein may comprise one or more surface-acting reagents or detergents. In some aspects, surface-acting reagents or detergents may be synthetic, natural, or semi-synthetic. In some aspects, compositions disclosed herein may comprise anionic detergents, cationic detergents, zwitterionic detergents, ampholytic detergents, amphoteric detergents, nonionic detergents having a steroid skeleton, or a combination thereof. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50% total amount of one or more surface-acting reagents or detergents by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of one or more surface-acting reagents or detergents by total weight of the composition. [00294] In certain aspects, pharmaceutical compositions disclosed herein may comprise one or more stabilizers. As used herein, a “stabilizer” refers to a compound used to stabilize an active agent against physical, chemical, or biochemical process that would otherwise reduce the therapeutic activity of the agent. Suitable stabilizers include, by way of example and without limitation, succinic anhydride, albumin, sialic acid, creatinine, glycine and other amino acids, niacinamide, sodium acetyltryptophonate, zinc oxide, sucrose, glucose, lactose, sorbitol, mannitol, glycerol, polyethylene glycols, sodium caprylate and sodium saccharin and others known to those of ordinary skill in the art. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50% total amount of one or more stabilizers by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of one or more stabilizers by total weight of the composition. [00295] In some aspects, pharmaceutical compositions disclosed herein may comprise one or more tonicity agents. As used herein, a “tonicity agents” refers to a compound that can be used to adjust the tonicity of the liquid formulation. Suitable tonicity agents include, but are not limited to, glycerin, lactose, mannitol, dextrose, sodium chloride, sodium sulfate, sorbitol, trehalose and others known to those or ordinary skill in the art. Osmolarity in a composition may be expressed in milliosmoles per liter (mOsm/L). Osmolarity may be measured using methods commonly known in the art. In some aspects, a vapor pressure depression method is used to calculate the osmolarity of the compositions disclosed herein. In some aspects, the amount of one or more tonicity agents comprising a pharmaceutical composition disclosed herein may result in a composition osmolarity of about 150 mOsm/L to about 500 mOsm/L, about 250 mOsm/L to about 500 mOsm/L, about 250 mOsm/L to about 350 mOsm/L, about 280 mOsm/L to about 370 mOsm/L or about 250 mOsm/L to about 320 mOsm/L. In some aspects, a composition herein may have an osmolality ranging from about 100 mOsm/kg to about 1000 mOsm/kg, from about 200 mOsm/kg to about 800 mOsm/kg, from about 250 mOsm/kg to about 500 mOsm/kg, or from about 250 mOsm/kg to about 320 mOsm/kg, or from about 250 mOsm/kg to about 350 mOsm/kg or from about 280 mOsm/kg to about 320 mOsm/kg. In some aspects, a pharmaceutical composition described herein may have an osmolarity of about 100 mOsm/L to about 1000 mOsm/L, about 200 mOsm/L to about 800 mOsm/L, about 250 mOsm/L to about 500 mOsm/L, about 250 mOsm/L to about 350 mOsm/L, about 250 mOsm/L to about 320 mOsm/L, or about 280 mOsm/L to about 320 mOsm/L. In some aspects, pharmaceutical compositions disclosed herein may comprise at least 5%, at least 10%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50% total amount of one or more tonicity modifiers by total weight of the composition. In some aspects, pharmaceutical compositions disclosed herein may comprise about 5% to about 99%, about 10%, about 95%, or about 15% to about 90% total amount of one or more tonicity modifiers by total weight of the composition. [00296] In some aspect, the pharmaceutical composition may comprise one or more active agents in addition to the CAR, vectors, cells and/or populations of cells provided herein. Non limiting examples of additional active agents include but are not restricted to antibiotics, anti-pyrectics, antimicrobials, antifungals, NSAIDs, chemotherapeutic and anticancer agents. [00297] Chemotherapeutic and anticancer agents commonly used to treat ovarian cancer, and which may be used in combination with any of the compositions disclosed herein include but are not limited to platinum compounds (such as cisplatin or carboplatin), and taxane compounds such as paclitaxel (Taxol®) or docetaxel (Taxotere®). Other chemotherapeutic agents used to treat ovarian cancer and which may be used in combination with any of the compositions disclosed herein, include but are not limited to: Albumin bound paclitaxel (nab-paclitaxel, Abraxane®), Pemetrexed (Alimta®), Irinotecan (CPT-11, Camptosar®), Cyclophosphamide (Cytoxan®), Liposomal doxorubicin (Doxil®), Gemcitabine (Gemzar®), Altretamine (Hexalen®), Ifosfamide (Ifex®), Melphalan (Alkeran), Vinorelbine (Navelbine®), Topotecan (Hycamtin), Etoposide (VP-16), and Capecitabine (Xeloda®). [00298] In some aspects, administration of the composition comprising the disclosed CAR-immune effector cells reduces tumor burden in a subject. In some aspects, reduction in tumor burden in a subject, comprises reduction in number of malignant cells, reduction in tumor size, and/or reduction in the tumor growth. Tumor burden in a subject can be assessed using any conventional methods know in the art, non-limiting examples of which include, diagnostic techniques such as X ray, CT scan, or MRI. In some aspects, administration of disclosed compostion reduces number of malignant cells, tumor size, and/or tumor growth in the subject, by at least 10%, e.g., 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or above, as compared to number of malignant cells, tumor size, and/or tumor growth before administration of the inhibitor (baseline) or a control subject not receiving the treatment. [00299] In some aspects, administration of the composition comprising the disclosed CAR-immune effector cells enhances survival and prolongs life of a subject. Survival of the subject can be determined using known methods in the art, non-limiting examples of which include Kaplan Meier analysis, Gleason score, Log-rank (Mantel- Cox) test, and Cox hazard analysis. In some aspects, administration of disclosed composition in the subject enhances survival, by at least 10%, e.g., 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or above, as compared to survival of a control subject not receiving the treatment, or expected survival of the subject before the treatment. [00300] In some aspects, administration of the composition comprising the disclosed CAR-immune effector cells enhances death of a malignant cell. Tumor cell death may be determined using any known methods in the art for measuring cell apoptosis or cell viability, including bioluminescent imaging or flow cytometry. In some aspects, administration of disclosed composition enhances death of malignant cells in the subject, by at least 10%, e.g., 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 95% or above, as compared to malignant cells, before administration of the inhibitor (baseline) or a control subject not receiving the treatment. [00301] The actual dosage amount of a composition according to the present disclosure, and the selection of any combination treatment to be administered to a subject can be determined by physical and physiological factors such as body weight, severity of condition, the type of disease being treated, previous or concurrent therapeutic interventions, idiopathy of the patient and on the route of administration. The practitioner responsible for administration will, in any event, determine the concentration of active ingredient(s) in a composition and appropriate dose(s) for the individual subject. EXAMPLES [00302] The following examples are included to demonstrate various embodiments of the present disclosure. It should be appreciated by those of skill in the art that the techniques disclosed in the examples that follow represent techniques discovered by the inventors to function well in the practice of the invention, and thus can be considered to constitute preferred modes for its practice. However, those of skill in the art should, in light of the present disclosure, appreciate that many changes can be made in the specific embodiments which are disclosed and still obtain a like or similar result without departing from the spirit and scope of the invention. Materials and Methods Generation of novel anti-FCRL5 antibodies [00303] The ATX-GK^TM mouse (Alloy Therapeutics) produces monoclonal human antibodies via expression of fully human kappa and heavy chain antibodies. ATX-GK mice were immunized with full-length human FCRL5 or domain 9 (D9) of FCRL5 (Alloy Therapeutics). Binding to all antibodies to full-length or D9 recombinant was assessed and KD was calculated. The screen identified 23 antibodies that bound to both human FCRL5 D9 monomer and full length FCRL5 monomer and 17 clones that do not bind D9, and instead bind somewhere within domain 1-8 (D1-8). CAR-T design [00304] Luc90 and HuLuc63 scFv (patent US8603477), CD19 scFv (14), CD79B scFv (patent US 8,691,531 B2) and BCMA (clone J22.xi, patent WO 2014/06879 A1) were synthesized (Genescript, Piscataway, NJ) and cloned into pLV (Vector Builder, Chicago, IL) or pELNS (kindly provided by Carl June, U of Penn.). Lentivirus production [00305] Lentivirus was produced using Calcium phosphate (Takara Bio, Mountain View, CA) or Lipofectamine (Invitrogen, Carlsbad, CA), 293T cells and DNA generated by (Genscript). CAR-T Production [00306] T cells were isolated from human PBMC from leftover platelet apheresis products or from purchased leukopacks (Miltenyi Biotech, Auburn, CA) using PAN-T kits and the AutoMACS (Miltenyi). T cells were cultured in TexMACS media (Miltenyi) supplemented with HAB serum (Sigma). Cells were activated with anti- CD3/CD28 dyna beads (Gibco, Waltham, MA) at a 3:1 bead:cell ratio for 4-6 days) and transduced with lentivirus on day +2 in the presence of 6 µg/ml polybrene (Sigma). In some experiments, CAR+T cells were purified by staining with anti-CD34 (CD34 Pool PE, Beckman Coulter) followed by anti-PE beads (Miltenyi) and sorted on an AutoMACS (Miltenyi). Cell lines [00307] MM.1S cells, kindly provided by Leif Bergsagel, were modified to express a GFP- Click beetle red luciferase fusion protein (MM.1S-CG) to facilitate detection via flow cytometry and bioluminescent imaging (BLI). OPM2 cells (DMSZ, Germany) were also modified to express CBR-GFP (NM_001195388.2; OPM2-CG) as above. Both cells were further modified to express human FCLRL5 protein (MM.1S-CG- FCRL5 and OPM2-CG-FCRL5. FCLR5 positive cells were sorted using an AUTOMACS and/or a MoFlo sorter followed by single cell cloning. In vitro Killing Assays [00308] CAR-T effector (E) cells were incubated with tumor target (T) cells at a range of (E:T) ratios for 24 and/or 48 hours. Cell death was assessed by addition of Luciferin (150 µg/µl) to the plates which were then imaged on an AMI Imager; Spectral Instruments, Tuscon, AZ. ) to measure photon flux. In some experiments, when MOLP- 2 cells were used as target cells, killing was measured using flow cytometry. In some experiments, MOLP-2-CG were used and BLI was used to quantitate killing. Flow cytometry [00309] Antibodies used were FCRL5 clone 1G7 (APC-Fire, Leinco) or purified 1G7 (Leinco) and modified to add PE using Lighting Link kits (Novus Biologicals). Unlabeled new antibodies generated (Alloy) were used in flow cytometry followed by incubation with R-Phycoerythrin (PE) AffiniPure Goat Anti-Human IgG, Fcg fragment specific (Jackson ImmunoResearch Laboratories).7AAD was used for viability. Samples were run on an Attune Flow Cytometer and analyzed using FlowJo V10 (TreeStar, Ashland, OR). Animal Model and in vivo efficacy [00310] Animal protocols compliant with regulations of Washington University School of Medicine Institutional animal care and use committee. Six to ten- week old NOD.Cg-Prkdcscid Il2rgtm1Wjl/SzJ (NSG) were used in all experiments. 2x10⁶ OPM2-CG-FCRL5 cells were injected intraveneously (i.v.) into tail veins of mice and treated with purified CAR-T cells i.v. For BLI, mice were injected intraperitoneally with 150 µg/g D-luciferin (Goldbio, Saint Louis, MO) and imaged as described previously using an IVIS Imager (Perkin Elmer, Waltham MA) or an AMI Imager (Spectral Instruments, Tucson, AZ). Significant differences in survival were determined using Log Rank (Mantel-Cox) analysis. Example 1 - Generation of human anti-FCRL5 antibodies [00311] ATX-GX^TM mice (Alloy Therapeutics), which are immunocompetent transgenic mice, were used to generate human antibodies that bind to FCRL5. Briefly, mice were immunized with of full length FCRL5 comprising extracellular domains 1-9, or domain 9 of FCRL5 (referred as “D9” (Fig.1). Screening was performed for identifying antibody clones that bind to domains 1-8 of FCRL5 (referred as “D1-8”), or that bind D9 of FCRL5 and full length FCRL5. Table 1 provides the list of anti-human FCRL5 antibody clones identified during the screening, including 23 antibody clones which binds recombinant D9 and full length FCRL5 and 17 antibody clones which binds recombinant D1-8 FCRL5. Table 2 provides the VH and VL sequences associated with the anti-human FCRL5 antibody clones.

Table 2: VH/VL sequences associated with generated clones

Example 2 - Binding of FCRL5 antibodies to MOLP-2 cells [00312] The identified anti-human FCRL5 antibody clones were further tested for their binding on myeloma cells which express FCRL5 at low levels. The MOLP-2 myeloma cell line, which endogenously expresses low levels of FCRL5, were incubated with FCRL5 antibodies and flow cytometry was used to assess binding (Fig 2A). As a negative control, secondary antibody alone was used and FCRL5 antibody clone 1G7 purified antibody and conjugated to PE was used as an independent positive control. The ranked mean fluorescence intensity (MFI) of binding of identified FCRL5 antibodies to MOLP-2 cells is shown in Fig.2B. Results from the experiment identified that ATX-P-973, ATX-P-942, ATX-P-947, ATX-P- 971, ATX-P 980, ATX-P 951, ATX-P- 977, ATX-P-968, ATX-P-948 and ATX-P-941 exhibited good binding efficiencies. Example 3 - Binding of FCRL5 antibodies to MM.1S-CG- FCRL5 cells [00313] The anti-human FCRL5 antibody clones identified from the screen were further assessed for binding to cells which express FCRL5 at high levels. MM.1S cells expressing a GFP-luciferase fusion protein (MM1S-CG) were engineered to express high levels of FCLR5. A set of anti-human FCRL5 antibody clones that bound to MOLP-2 cells were assessed for binding to MM1S-CG-FCRL5 cells. As a negative control, secondary antibody alone was used and FCRL5 antibody clone 1G7 conjugated to PE was used as an independent positive control. Results from flow cytometry is shown in Fig 3A. The specificity of binding the anti-human FCRL5 antibody clones were further demonstrated by flow cytometry analysis of binding of antibody clones to parental MM.1S-CG cells, which do not express FCRL5 (Fig.3B). Example 4 – Killing of human multiple myeloma cell line expressing low and high levels of FCRL5 in vitro. [00314] The anti-human FCRL5 antibody clones were assessed for efficiency of killing myeloma cells lines in vitro. The human multiple myeloma cell line OPM2, was modified to express a GFP-luciferase fusion protein (CG) and human FCRL5, to obtain cells expressing FCRL5 at high levels (OPM2-CG-FCRL5; Fig.4A). Additionally, MOLP-2, a human multiple myeloma cell line expressing FCRL5 at low levels, modified to express GFP and luciferase, MOLP2-CG were also used. FCRL5 expression levels on MOLP-2 and OPM2-CG-FCRL5 cells were compared, as shown in Fig.4B. MOLP-2-CG and OPM2-CG -FCRL5 were evaluated for killing by FCRL5-CAR- T in vitro. FCRL5-CAR-T effector (E) cells generated with scFv sequences from two anti-human FCRL5 antibody clones ATX-942; and ATX-947 were incubated with MOLP-2-CG or OPM2-CG FCRL5 target (T) cells at a range of E:T ratios. Both showed efficient killing in vitro of both MOLP2-CG and OPM2-CG-FCRL5 target cells using bioluminescent imaging (BLI) to measure cell death. (Fig.4C-4D). OPM2-CG-FCRL5 target cells were incubated with FCRL5-CAR-T cells engineered using scFv sequences from seven different antibody clones for 24 hours and 48 hours at a range of E:T ratios and percentage of cell killing was assessed using BLI (Fig.4E). Similarly, MOLP2 target cells were incubated with FCRL5-CAR-T cells engineered using the same scFv sequences from seven different antibody clones for 48 hours. Percentage of cell killing was assessed using flow cytometry and Fig.4F shows data from two separate experiments with either 0.25:1 E:T (left) or 0.13:1 (right). All the antibody clones tested exhibited high killing efficiency compared to control non-transduced T (NTD) cells. Example 5 – FCRL5 CAR-T reduces tumor burden and enhances survival of xenograft mouse model of myeloma. [00315] To the assess the efficacy of FCRL5 CAR-T engineered using the antibody clones in vivo, FCRL5 CAR-T was tested in a xenograft mouse model of myeloma. FCRL5 CAR-T-970 was tested in an in vivo model.2x10⁶ OPM2-CG-FCRL5 cells were injected via i.v. into tail veins of NSG mice. Eighteen days later, 2x10⁶ FCRL5-CAR-T was injected via i.v. into tail veins. (avg. BLI signal at time of treatment: 4.4x10⁸). As control, non-transduced T cells were injected into the mice or the mice were left untreated. Survival was assessed using Kaplan Meier analysis, and tumor burden was measured over time via longitudinal live mouse bioluminescent imaging (BLI). Figs.5A-5B show enhanced survival and reduced tumor burden of mice treated with FCRL5-CAR-T-970 comprising scFv sequence of ATX-P-970. In a separate experiment, NSG mice were engrafted i.v. with OPM2-CG-FCRL5 and treated on day 18 (avg. BLI signal at time of treatment: 1.8x10⁹) with 2x10⁶ FCRL5-CAR-T comprising scFv sequence of ATX-P-948, ATX-P-951, ATX-P-957, or ATX-P-970. FCRL5 CAR-T treated mice exhibited enhanced survival and reduced tumor burden (Figs.5C-5D). Normalized BLI mouse images are further shown in Fig.5E. These results confirm that the antibody clones identified, have high efficacy of killing tumor cells in vivo. Summary of examples [00316] FCRL5 has a large extracellular domain comprised of nine Ig subunits (domains 1-9; D1-9) useful for antibody-based targeting. Since cell surface membrane proximal epitopes can enhance membrane synapse interactions leading to higher function, fully human anti-FCRL5 antibodies were generated to bind specifically to membrane proximal D9, and within D1-8. The generated antibodies were integrated into immune effector cells as targeting domains for chimeric antigen receptors (CAR). Immune effector cells modified with FCRL5-CAR were found to exhibit anti-tumor activities in both multiple myeloma cells that express FCRL5 at low levels and in multiple myeloma cells that express FCRL5 at high levels.

Claims

CLAIMS What is claimed is: 1. An immune effector cell comprising a chimeric antigen receptor (CAR-immune effector cell), wherein the antigen recognition domain of the chimeric antigen receptor specifically binds to FCRL5.

2. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising an amino acid sequence with at least 80% identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. 3. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VL comprising an amino acid sequence with at least 80% identity to the sequence of any one of SEQ ID NOs: 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. 4. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises: a VH comprising an amino acid sequence with at least 80% identity to the sequence of any one of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80; and a VL comprising an amino acid sequence with at least 80% identity to the sequence of any one of SEQ ID NOs: 1,

3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. 5. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising an amino acid sequence of any one of SEQ ID NOs: 2,

4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80. 6. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VL comprising an amino acid sequence of any one of SEQ ID NOs: 1, 3,

5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81. 7. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises: a VH comprising an amino acid sequence of any one of SEQ ID NOs: 2, 4,

6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80; and a VL comprising an amino acid sequence of any one of SEQ ID NOs: 1, 3, 5,

7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81.

8. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLQESGPGLVKPSQTLSLTCTVSGGSISSGGYFWSWIRQHPGKGLEWIGFIYYSG NTYYNPSLKSRVTISVDTSKSQFSLELSSVTAADTAVYYCAREGAAAGTFHYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIK.

9. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLIQPGGSLRLSCAASGLTVSSNYMSWVRQAPGKGLEWVSLIYTGGST YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGWVAFDIWGQGTMVTVS S and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSLTFGGGTKVDIK.

10. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLIQPGGSLRLSCAASGFTVSRNYMTWVRQAPGKGLEWVSVIYSGGTT YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGVVAFDIWGQGTMVTVS S and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPPLTFGGGTKVEIK.

11. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLIQPGGSLRLSCAASGFTVSRNYMTWVRQAPGKGLEWVSVIYTGGST YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGGVAFDIWGQGTMVTVS S and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFALYYCQQYGNSPMSTFGQGTRLEIK.

12. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLIQPGGSLRLSCAASGFTVSRNYMTWVRQAPGKGLEWVSVIYSGGST YYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGVIAFDYWGQGILVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPITFGQGTRLEIK.

13. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMHWVRQAPGQGLEWMGWINPNS GGTKYAQKFQGRVTMTRDTSISTAYMELRRLTSDDTAVYYCVREGGSYYYASSGYDY VPFEYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSMYTFGQGTKVEIK.

14. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFNGYYMHWVRQAPGQGLEWMGWISAYN GNTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCVREGGSYYYASSGYDY VPFEYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKLEIK.

15. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKTSGYTFTGYYIHWVRQAPGQGLEWMGWISAYNG NTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCAREGGSYYYANGGYDY VPFEYWGQGTLVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSFLSASVGDRVTITCRASQGISSYLAWYQQKPGKAPKLLIYAASSLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPITFGQGTRLEIK.

16. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMTPNS VNTGYAQKFQGRVTMTTDTSTSTAYMELSRLRSDDTAVYYCARGPSIMITFGGVIVTP FDYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKVDIK.

17. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMNPNS GNTGYAQKFQGRVTMTRNTSISTAYMELSSLRSEDTAVYYCARGPSILITFGGVIVTPF DYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPYTFGQGTKVDIK.

18. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor of comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMTPNS GNTGYAQKFQGRVTMTRNTSISTAYMELSSLRSEDTAVYYCARGPSILITFGGVIVTPF DYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPATLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASNRATGI PARFSGSGSGTDFTLTISSLQPEDFAVYYCQQYGSSPYTFGQGTRLEIK.

19. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYVHWVRQAPGQGLEWMGWINPNS GGTVSAQKFQGRVTMTRDTSISTAYMELSGLKSDDTAVYSCARFCSITSCYMRGFDY WGQGTLVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSASVGDRVTITCRASQSISSWLAWYQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPLTFGGGTKVDIK.

20. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLEWMGWINPNSG GTDSAQKFQGRVTMTRDTSISTAYMELSRLRSDDTAVYYCAREGGSYYYANGGYYYL PFDFWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYNNWPPTFGQGTKVDIK.

21. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor of comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMQWVRQAPGQGLEWMGWINPNS GDTNYAQKFQGRVTMTRDTSINTVYMELSRLRSDDTAVYYCAREGGSYYYAGGGYY YLPFDYWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSLFTFGPGTKLEIK.

22. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLEWMGLINPNSG GTNYAQKFQGRVTMTRDTSIGTAYMELSRLRSDDSAIYYCTREGGSYYYANGGYYYL PFDFWGQGTLVTVSS and/or a VL comprising the amino acid sequence EIVLTQSPGTLSLSPGERATLSCRASQSVSSSYLAWYQQKPGQAPRLLIYGASSRATGI PDRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKVDIK.

23. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYLYWVRQAPGQGLEWMGWINPNS GDTSYVQKFQGRVTMTRDTSTSTVYMELSRLRSDDTAVYYCARRYSGYLDYWGQGT LVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPVTFGGGTKVEIK.

24. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor of the disclosure comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMYWVRQAPGQGLEWMGLINPNS GDTSYAQKFQGRVTMTRDTSISTVYMELSGLTSDDTAVYYCARRYSGYLDYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPITFGQGTRLEIK.

25. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMEWVRQAPGQGLEWMGLINPNS GGTNYEENFKGRVTMTRDTSISTAYMELSRLRSDDTAVYYCARRDSGFLDYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKAGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPLTFGGGTKVEIK.

26. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of thechimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLQESGPGLVKPSETLSLTCTVSGGSVSSGSYYWSWIRQPPGKGLEWIGFIYYSG STYYNPSLKSRVTISVDTSKNQFSLKLTSVTAADTAVYYCARDGGAAAGTLDYWGQGT LVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPYTFGQGTKVEIK.

27. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLVKPGGSLRLSCAASGFTFSSYDMHWVRQAPGKGLVWVSRIDSYGT YTNYADSVKGRFTISRDNAKNTLYLQMNNLRAEDTAVYYCARIAATASGYWGQGTPVT VSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQRISNYLNWYQQKPGKAPKPLIYAASRLQSGV PSRFSGSGSVTDFTLTISSLQPEDFASYYCQQSYSTPYTFGQGTKVEIK.

28. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QITLKESGPTLVKPTQTLTLTCTFSGFSLSTSGVGVGWIRQPPGKALEWLALIYWNDDK RYSPSLKSRLTITKDTSKNQVVLTMTNVDPVDTATYYCAHRRNSRWYPFDYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIQLTQSPSFLSASVGDRVTITCRASQGISSYLAWYRQKPGKAPKLLIYAVSILQSGVPS RFSGSGSGTDFTLTISSLQPEDFATYYCQQLNSYPITFGQGTRLEIK.

29. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGADVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLEWMGWINPNSG GTNYEQKFQGRVTMTRDTSITTAYMEVSRLRSDDTAVYYCARRWNYGIDYWGQGTL VTVSS and/or a VL comprising the amino acid sequence DIVMTQTPLSSPVTLGQPASISCRSSQSLVYSDGNTYLSWLQQRPGQPPRLLIYKISNR FSGVPDRFSGSGAGTDFTLKISRVEAEDVGVYYCMQAIQFPYTFGQGTKLEIK.

30. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYDG SNKYYVDSVKGRVTISRDNSKNTLYLQMNSLRAEDTAVYYCARGGFDYLPLMDVWGK GTTVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLAVSLGERAIINCKSSQSVLHSSDNKNYLAWYQQKPGQPPKLLIHWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTPWTFGQGTKVEIK.

31. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLQESGPGLVKPSQTLSLTCTVSGGSISSGGYYWSWIRQHPGKGLEWIGYIYYSG STYYNPSLKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCARDGHYDSIGYYFDYWGQ GTLVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQNPGKAPKLLIFTASSLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPRTFGQGTKVEIK.

32. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYDINWVRQATGQGLEWMGWMNPTS GNTGYAQKFQGRVTMTKNTSISTAYMELSNLRSEDTAVYFCARGLYKWNYWGQGTL VTVSS and/or a VL comprising the amino acid sequence EIVMTQSPATLSVSPGERATLSCRASQSVSRNLAWYQQKPGQAPRLLIYGASTRATGI PARFSGSGSGTEFTLTISSLQSEDFAVYSCQQYTNWPALTFGGGTKVEIK.

33. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGVLVQPGGSLRLSCAASGFTFSSYWMHWVRQAPGKGLMWVSRIDSDGT TTNYADSVKGRFTISRDNAKNTLNLQMNSLRAEDTAVYYCARIAATASGYWGQGTLVT VSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSTSVGDRVTITCRASQSISSYLNWYQQKPGKAPNLLIYAASSLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTPITFGQGTRLEIK.

34. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QLQLQESGPGLVKPSETLSLICTVSGGSISSSNYYWGWIRQPPGKGLEWIGSIYYSGS TYYNPSLKSRVTISVDTSNNQFSLRLNSVTAADTAVYYCAREGELKYWFFDLWGRGTL VTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSTLSASVGDRVTITCRASQSIISWLAWYQEKPGKAPKVLIYKASSLESGVP SRFSGSGSGTEFTLTISSLQPDDFATYYCQQYNSYSRTFGQGTKVEIK.

35. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYIHWVRQAPGQGLDWMGWINPNSG VTNYAQKFQGRVTMTRDTSISTAYMDLSRLRSDDTAVYSCARDRGGDSPDAFDLWG QGTMVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLTVSLGERATINCKSSQSVLYSSKNKNYLAWYQQKPGQPPKLLIYWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVFYCQQYYSTPWTFGHGTKVEIK.

36. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTNYGITWVRQAPGQGLEWMGWISAYDG YTNYAQKLQGRVTMTTDTSTSTAYMELRSLRSDDTAVYYCARDYDFWSGLDPWGQG TLVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPLSLPVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKPGQSPQLLIYLGSN RASGVPDRFSGSGSGTDFTLKISRVEAEDVGIYYCMQALQTPWTFGRGTKVEIK.

37. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLVQPGGSLRLSCAASGFILSSYDMHWVRQATGKGLEWVSGIGTAGET YYSGSVKGRFTISRENAKNSLYLQMNSLRAGDTAVYYCAREDYFYYMDVWGKGTTVT VSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQSIRSYLNWYQQKPGKAPKLLIYAASTLQSGVP SRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTRTFGQGTKVEIK.

38. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGDLVKPGGSLRLSCAASGFTFNNAWMSWVRQAPGKGLEWVGRIQSKTD GGTTDYAAPVKGRFTISRDDSKNTLYMQMNSLKAEDTAVYYCTSILTGYYYYYYMDV WGRGTTVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQGISIYLAWYQQKPGKVPKLLIYAASSLQSGVP SRFSGSKSGTDFTLTISSLQPEDVATYYCQKYDSAPFTFGPGTKVDIK.

39. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYWMSWVRQAPGKGLEWVANIKQDGI KKYYVDSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCARDQYCTNGVCYGGWF DPWGQGTLVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSTLSASVGDRVTITCRASQSISSWLAWYQQKPGKAPKVLIYKASSLESGV PSRFSGSGSGTDFTLTISSMQPDDFATYYCQQYNGYSRTFGQGTKVEIK.

40. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLVQPGGSLRLSCAASGFTFNSYAMSWVRQAPGKGLEWVSAISGSGD TTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYHCVKGWKHLWSDYFDHWG PGTLVTVSS and/or a VL comprising the amino acid sequence EIVMTQSPATQSVSPGERATLSCRASQSVNNNLAWYQQKPGQAPRLLIYGASTRATGI PARFSGSGSGTEFTLTISSLQSEDFAVYYCQQYNNWPIAFGQGTRLEIK.

41. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYVMHWVRQAPGKGLEWVSTINWNGD YIGYADSVKGRFTISRDNAKNSLYLQMNSLRAEDTALYYCAKASYMDVWGKGTTVTVS S and/or a VL comprising the amino acid sequence DVVMTQSPLSLPVTLGQPASVSCRSSQSLVYSDGNTYLNWFQQRPGQSPRRLIYKVS NRDSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGTHWTWTFGQGTKLEIK.

42. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVESGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTT NYAQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCARDELYSSSWYGVYWGQGT LVTVSS and/or a VL comprising the amino acid sequence DIVMTQSPLSLPVTPGEPASISCRSSQSLLHSNGYNYLDWYLQKPGQSPQLLIYLGSN RASGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQALQTPWTFGQGTKLEIK.

43. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVQSGAEVKKPGASVKVSCKASGYTFTSYYMYWVRQAPGPGLEWMGIINPSGG RTTYAQKFQGRVTMTRDTSTSTVYMELSSLRSEDTAVYYCARRDDYGALDYWGQGT LVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSLSASVGDRVTITCRASQSIRNYLNWYQQKPGKAPKLLIYDTSNLQSGV PSRFSGSGSGTDLTLTISSLQPDDFATYYCQQSYSIPITFGQGTRLEIK.

44. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLQQSGPGLVKPSQTLSLTCAISGDSVSSNSAAWNWIRQSPSRGLEWLGRTYYRS KWYNDYAASVKSRITINPDTSKNQFSLQLNSVTPEDTAVYYCARDDWYFDLWGRGTL VTVSS and/or a VL comprising the amino acid sequence DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQQPGLPPKLLIFWAS TRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSSPYTFGQGTKVEIK.

45. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence QVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVIWYEG SNKYFADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARDRGTMVRGLHYFDY WGQGTLVTVSS and/or a VL comprising the amino acid sequence AIQMTQSPSSLSASVGDRVTITCRASQDIRNDLGWYQQKPGKAPKLLIYGASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCLQDYNYPWTFGQGTKVEIK.

46. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGVVVQPGGSLRLSCAASGFTFDDYTMHWVRQAPGKGLEWVSLITWDGG RTYYADSVKGRFTISRDNSKNSLYLQMNSLRTEDTALYYCAKDISLDYWGQGTLVTVS S and/or a VL comprising the amino acid sequence DVVMTQSPLSLSVTLGQPASISCRSSQSLVYSDGNTYLNWFQQRPGQSPRRLIYKVS NRDSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGIHWPLTFGGGTKVEIK.

47. The immune effector cell of claim 1, wherein the anti-FCRL5 antigen recognition domain of the chimeric antigen receptor comprises a VH comprising the amino acid sequence EVQLVESGGGLVKPGGSLRLSCAASGFTFSNAWMSWVRQAPGKGLEWVGRIKSKTD GGTTDYAAPVKGRFTISRDDSKNTLYLQMNSLRTEDTAVYYCSTTSLSYYDILTGYYKD YYYYYMDVWGKGTTVTVSS and/or a VL comprising the amino acid sequence DIQMTQSPSSVSTSVGDRVTITCRASQGISSWLAWFQQKPGKAPKLLIYAASSLQSGV PSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFPLTFGGGTKVEIK.

48. The immune effector cell of any of the preceding claims, wherein the CAR-T cell further comprises a suicide gene.

49. The immune effector cell of claim 48, wherein the suicide gene encodes a modified Human-Herpes Simplex Virus-1-thymidine kinase (TK) gene fused in-frame to the extracellular and transmembrane domains of the human CD34 cDNA.

50. A method of killing a malignant cell in a subject in need thereof, the method comprising administering an immune effector cell of any one of the preceding claims.

51. The method of claim 50, wherein the malignant cell is a malignant B cell or a malignant plasma cell.

52. The method of claim 50, wherein the malignant cell is a Burkitt lymphoma, chronic lymphocytic leukemia/small lymphocytic lymphoma (CLL/SLL), diffuse large B-cell lymphoma, follicular lymphoma, or mantle cell lymphoma, Monoclonal gammopathy of undetermined significance, Lymphoplasmacytic lymphoma, Plasmacytoma, or myeloma.

53. The method of claim 50, wherein the malignant cell is a myeloma cell.

54. A method of treating a mammal having a cell malignancy, the method comprising administering to the mammal a plurality of chimeric antigen receptor immune effector cells of any one of the preceding claims.