Human Fc Receptor–Like 5 Binds Intact IgG via Mechanisms Distinct from Those of Fc Receptors
Open accessAbstract
Fc receptor–like (FCRL) 5 regulates B cell Ag receptor signaling and has been reported to bind aggregated IgG. Using surface plasmon resonance, we analyzed the interaction of native IgG samples with FCRL5, revealing a complex binding mechanism, where isotype is just one factor. FCRL5 bound IgG1 and IgG4 with ∼1 μM KD, whereas the interaction with IgG3 was a magnitude weaker. However, IgG2 samples displayed a wide range of affinities, indicating that additional factors affect binding. We used a panel of 19 anti-FCRL5 mAbs with defined reactivity to identify domains involved in ligand binding. Six mAbs blocked IgG binding, indicating critical roles of FCRL5 domains 1 and 3, as well as epitopes at the domain 1/2 and domain 2/3 boundaries. We found that only glycosylated IgG containing both Fab arms and the Fc region bound with high affinity. Furthermore, the presence of sialic acid in the IgG carbohydrate altered FCRL5 binding. The interaction of IgG and FCRL5 consisted of two kinetic components, suggesting a complex binding mechanism. We established that the IgG-Fc and IgG-F(ab′)2 fragments bind FCRL5 independently but with low affinity, revealing the mechanism behind the two-step binding of whole IgG. This complex binding mechanism is distinct from that of Fc receptors, which bind through the Fc. We propose that FCRL5 is a new type of receptor that recognizes intact IgG, possibly enabling B cells to sense Ig quality. Recognition of undamaged IgG molecules by FCRL5 could allow B cells to engage recently produced Abs.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
FCRL5 encodes Fc receptor-like 5 that regulates B-cell antigen receptor signaling.
“FCRL5 encodes Fc receptor-like 5 that regulates B-cell antigen receptor signaling.59”
From APOE*E2 allele delays age of onset in PSEN1 E280A Alzheimer’s disease (2016) · cites this paper as [59]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Fcγ receptors as regulators of immune responses
Nimmerjahn, F., & Ravetch, J. V. (2008) · Nature Reviews Immunology · doi:10.1038/nri2206 · Cited by 2,947 · see citing works
Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation
Kaneko, Y., Nimmerjahn, F., & Ravetch, J. V. (2006) · Science · doi:10.1126/science.1129594 · Cited by 1,754 · see citing works
Bruhns, P., Iannascoli, B., England, P., Mancardi, D. A., Fernandez, N., Jorieux, S., & Daëron, M. (2009) · Blood · doi:10.1182/blood-2008-09-179754 · Cited by 1,479 · see citing works
Friguet, B., Chaffotte, A. F., Djavadi‐Ohaniance, L., & Goldberg, M. E. (1985) · Journal of Immunological Methods · doi:10.1016/0022-1759(85)90044-4 · Cited by 1,235 · see citing works
Anti-Inflammatory Activity of Human IgG4 Antibodies by Dynamic Fab Arm Exchange
Kolfschoten, M. V. D. N., Schuurman, J., Losen, M. H., Bleeker, W. K., Martínez‐Martínez, P., Vermeulen, E., den Bleker, T. H., Wiegman, L., Vink, T., Aarden, L. A., et al. (2007) · Science · doi:10.1126/science.1144603 · Cited by 972 · see citing works
The 3.2-Å crystal structure of the human IgG1 Fc fragment–FcγRIII complex
Sondermann, P., Huber, R., Oosthuizen, V., & Jacob, U. (2000) · Nature · doi:10.1038/35018508 · Cited by 719 · see citing works
Kochi, Y., Yamada, R., Suzuki, A., Harley, J. B., Shirasawa, S., Sawada, T., Bae, S., Tokuhiro, S., Chang, X., Sekine, A., et al. (2005) · Nature Genetics · doi:10.1038/ng1540 · Cited by 390 · see citing works
The Carbohydrate at FcγRIIIa Asn-162
Ferrara, C., Stuart, F., Sondermann, P., Brünker, P., & Umaña, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510171200 · Cited by 355 · see citing works
Mimura, Y., Church, S., Ghirlando, R., Ashton, P., Dong, S.-C., Goodall, M., Lund, J., & Jefferis, R. (2000) · Molecular Immunology · doi:10.1016/s0161-5890(00)00105-x · Cited by 337 · see citing works
Human IgG2 Antibodies Display Disulfide-mediated Structural Isoforms
Wypych, J., Li, M., Guo, A., Zhang, Z., Martinez, T., Allen, M. J., Fodor, S., Kelner, D. N., Flynn, G. C., Liu, D., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709987200 · Cited by 286 · see citing works
Contrasting IgG structures reveal extreme asymmetry and flexibility.
Saphire, E., Stanfield, R., Maxcrispin, M., Parren, P., Rudd, P., Dwek, R., Burton, D., & Wilson, I. A. G. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00244-9 · Cited by 249 · see citing works
Role of Oligosaccharide Residues of IgG1-Fc in FcγRIIb Binding
Mimura, Y., Sondermann, P., Ghirlando, R., Lund, J., Young, S. P., Goodall, M., & Jefferis, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107478200 · Cited by 236 · see citing works
Davis, R. S. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141541 · Cited by 225 · see citing works
Identification of a family of Fc receptor homologs with preferential B cell expression
Davis, R. S., Wang, Y., Kubagawa, H., & Cooper, M. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171308498 · Cited by 217 · see citing works
Hatzivassiliou, G., Miller, I. J., Takizawa, J., Palanisamy, N., Rao, P. H., Iida, S., Tagawa, S., Taniwaki, M., Russo, J. J., Neri, A., et al. (2001) · Immunity · doi:10.1016/s1074-7613(01)00109-1 · Cited by 193 · see citing works
Polson, A. G. (2006) · International Immunology · doi:10.1093/intimm/dxl069 · Cited by 141 · see citing works
Maenaka, K., van der Merwe, P. A., Stuart, D. I., Jones, E. Y., & Sondermann, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106819200 · Cited by 134 · see citing works
Cutting Edge: Human FcRL4 and FcRL5 Are Receptors for IgA and IgG
Wilson, T. J., Fuchs, A. G., & Colonna, M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102651 · Cited by 134 · see citing works
The inhibitory potential of Fc receptor homolog 4 on memory B cells
Ehrhardt, G. R. A., Davis, R. S., Hsu, J. T., Leu, C., Ehrhardt, A., & Cooper, M. D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1935944100 · Cited by 127 · see citing works
Human IgG2 Can Form Covalent Dimers
Yoo, E. M., Wims, L. A., Chan, L. A., & Morrison, S. L. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.6.3134 · Cited by 126 · see citing works
Käsermann, F., Boerema, D. J., Monika, R., Hofmann, A., Wymann, S., Zuercher, A. W., & Miescher, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037243 · Cited by 124 · see citing works
The recombination of dimers of immunoglobulin peptide chains
Stevenson, G. T., & Dorrington, K. J. (1970) · Biochemical Journal · doi:10.1042/bj1180703 · Cited by 121 · see citing works
Human IgG2 Antibody Disulfide Rearrangement in Vivo
Liu, D., Chen, X., Enk, J. Z.-V., Plant, M., Dillon, T. M., & Flynn, G. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804787200 · Cited by 116 · see citing works
Guhr, T., Bloem, J., Derksen, N. I. L., Wuhrer, M., Koenderman, A. H. L., Aalberse, R. C., & Rispens, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021246 · Cited by 113 · see citing works
A close look at human IgG sialylation and subclass distribution after lectin fractionation
Stadlmann, J., Weber, A., Pabst, M., Anderle, H., Kunert, R., Ehrlich, H. J., Schwarz, H. P., & Altmann, F. (2009) · PROTEOMICS · doi:10.1002/pmic.200800931 · Cited by 109 · see citing works
Fc receptor-like 5 inhibits B cell activation via SHP-1 tyrosine phosphatase recruitment
Haga, C. L., Ehrhardt, G. R. A., Boohaker, R. J., Davis, R. S., & Cooper, M. D. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703354104 · Cited by 107 · see citing works
Kochi, Y., Myouzen, K., Yamada, R., Suzuki, A., Kurosaki, T., Nakamura, Y., & Yamamoto, K. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901982 · Cited by 101 · see citing works
FcRL5 as a Target of Antibody–Drug Conjugates for the Treatment of Multiple Myeloma
Elkins, K., Zheng, B., Go, M., Slaga, D., Du, C., Scales, S. J., Yu, S., McBride, J., Tute, R. M. D., Rawstron, A. C., et al. (2012) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-0087 · Cited by 97 · see citing works
A Plasmablast Biomarker for Nonresponse to Antibody Therapy to CD20 in Rheumatoid Arthritis
Owczarczyk, K. M., Lal, P. G., Abbas, A. R., Wolslegel, K., Holweg, C. T. J., Dummer, W., Kelman, A., Brunetta, P. G., Lewin‐Koh, N., Sorani, M. D., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002432 · Cited by 94 · see citing works
FcRH1: an activation coreceptor on human B cells
Leu, C.-M. (2004) · Blood · doi:10.1182/blood-2004-06-2344 · Cited by 82 · see citing works
Cutting Edge: FcR-Like 6 Is an MHC Class II Receptor
Schreeder, D. M., Cannon, J. P., Wu, J., Li, R., Shakhmatov, M. A., & Davis, R. S. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000832 · Cited by 71 · see citing works
Ise, T., Nagata, S., Kreitman, R. J., Wilson, W. H., Wayne, A. S., Stetler‐Stevenson, M., Bishop, M. R., Scheinberg, D., Rassenti, L. Z., Kipps, T. J., et al. (2006) · Leukemia · doi:10.1038/sj.leu.2404445 · Cited by 67 · see citing works
Self-citationDement-Brown, J., Newton, C. S., Ise, T., Damdinsuren, B., Nagata, S., & Tolnay, M. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.0211096 · Cited by 66 · see citing works
Self-citationLi, F. J., Ding, S., Pan, J., Shakhmatov, M. A., Kashentseva, E. A., Wu, J., Li, Y., Soong, S.-J., Chiorazzi, N., & Davis, R. S. (2008) · Blood · doi:10.1182/blood-2008-01-131359 · Cited by 62 · see citing works
Vidal-Laliena, M., Ros, X. R., March, S., Requena, V., Pétriz, J., & Engel, P. (2005) · Cellular Immunology · doi:10.1016/j.cellimm.2005.08.002 · Cited by 60 · see citing works
FcR-Like 2 Inhibition of B Cell Receptor-Mediated Activation of B Cells
Jackson, T., Haga, C. L., Ehrhardt, G. R. A., Davis, R. S., & Cooper, M. D. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1002305 · Cited by 55 · see citing works
Nagata, S., Salvatore, G., & Pastan, I. H. (2003) · Journal of Immunological Methods · doi:10.1016/s0022-1759(03)00192-3 · Cited by 48 · see citing works
Self-citationIse, T., Maeda, H., Santora, K., Xiang, L., Kreitman, R. J., Pastan, I. H., & Nagata, S. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.87.11.1 · Cited by 42 · see citing works
Self-citationSantiago, T., Викторович, К. С., Reshetnikova, E. S., Chikaev, N. A., Volkova, O. Y., Мечетина, Л. В., Zhao, M., Davis, R. S., Taranin, A. V., Najakshin, A. M., et al. (2010) · International Immunology · doi:10.1093/intimm/dxq456 · Cited by 40 · see citing works
Wilson, T. J., Gilfillan, S., & Colonna, M. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1001428 · Cited by 38 · see citing works
SPAP2, an Ig family receptor containing both ITIMs and ITAMs
Xu, M., Zhao, R., Cao, H., & Zhao, Z. J. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00332-7 · Cited by 33 · see citing works
Hambly, D. M., Banks, D. D., Scavezze, J. L., Siska, C. C., & Gadgil, H. S. (2009) · Analytical Chemistry · doi:10.1021/ac901258g · Cited by 32 · see citing works
Epstein-Barr virus nuclear antigen 2 induces FcRH5 expression through CBF1
Mohan, J., Dement-Brown, J., Maier, S., Ise, T., Kempkes, B., & Tolnay, M. (2006) · Blood · doi:10.1182/blood-2005-09-3815 · Cited by 31 · see citing works
Self-citationNagata, S., Numata, Y., Onda, M., Ise, T., Hahn, Y., Lee, B., & Pastan, I. H. (2004) · Journal of Immunological Methods · doi:10.1016/j.jim.2004.06.009 · Cited by 27 · see citing works
Self-citationIse, T., Kreitman, R. J., Pastan, I. H., & Nagata, S. (2006) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2006.115 · Cited by 6 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Circulating and intrahepatic antiviral B cells are defective in hepatitis B
Burton, A. R., Pallett, L. J., McCoy, L. E., Suveizdytė, K., Amin, O. E., Swadling, L., Alberts, E., Davidson, B. R., Kennedy, P. T. F., Gill, U. S., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci121960 · Cited by 327 · see citing works
The unique properties of IgG4 and its roles in health and disease
Rispens, T., & Huijbers, M. G. M. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00871-z · Cited by 268 · see citing works
Fc fusion as a platform technology: potential for modulating immunogenicity
Levin, D., Golding, B., Strome, S. E., & Sauna, Z. E. (2014) · Trends in biotechnology · doi:10.1016/j.tibtech.2014.11.001 · Cited by 192 · see citing works
The Ligands for Human IgG and Their Effector Functions
de Taeye, S. W., Rispens, T., & Vidarsson, G. (2019) · Antibodies · doi:10.3390/antib8020030 · Cited by 170 · see citing works
Of ITIM s, ITAM s, and ITAM is: revisiting immunoglobulin Fc receptor signaling
Getahun, A., & Cambier, J. C. (2015) · Immunological Reviews · doi:10.1111/imr.12336 · Cited by 163 · see citing works
FCRL5 Delineates Functionally Impaired Memory B Cells Associated with Plasmodium falciparum Exposure
Sullivan, R. T., Kim, C. C., Fontana, M. F., Feeney, M. E., Jagannathan, P., Boyle, M. J., DRAKELEY, C. J., Ssewanyana, I., Nankya, F., Mayanja‐Kizza, H., et al. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004894 · Cited by 150 · see citing works
Gillis, C. M., Gouél‐Cheron, A., Jönsson, F., & Bruhns, P. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00254 · Cited by 137 · see citing works
Fc Receptors for Immunoglobulins and Their Appearance during Vertebrate Evolution
Akula, S., Mohammadamin, S., & Hellman, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096903 · Cited by 127 · see citing works
Impact of structural modifications of IgG antibodies on effector functions
Damelang, T., Brinkhaus, M., van Osch, T. L. J., Schuurman, J., Labrijn, A. F., Rispens, T., & Vidarsson, G. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1304365 · Cited by 128 · see citing works
APOE*E2 allele delays age of onset in PSEN1 E280A Alzheimer’s disease
Vélez, J. I., Lopera, F., Sepulveda-Falla, D., Patel, H. R., Johar, A. S., Chuah, A., Tobón, C., Rivera, D., Villegas, A., Cai, Y., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2015.177 · Cited by 111 · see citing works
Caraccio, C., Krishna, S., Phillips, D. J., & Schürch, C. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00501 · Cited by 106 · see citing works
CAR-T cell therapy in Multiple Myeloma: current status and future challenges
Swan, D., Madduri, D., & Hocking, J. S. (2024) · Blood Cancer Journal · doi:10.1038/s41408-024-01191-8 · Cited by 104 · see citing works
Highly parallel characterization of IgG Fc binding interactions
Boesch, A. W., Brown, E. P., Cheng, H. D., Ofori, M. O., Normandin, E., Nigrovic, P. A., Alter, G., & Ackerman, M. E. (2014) · mAbs · doi:10.4161/mabs.28808 · Cited by 90 · see citing works
Li, H., Borrego, F., Nagata, S., & Tolnay, M. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501027 · Cited by 81 · see citing works
Self-citationHuman Fc Receptor-like 3 Inhibits Regulatory T Cell Function and Binds Secretory IgA
Agarwal, S., Kraus, Z., Dement-Brown, J., Alabi, O., Starost, K. A., & Tolnay, M. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.099 · Cited by 77 · see citing works
Self-citationUpdate on Fc receptor-like (FCRL) family: new immunoregulatory players in health and diseases
Rostamzadeh, D., Kazemi, T., Amirghofran, Z., & Shabani, M. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2018.1472768 · Cited by 68 · see citing works
A close-up on the expanding landscape of CD21–/low B cells in humans
Gjertsson, I., McGrath, S., Grimstad, K., Jonsson, C. A., Camponeschi, A., Thorarinsdottir, K., & Mårtensson, I. (2022) · Clinical & Experimental Immunology · doi:10.1093/cei/uxac103 · Cited by 65 · see citing works
Walsh, A. M., Whitaker, J. W., Huang, C., Cherkas, Y., Lamberth, S. L., Brodmerkel, C. M., Curran, M. E., & Dobrin, R. (2016) · Genome biology · doi:10.1186/s13059-016-0948-6 · Cited by 58 · see citing works
Emerging Roles for the FCRL Family Members in Lymphocyte Biology and Disease
Li, F. J., Won, W.-J., Becker, E., Easlick, J. L., Tabengwa, E. M., Li, R., Shakhmatov, M. A., Honjo, K., Burrows, P. D., & Davis, R. S. (2014) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-07911-0_2 · Cited by 60 · see citing works
The Multiple Functions of B Cells in Chronic HBV Infection
Cai, Y., & Yin, W. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.582292 · Cited by 54 · see citing works
Mohan, N., Luo, X. L., Shen, Y., Olson, Z., Agrawal, A., Endo, Y., Rotstein, D. S., Pelosof, L. C., & Wu, W. J. (2021) · Cancers · doi:10.3390/cancers13051027 · Cited by 54 · see citing works
Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies
Le, N. P. L., Bowden, T. A., Struwe, W. B., & Crispin, M. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.04.016 · Cited by 49 · see citing works
Ambegaonkar, A. A., Nagata, S., Pierce, S. K., & Sohn, H. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00852 · Cited by 44 · see citing works
Self-citationBispecific Antibodies in Multiple Myeloma: Opportunities to Enhance Efficacy and Improve Safety
Swan, D., Murphy, P. T., Glavey, S. V., & Quinn, J. (2023) · Cancers · doi:10.3390/cancers15061819 · Cited by 42 · see citing works
Promising Antigens for the New Frontier of Targeted Immunotherapy in Multiple Myeloma
Cho, S., Xing, L., Anderson, K. C., & Tai, Y. (2021) · Cancers · doi:10.3390/cancers13236136 · Cited by 40 · see citing works
Characterization of heme binding to recombinant α1-microglobulin
Karnaukhova, E., Rutardottir, S., Rajabi, M., Wester-Rosenlöf, L., Alayash, A. I., & Ã...kerström, B. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00465 · Cited by 39 · see citing works
Developing the IVIG biomimetic, Hexa-Fc, for drug and vaccine applications
Czajkowsky, D. M., Andersen, J. T., Fuchs, A., Wilson, T. J., Mekhaiel, D., Colonna, M., He, J., Shao, Z., Mitchell, D. A., Wu, G., et al. (2015) · Scientific Reports · doi:10.1038/srep09526 · Cited by 38 · see citing works
Roles for the FCRL6 Immunoreceptor in Tumor Immunology
Davis, R. S. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.575175 · Cited by 33 · see citing works
Potential functions of atypical memory B cells in Plasmodium-exposed individuals
Braddom, A. E., Batugedara, G., Bol, S. M., & Bunnik, E. M. (2020) · International Journal for Parasitology · doi:10.1016/j.ijpara.2020.08.003 · Cited by 31 · see citing works
FCRL regulation in innate‐like B cells
Davis, R. S. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12771 · Cited by 31 · see citing works
Fc receptor-like 4 and 5 define human atypical memory B cells
Li, H., Dement-Brown, J., Liao, P., Mazo, I. A., Mills, F., Kraus, Z., Fitzsimmons, S. P., & Tolnay, M. (2020) · International Immunology · doi:10.1093/intimm/dxaa053 · Cited by 30 · see citing works
Self-citationLymphocytes sense antibodies through human FCRL proteins: Emerging roles in mucosal immunity
Tolnay, M. (2021) · Journal of Leukocyte Biology · doi:10.1002/jlb.4ru0221-102rr · Cited by 30 · see citing works
Self-citationCheng, H. D., Stöckmann, H., Adamczyk, B., McManus, C. A., Ercan, A., Holm, I. A., Rudd, P. M., Ackerman, M. E., & Nigrovic, P. A. (2017) · Glycobiology · doi:10.1093/glycob/cwx082 · Cited by 29 · see citing works
CD21 and FCRL5 form a receptor complex with robust B-cell activating capacity
Franco, A., Kraus, Z., Li, H., Seibert, N., Dement-Brown, J., & Tolnay, M. (2018) · International Immunology · doi:10.1093/intimm/dxy052 · Cited by 29 · see citing works
Self-citationShi, Y., Zhang, Q. Y., Zhai, T.-T., Zhou, Y., Yang, D., Wang, F., & Xia, X. (2018) · Electrochimica Acta · doi:10.1016/j.electacta.2018.03.167 · Cited by 28 · see citing works
Engineering of Fc Multimers as a Protein Therapy for Autoimmune Disease
Fitzpatrick, E. A., Wang, J., & Strome, S. E. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00496 · Cited by 26 · see citing works
Upregulated Fcrl5 disrupts B cell anergy and causes autoimmune disease
Ono, C., Tanaka, S., Myouzen, K., Iwasaki, T., Ueda, M. T., Oda, Y., Yamamoto, K., Kochi, Y., & Baba, Y. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1276014 · Cited by 25 · see citing works
Hosny, M., Verkleij, C. P. M., van der Schans, J., Frerichs, K. A., Mutis, T., Zweegman, S., & van de Donk, N. W. C. J. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10194593 · Cited by 24 · see citing works
FCRL1 immunoregulation in B cell development and malignancy
Mamidi, M. K., Huang, J., Honjo, K., Li, R., Tabengwa, E. M., Neeli, I., Randall, N. L., Ponnuchetty, M. V., Radic, M. Z., Leu, C., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1251127 · Cited by 21 · see citing works
Evolution of Fc Receptor-Like Scavenger in Mammals
Matos, M. C., Pinheiro, A., Melo‐Ferreira, J., Davis, R. S., & Esteves, P. J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.590280 · Cited by 20 · see citing works
IgG opsonization of merozoites: multiple immune mechanisms for malaria vaccine development
Hill, D. L., Schofield, L., & Wilson, D. W. (2017) · International Journal for Parasitology · doi:10.1016/j.ijpara.2017.05.004 · Cited by 20 · see citing works
Owczarczyk, K. M., Cascino, M. D., Holweg, C. T. J., Tew, G. W., Ortmann, W. A., Behrens, T. W., Schindler, T. H., Langford, C. A., Clair, E. W. S., Merkel, P. A., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.136180 · Cited by 19 · see citing works
Terrier, B., Nagata, S., Ise, T., Rosenzwajg, M., Pastan, I. H., Klatzmann, D., Saadoun, D., & Cacoub, P. (2013) · Arthritis & Rheumatology · doi:10.1002/art.38222 · Cited by 19 · see citing works
Self-citationThe evolving status of immunotherapies in multiple myeloma: the future role of bispecific antibodies
Swan, D., Routledge, D. J. M., & Harrison, S. J. (2021) · British Journal of Haematology · doi:10.1111/bjh.17805 · Cited by 19 · see citing works
Improved protein binder design using β-pairing targeted RFdiffusion
Sappington, I., Toul, M., Lee, D. S., Robinson, S. A., Goreshnik, I., McCurdy, C., Chan, T. C., Buchholz, N., Huang, B., Vafeados, D. K., et al. (2026) · Nature Communications · doi:10.1038/s41467-025-67866-3 · Cited by 33 · see citing works
Antibody Fc-chimerism and effector functions: When IgG takes advantage of IgA
Cottignies-Calamarte, A., Tudor, D., & Bomsel, M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1037033 · Cited by 18 · see citing works
O’Neill, C. A., & van de Donk, N. W. C. J. (2023) · eJHaem · doi:10.1002/jha2.729 · Cited by 17 · see citing works
Goldmann, K., Spiliopoulou, A., Iakovliev, A., Plant, D., Nair, N., Çubuk, C., McKeigue, P., Barnes, M. R., Barton, A. C., Pitzalis, C., et al. (2023) · Annals of the Rheumatic Diseases · doi:10.1136/ard-2023-224540 · Cited by 18 · see citing works
Therapeutic normal IgG intravenous immunoglobulin activates Wnt-β-catenin pathway in dendritic cells
Karnam, A., Rambabu, N., Das, M., Bou-Jaoudeh, M., Delignat, S., Käsermann, F., Lacroix‐Desmazes, S., Kaveri, S. V., & Bayry, J. (2020) · Communications Biology · doi:10.1038/s42003-020-0825-4 · Cited by 18 · see citing works
Dual B-cell targeting therapy ameliorates autoimmune cholangitis
Zhang, W., Shao, T., Leung, P. S. C., Tsuneyama, K., Heuer, L. S., Young, H. A., Ridgway, W. M., & Gershwin, M. E. (2022) · Journal of Autoimmunity · doi:10.1016/j.jaut.2022.102897 · Cited by 17 · see citing works
Antibody-drug conjugates, bispecific antibodies and CAR-T cells therapy in multiple myeloma
Tacchetti, P., Talarico, M., Barbato, S., Pantani, L., Mancuso, K., Rizzello, I., Zamagni, E., & Cavo, M. (2024) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2024.2344647 · Cited by 16 · see citing works
Gu, Z., Shen, Y., Tang, X., Xia, K., Yao, H., Hong, S., & Kang, H. (2019) · International Journal of Pediatric Otorhinolaryngology · doi:10.1016/j.ijporl.2019.02.015 · Cited by 14 · see citing works
Bispecific Antibodies for the Management of Relapsed/Refractory Multiple Myeloma
Tacchetti, P., Barbato, S., Mancuso, K., Zamagni, E., & Cavo, M. (2024) · Cancers · doi:10.3390/cancers16132337 · Cited by 12 · see citing works
Blackburn, T. E., Santiago, T., & Burrows, P. D. (2017) · Current topics in microbiology and immunology · doi:10.1007/82_2017_40 · Cited by 11 · see citing works
Damdinsuren, B., Dement-Brown, J., Li, H., & Tolnay, M. (2016) · Molecular Immunology · doi:10.1016/j.molimm.2016.04.001 · Cited by 11 · see citing works
Self-citationBlundell, P. A., Lu, D., Wilkinson, M., Dell, A., Haslam, S., & Pleass, R. J. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1801337 · Cited by 11 · see citing works
Human Fc receptor-like 5 distinguishes IgG2 disulfide isoforms and deamidated charge variants
Alabi, O., Dement-Brown, J., & Tolnay, M. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.10.020 · Cited by 10 · see citing works
Self-citationWang, J., Belosevic, M., & Stafford, J. L. (2021) · Immunogenetics · doi:10.1007/s00251-020-01193-3 · Cited by 10 · see citing works
The yin/yang balance of the MHC-self-immunopeptidome
Santambrogio, L., & Franco, A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1035363 · Cited by 8 · see citing works
Self-citationHuman FcRL5 is an Fc receptor that simultaneously engages two IgGs
Chen, S., Li, S., Zhang, Z., & Xiao, J. (2026) · Science Advances · doi:10.1126/sciadv.aeb8865 · Cited by 6 · see citing works
Fc receptor-like proteins and their role in B-cell responses and autoimmune diseases
Haroun, C., Kroese, F. G. M., & Verstappen, G. M. P. J. (2026) · Immunology Letters · doi:10.1016/j.imlet.2026.107144 · Cited by 5 · see citing works
Fc Receptors and Fc Receptor-Like Molecules within the Immunoreceptor Family
Daëron, M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-374279-7.02017-8 · Cited by 5 · see citing works
Segers, F., & Delforge, M. (2026) · Targeted Oncology · doi:10.1007/s11523-025-01189-7 · Cited by 4 · see citing works
Ravetch, J. V., & Bournazos, S. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95895-0.00005-2 · Cited by 4 · see citing works
Matos, M. C., Pinheiro, A., Davis, R. S., & Esteves, P. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054531 · Cited by 4 · see citing works
Humoral responses are enhanced by facilitating B cell viability by Fcrl5 overexpression in B cells
Ono, C., Kochi, Y., Baba, Y., & Tanaka, S. (2024) · International Immunology · doi:10.1093/intimm/dxae028 · Cited by 3 · see citing works
FCRL5, a B-Cell Marker With Novel Diagnostic and Prognostic Value for Multiple Sclerosis
Deltombe, M., Stölting, A., Maggi, P., & Pesch, V. V. (2025) · Neurology Neuroimmunology & Neuroinflammation · doi:10.1212/nxi.0000000000200485 · Cited by 2 · see citing works
Fcγ receptors in autoimmunity and end-organ damage
Ernandez, T., Okubo, K., Saggu, G., & Mayadas, T. N. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-814551-7.00022-2 · Cited by 1 · see citing works
Bhatia, U., Tadman, S., Rocha, A., Rudraboina, R., Contreras‐Ruiz, L., & Guinan, E. C. (2024) · American Journal of Transplantation · doi:10.1016/j.ajt.2024.06.014 · Cited by 1 · see citing works
Ernandez, T., Saggu, G., & Mayadas, T. N. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801917-7.00020-6 · Cited by 1 · see citing works
Herpers, B. M., Guo, M., Ko, S., Delidakis, G., Kim, J. E., Lee, C.-H., Gadallah, M. I., Brodbelt, J. S., Zhang, Y. J., & Georgiou, G. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.16.718972 · Cited by 1 · see citing works
Ravetch, J. V., Nimmerjahn, F., & Carroll, M. C. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397933-9.00011-4
Upregulated Fcrl5 disrupts B cell anergy and causes autoimmunityPreprint
Ono, C., Tanaka, S., Myouzen, K., Iwasaki, T., Ueda, M. T., Oda, Y., Yamamoto, K., Kochi, Y., & Baba, Y. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.20.549843
Fc Receptors and Fc Receptor-Like Molecules
Daëron, M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-128-24465-4.00130-7
Enrichment and Clinical Relevance of FcRL5⁺CD27⁺ B Cells in Autoimmune HepatitisPreprint
Liu, Y., Pu, X., Guo, C., Wen, H., Zhao, Y., Xia, Q., Qian, J., Ma, X., You, Z., & Wang, Q. (2025) · Research Square · doi:10.21203/rs.3.rs-6509177/v1
Gillis, C. M. (2016) · theses.fr (ABES) · doi:10.70675/1241fe8dz6786z444dz9ee3z6e9ecc9348a2
Deveuve, Q. (2020) · theses.fr (ABES) · doi:10.70675/0846fa89zb47dz41afzaa8bz1aba36466f1d
Eradication of FVIII inhibitors in patients with hemophilia A
Bou-Jaoudeh, M. (2023) · theses.fr (ABES) · doi:10.70675/fb0159d0zb989z4a8dz9ca2zc27e4e44e055
Humoral pathogenesis: Fcγ receptors in autoimmunity and end-organ damage
Ganesan, L. P., Ito, Y., Ernandez, T., & Mayadas, T. N. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-33957-8.00027-5
Yu, C., Zhang, M., Hui, J., Zhu, M., Sun, Z., Sun, Y., Sun, Q., Yan, Z., Zhu, F., Niu, M., et al. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1765006
van der Hoeven, N., Holborough-Kerkvliet, M. D., Bao, Y., Bentlage, A. E. H., Heer, P. O., Derksen, N. I. L., Damelang, T., de Kreuk, B.-J., Labrijn, A. F., Vidarsson, G., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.01.735886
Herpers, B. M., Guo, M., Ko, S., Delidakis, G., Kim, J. E., Lee, C., Gadallah, M. I., Brodbelt, J. S., Zhang, Y., & Georgiou, G. (2026) · Science Advances · doi:10.1126/sciadv.aei1233 · Cited by 1 · see citing works
Rietdijk, M. H., Kuhnen, L. C., van den Braber, M., Paul, A., Pascutti, M. F., & García-Vallejo, J. J. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1894779
Su, S., Yan, S., Wu, J., & Xiao, Y. (2026) · Stem Cell Reviews and Reports · doi:10.1007/s12015-026-11228-z
- Authors
- Franco, A., Damdinsuren, B., Ise, T., Dement-Brown, J., Li, H., Nagata, S., & Tolnay, M.
- Affiliations
- United States Food and Drug Administration (US)
- Sanford Research (US)
- Division of Monoclonal Antibodies, Center for Drug Evaluation and Research, Food and Drug Administration , Silver Spring, MD 20993
- Corresponding author
- Franco, Andrea
- Damdinsuren, Bazarragchaa
- Li, Huifang
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-06-01
- Volume
- 190
- Issue
- 11
- Pages
- 5739-5746
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- PMC
- PMC3660407
- OpenAlex
- W2164793815
- Cited by
- 85
- References
- 45
- Citations by year
- 2026: 11 · 2025: 2 · 2024: 8 · 2023: 10 · 2022: 3 · 2021: 7 · 2020: 12 · 2019: 4 · 2018: 4 · 2017: 4 · 2016: 7 · 2015: 5 · 2014: 7 · 2013: 1
- FWCI
- 5.16
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The Journal of Immunology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Center for Research Resources (P20RR024219)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- FCRL5, IgG isotypes, B cell receptor signaling, sialic acid, IgG glycosylation, Fc fragment, F(ab')2 fragments, binding kinetics
- MeSH terms
- Antibody Affinity, Epitopes, Cell Line, Cell Membrane, Humans, Immunoglobulin G, Kinetics, Protein Binding, Receptors, Cell Surface, Receptors, Fc, Recombinant Proteins, Protein Interaction Domains and Motifs
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
