ArticleJournal of immunology (Baltimore, Md. : 1950)2013
Human Fc receptor-like 5 binds intact IgG via mechanisms distinct from those of Fc receptors.
Article in Journal of immunology (Baltimore, Md. : 1950), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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The trial behind it
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Who cites it
53 citing papers in PubMed, 74 citations in OpenAlex.
- Fc receptor-like 5 and anti-CD20 treatment response in granulomatosis with polyangiitis and microscopic polyangiitis.JCI insight · 2020Trial
- Circulating and intrahepatic antiviral B cells are defective in hepatitis B.The Journal of clinical investigation · 2018Trial
- High-throughput characterization of the functional impact of IgG Fc glycan aberrancy in juvenile idiopathic arthritis.Glycobiology · 2017Trial
- Structure-function analysis of the FCRL5-IgG1 Fc complex reveals an unappreciated pathway for B cell modulation by Fc-attenuated IgG.Science advances · 2026Article
- Structure-Function Analysis of the FCRL5-IgG1 Fc Complex Reveals an Unappreciated Effect of Fc-Silent Antibodies on B cells.bioRxiv : the preprint server for biology · 2026Article
- Improved protein binder design using β-pairing targeted RFdiffusion.Nature communications · 2026Article
- Human FcRL5 is an Fc receptor that simultaneously engages two IgGs.Science advances · 2026Article
- Comprehensive immune profiling of human peripheral blood mononuclear cells using two complementary spectral flow cytometry panels encompassing 60 unique markers.Frontiers in immunology · 2026Article
- High FCRL5 expression predicts poor treatment response and survival in newly diagnosed multiple myeloma: a retrospective study.Frontiers in oncology · 2026Article
- Antibody-Drug Conjugates, T-Cell Engager Bispecific Antibodies and Chimeric Antigen Receptor T Cells for Multiple Myeloma: What's the Current Status?Targeted oncology · 2026Review
- FCRL5, a B-Cell Marker With Novel Diagnostic and Prognostic Value for Multiple Sclerosis.Neurology(R) neuroimmunology & neuroinflammation · 2025Article
- CAR-T cell therapy in Multiple Myeloma: current status and future challenges.Blood cancer journal · 2024Review
- Review
- Expression quantitative trait loci analysis in rheumatoid arthritis identifies tissue specific variants associated with severity and outcome.Annals of the rheumatic diseases · 2024Article
- The unique properties of IgG4 and its roles in health and disease.Nature reviews. Immunology · 2023Review
- T-cell redirecting bispecific antibodies in multiple myeloma: Current landscape and future directions.EJHaem · 2023Review
- Bispecific Antibodies in Multiple Myeloma: Opportunities to Enhance Efficacy and Improve Safety.Cancers · 2023Review
- Evidence for Extensive Duplication and Subfunctionalization ofInternational journal of molecular sciences · 2023Article
- FCRL1 immunoregulation in B cell development and malignancy.Frontiers in immunology · 2023Review
- Impact of structural modifications of IgG antibodies on effector functions.Frontiers in immunology · 2023Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.