ArticleJournal of immunology (Baltimore, Md. : 1950)2011
Structural basis for Fc gammaRIIa recognition of human IgG and formation of inflammatory signaling complexes.
Article in Journal of immunology (Baltimore, Md. : 1950), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
86 citing papers in PubMed, 1 synthesis or guideline pooled it, 152 citations in OpenAlex.
- Association ofFrontiers in immunology · 2025Pooled it
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- Human FcRL5 is an Fc receptor that simultaneously engages two IgGs.Science advances · 2026Article
- Exploring glycoform-dependent dynamic modulations in human immunoglobulin G via computational and experimental approaches.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Impact of Monoclonal Antibody Aggregates on Effector Function Characterization.Antibodies (Basel, Switzerland) · 2025Article
- The Crystal Structure of Human IgD-Fc Reveals Unexpected Differences With Other Antibody Isotypes.Proteins · 2025Article
- Fc gamma receptor polymorphisms in antibody therapy: implications for bioassay development to enhance product quality.Antibody therapeutics · 2025Review
- A Comprehensive Review of Fc Gamma Receptors and Their Role in Systemic Lupus Erythematosus.International journal of molecular sciences · 2025Review
- Cross-species analysis of FcγRIIa/b (CD32a/b) polymorphisms at position 131: structural and functional insights into the mechanism of IgG- mediated phagocytosis in human and macaque.Frontiers in immunology · 2025Article
- Fc engineering by monoclonal mammalian cell display for improved affinity and selectivity towards FcγRs.Antibody therapeutics · 2024Article
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- Control of acute myeloid leukemia by a trifunctional NKp46-CD16a-NK cell engager targeting CD123.Nature biotechnology · 2023Article
- HED, a Human-Engineered Domain, Confers a Unique Fc-Binding Activity to Produce a New Class of Humanized Antibody-like Molecules.International journal of molecular sciences · 2023Article
- FcγRI FG-loop functions as a pH sensitive switch for IgG binding and release.Frontiers in immunology · 2023Article
- Function-structure approach reveals novel insights on the interplay of Immunoglobulin G 1 proteoforms and Fc gamma receptor IIa allotypes.Frontiers in immunology · 2023Article
- Article
- Affinity capillary electrophoresis - mass spectrometry permits direct binding assessment of IgG and FcγRIIa in a glycoform-resolved manner.Frontiers in immunology · 2022Article
- Next generation Fc scaffold for multispecific antibodies.iScience · 2021Article
26 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 5 institutions in 1 country.
Funding
Abstract
The interaction of Abs with their specific FcRs is of primary importance in host immune effector systems involved in infection and inflammation, and are the target for immune evasion by pathogens. FcγRIIa is a unique and the most widespread activating FcR in humans that through avid binding of immune complexes potently triggers inflammation. Polymorphisms of FcγRIIa (high responder/low responder [HR/LR]) are linked to susceptibility to infections, autoimmune diseases, and the efficacy of therapeutic Abs. In this article, we define the three-dimensional structure of the complex between the HR (arginine, R134) allele of FcγRIIa (FcγRIIa-HR) and the Fc region of a humanized IgG1 Ab, hu3S193. The structure suggests how the HR/LR polymorphism may influence FcγRIIa interactions with different IgG subclasses and glycoforms. In addition, mutagenesis defined the basis of the epitopes detected by FcR blocking mAbs specific for FcγRIIa (IV.3), FcγRIIb (X63-21), and a pan FcγRII Ab (8.7). The epitopes detected by these Abs are distinct, but all overlap with residues defined by crystallography to contact IgG. Finally, crystal structures of LR (histidine, H134) allele of FcγRIIa and FcγRIIa-HR reveal two distinct receptor dimers that may represent quaternary states on the cell surface. A model is presented whereby a dimer of FcγRIIa-HR binds Ag-Ab complexes in an arrangement that possibly occurs on the cell membrane as part of a larger signaling assembly.
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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.