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Article

Fc gamma receptor glycosylation modulates the binding of IgG glycoforms: a requirement for stable antibody interactions.

Journal of proteome research - 5 Dec 2014

Hayes Jerrard M, Frostell Asa, Cosgrave Eoin F J, Struwe Weston B, Potter Oscar, Davey Gavin P, Karlsson Robert, Anneren Cecilia, Rudd Pauline M

Abstract excerpt

FcγRs play a critical role in the immune response following recognition of invading particles and tumor associated antigens by circulating antibodies. In the present study we investigated the role of FcγR glycosylation in the IgG interaction and observed a stabilizing role for receptor N-glycans. We performed a complete glycan analysis of the recombinant FcγRs (FcγRIa, FcγRIIa, FcγRIIb, FcγRIIIa(Phe158/Val158),...

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Share to Antibodies, Monoclonal, Murine-Derived
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 25345863
DOI: 10.1021/pr500414q

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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