ArticleScientific reports2018
Site-specific N-glycosylation analysis of soluble Fcγ receptor IIIb in human serum.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Dynamic inter-glycan interactions regulate site-specific N-glycan maturation in human Fcγ receptor III.Glycobiology · 2026Article
- Restoring protein glycosylation with GlycoShape.Nature methods · 2024Article
- Site-Specific Glycosylation Analysis of Murine and Human Fcγ Receptors Reveals High Heterogeneity at ConservedJournal of proteome research · 2024Article
- Decoding human-macaque interspecies differences in Fc-effector functions: The structural basis for CD16-dependent effector function in Rhesus macaques.Frontiers in immunology · 2022Article
- Site-Specific Glycosylation Mapping of Fc Gamma Receptor IIIb from Neutrophils of Individual Healthy Donors.Analytical chemistry · 2020Article
- Biophysical characterization of dynamic structures of immunoglobulin G.Biophysical reviews · 2020Review
- Monitoring of immunoglobulin N- and O-glycosylation in health and disease.Glycobiology · 2020Review
- Site-specific N-glycan Analysis of Antibody-binding Fc γ Receptors from Primary Human Monocytes.Molecular & cellular proteomics : MCP · 2020Article
- Primary Human Natural Killer Cells Retain Proinflammatory IgG1 at the Cell Surface and Express CD16a Glycoforms with Donor-dependent Variability.Molecular & cellular proteomics : MCP · 2019Article
- Article
- Characterization of Endogenous Human FcγRIII by Mass Spectrometry Reveals Site, Allele and Sequence Specific Glycosylation.Molecular & cellular proteomics : MCP · 2019Article
- Intradomain Interactions in an NMDA Receptor Fragment Mediate N-Glycan Processing and Conformational Sampling.Structure (London, England : 1993) · 2019Article
- Multiple Variables at the Leukocyte Cell Surface Impact Fc γ Receptor-Dependent Mechanisms.Frontiers in immunology · 2019Review
- A single amino acid distorts the Fc γ receptor IIIb/CD16b structure upon binding immunoglobulin G1 and reduces affinity relative to CD16a.The Journal of biological chemistry · 2018Article
- CD16a with oligomannose-typeThe Journal of biological chemistry · 2018Article
- Fc γ receptor IIIa/CD16a processing correlates with the expression of glycan-related genes in human natural killer cells.The Journal of biological chemistryArticle
- Fc γ receptor compositional heterogeneity: Considerations for immunotherapy development.The Journal of biological chemistryReview
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fc-receptors for immunoglobulin G (FcγRs) mediate a variety of effector and regulatory mechanisms in the immune system. N-glycosylation of FcγRs critically affects their functions which is well exemplified by antibody-dependent cell-mediated cytotoxicity (ADCC) and phagocytosis mediated by homologous FcγRIIIa and FcγRIIIb, respectively. Although several reports describe N-glycosylation profiles of recombinant FcγRIII glycoproteins, much remains unknown regarding their native glycoforms. Here we performed site-specific N-glycosylation profiling of a soluble form of FcγRIIIb purified from human serum based on mass spectrometric analysis. Our data indicate a distinct and common tendency of the glycoforms exhibited at each N-glycosylation site between the native and the previously reported recombinant FcγRIII glycoproteins. Among the six N-glycosylation sites of serum soluble FcγRIIIb, Asn45 was shown to be exclusively occupied by high-mannose-type oligosaccharides, whereas the remaining sites were solely modified by the complex-type oligosaccharides with sialic acid and fucose residues. The results of our endogenous FcγRIII glycoform analyses are important for the optimization of therapeutic antibody efficacy.
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