ArticleImmunology2003
Glycosylation of FcgammaRIII in N163 as mechanism of regulating receptor affinity.
Article in Immunology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Molecular Basis of Core Fucosylation-Dependent Modulation of IgG1 Fc-CD16a Binding.bioRxiv : the preprint server for biology · 2026Article
- Extracellular Metabolites and Natural Killer Cell Antitumor Function: Mechanisms and Therapeutic Strategies.Research (Washington, D.C.) · 2026Review
- Spatial localization of CD16a at the human NK cell ADCC lytic synapse.bioRxiv : the preprint server for biology · 2024Article
- Site-Specific Glycosylation Analysis of Murine and Human Fcγ Receptors Reveals High Heterogeneity at ConservedJournal of proteome research · 2024Article
- The antibody-binding Fc gamma receptor IIIa / CD16a is N-glycosylated with high occupancy at all five sites.Current research in immunology · 2022Article
- Bispecific killer cell engager with high affinity and specificity toward CD16a on NK cells for cancer immunotherapy.Frontiers in immunology · 2022Article
- 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
- Molecular and Functional Characterization of Fcγ Receptor IIIb-Ligand Interaction: Implications for Neutrophil-Mediated Immune Mechanisms in Malaria.Infection and immunity · 2018Article
- Enrichment of high affinity subclasses and glycoforms from serum-derived IgG using FcγRs as affinity ligands.Biotechnology and bioengineering · 2018Article
- Effects of anchor structure and glycosylation of Fcγ receptor III on ligand binding affinity.Molecular biology of the cell · 2016Article
- Natural Killer Cell Receptors and Cytotoxic Activity in Phosphomannomutase 2 Deficiency (PMM2-CDG).PloS one · 2016Article
- CD16 expression on monocytes in healthy individuals but not schistosome-infected patients is positively associated with levels of parasite-specific IgG and IgG1.PLoS neglected tropical diseases · 2014Article
- Fcγ receptor IIIa single-nucleotide polymorphisms and haplotypes affect human IgG binding and are associated with lupus nephritis in African Americans.Arthritis & rheumatology (Hoboken, N.J.) · 2014Article
- Article
- Glycosylation of the sodium channel β4 subunit is developmentally regulated and involves in neuritic degeneration.International journal of biological sciences · 2012Article
- Structural basis for Fc gammaRIIa recognition of human IgG and formation of inflammatory signaling complexes.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
- Ileal Immunoglobulin Binding by the Neonatal Fc Receptor: A Previously Unrecognized Mechanism of Protection in the Neonatal Rat Model of Necrotizing Enterocolitis?The e-journal of neonatology research · 2011Article
- N-glycosylation at the SynCAM (synaptic cell adhesion molecule) immunoglobulin interface modulates synaptic adhesion.The Journal of biological chemistry · 2010Article
- Dramatically reduced surface expression of NK cell receptor KIR2DS3 is attributed to multiple residues throughout the molecule.Genes and immunity · 2009Article
- Analysis and validation of carbohydrate three-dimensional structures.Acta crystallographica. Section D, Biological crystallography · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human FcgammaRIII (CD16) is a low-affinity receptor for immunoglobulin G (IgG). There are two different isoforms of this protein: CD16a (transmembranous, expressed on natural killer cells and on macrophages) and CD16b (glycosylphosphatidylinositol-linked, expressed on neutrophilic granulocytes in two allelic forms NA1 and NA2). Both forms of the protein have a variable glycosylation pattern. The NA1 allele of CD16B has four asparagine (N)-linked glycosylation sites. One of them (N163) is localized in the ligand-binding site of domain II. This site is shared by the NA2 allele and CD16A. To examine the functional role of the glycosylation we mutated the four glycosylation sites of the NA1 allele (N39, N75, N163, N170) into glutamine (Q). HEK293 cells were stably transfected with the single mutants and wild-type CD16 as control. We determined binding of human IgG to transfected cells using immunofluorescence studies with anti-human IgG antibody. Monomeric IgG bound to N163Q transfectants with higher affinity than to other transfectants, showing that glycosylation in N163 influences the affinity of CD16 to its ligand. In addition, preincubation of WT-CD16-transfected cells with Tunicamycin (an inhibitor of N-glycosylation) resulted in an increased binding of monomeric IgG whereas N163Q-CD16-transfected cells remained unaffected. Therefore, glycosylation in N163 is a mechanism of regulating affinity of FcgammaRIII to its ligand IgG.
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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.