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    Tissue Antigens. 2001 Apr;57(4):363-6.

    Evidence for a novel polymorphism affecting both N-linked glycosylation and ligand binding of the IgG receptor IIIB (CD16).

    Yamamoto K, Sugita N, Kobayashi T, Okuda K, Van De Winkel JG, Yoshie H.

    Department of Periodontology, Faculty of Dentistry, Niigata University, Niigata, Japan.

    Immunoglobulin G Fc receptor IIIb (FcgammaRIIIb) is constitutively expressed on neutrophils, and has three allelic forms: FcgammaRIIIb-NA1, FcgammaRIIIb-NA2, and FcgammaRIIIb-SH. We identified two Japanese subjects in whom an A to G substitution at nt 221 changes asparagine (N) to serine (S) at amino acid position 45 in the FcgammaRIIIb-NA2 gene. FcgammaRIIIb-NA2-specific monoclonal antibodies (GRM1 and PEN1) did not bind to mutant neutrophils, which lack an N-linked glycosylation site. Furthermore, IgG3-mediated neutrophil phagocytosis by mutant was slightly increased as compared to wild-type donors (Note).

    PMID: 11380948 [PubMed - indexed for MEDLINE]

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