Evidence for a novel polymorphism affecting both N-linked glycosylation and ligand binding of the IgG receptor IIIB (CD16).
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).
Yamamoto
K
K
Department of Periodontology, Faculty of Dentistry, Niigata University, Niigata, Japan.
Sugita
N
N
Kobayashi
T
T
Okuda
K
K
Van De Winkel
J G
JG
Yoshie
H
H
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution / Q000235:genetics; D001483:Base Sequence; D002236:Carbohydrate Conformation; D005260:Female; D006031:Glycosylation; D006579:Heterozygote; D006801:Humans; D008024:Ligands; D008297:Male; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000276:immunology; D010587:Phagocytosis / Q000235:genetics; D011110:Polymorphism, Genetic / Q000276:immunology*; D017452:Receptors, IgG / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*
D008024:Ligands; D017452:Receptors, IgG