A naturally occurring mutation in FcyRIIA: a Q to K127 change confers unique IgG binding properties to the R131 allelic form of the receptor

Norris, Cynthia F., Pricop, Luminita, Millard, Sean S., Taylor, Scott M., Surrey, Saul, Schwartz, Elias, Salmon, Jane E. and McKenzie, Steven E. (1998) A naturally occurring mutation in FcyRIIA: a Q to K127 change confers unique IgG binding properties to the R131 allelic form of the receptor. Blood, 91 2: 656-662.

Author Norris, Cynthia F.
Pricop, Luminita
Millard, Sean S.
Taylor, Scott M.
Surrey, Saul
Schwartz, Elias
Salmon, Jane E.
McKenzie, Steven E.
Title A naturally occurring mutation in FcyRIIA: a Q to K127 change confers unique IgG binding properties to the R131 allelic form of the receptor
Formatted title
A naturally occurring mutation in FcγRIIA: a Q to K127 change confers unique IgG binding properties to the R131 allelic form of the receptor
Journal name Blood   Check publisher's open access policy
ISSN 0006-4971
1528-0020
Publication date 1998-01-15
Year available 1998
Sub-type Article (original research)
Open Access Status Not Open Access
Volume 91
Issue 2
Start page 656
End page 662
Total pages 7
Place of publication Washington, DC, United States
Publisher American Society of Hematology
Language eng
Formatted abstract
FcγRIIa is widely expressed on hematopoietic cells. There are two known allelic polymorphic forms of FcγRIIa, FcγRIIaR131 and FcγRIIa-H131, which differ in the amino acid at position 131 in the second Ig-like domain. In contrast to FcγRIIa-R131, FcγRIIa-H131 binds hIgG2 but not mIgG1, and this differential binding has clinical implications for host defense, autoimmune disease, immunohematologic disease, and response to therapeutic monoclonal antibodies. We identified a novel FcγRIIA genotype in a healthy individual homozygous for FcγRIIA R/R131 in whom a C to A substitution at codon 127 changes glutamine (Q) to lysine (K) in one of the two FcγRIIA genes. This individual’s homozygosity for FcγRIIA-R/R131 leads to the prediction that the receptors on her cells would not bind hIgG2. Monocyte and neutrophil phagocytosis of hIgG2-opsonized erythrocytes was significantly higher (P < .05) for cells from this K/Q127, R/R131 individual than for Q/Q127, R/R131 donors. Platelet aggregation stimulated by an mIgG1 anti-CD9 antibody in this individual was significantly different (P < .05) from Q/Q127, H/R131 and Q/Q127, H/H131 donors and similar to Q/Q127, R/R131. Our data show that the K127/R131 receptors have a unique phenotype, binding both hIgG2 and mIgG1. Further functionally significant mutations in human Fcγ receptors and possible novel mechanisms for inherited differences in disease susceptibility should be sought with unbiased screening methods.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Biomedical Sciences Publications
 
Versions
Version Filter Type
Citation counts: Google Scholar Search Google Scholar
Created: Fri, 04 Mar 2016, 10:23:08 EST by Ms Joanne Biles on behalf of School of Biomedical Sciences