| Literature DB >> 35904629 |
Andrew R Crowley1, Simone I Richardson2,3, Marina Tuyishime4, Madeleine Jennewein5, Meredith J Bailey6, Jiwon Lee6, Galit Alter5, Guido Ferrari4, Lynn Morris2,3, Margaret E Ackerman7,8.
Abstract
Heritable polymorphisms within the human IgG locus, collectively termed allotypes, have often been linked by statistical associations, but rarely mechanistically, to a wide range of disease states. One potential explanation for these associations is that IgG allotype alters host cell receptors' affinity for IgG, dampening or enhancing an immune response depending on the nature of the change and the receptors. In this work, a panel of allotypic antibody variants were evaluated using multiplexed, label-free biophysical methods and cell-based functional assays to determine what effect, if any, human IgG polymorphisms have on antibody function. While we observed several differences in FcγR affinity among allotypes, there was little evidence of dramatically altered FcγR-based effector function or antigen recognition activity associated with this aspect of genetic variability.Entities:
Keywords: Allotype; Effector function; Fc receptor; IgG; Immunuglobulin; Polymorphism
Year: 2022 PMID: 35904629 DOI: 10.1007/s00251-022-01272-7
Source DB: PubMed Journal: Immunogenetics ISSN: 0093-7711 Impact factor: 3.330