Journal article
Polymorphisms and interspecies differences of the activating and inhibitory FcγRII of Macaca nemestrina influence the binding of human IgG subclasses
HM Trist, PS Tan, BD Wines, PA Ramsland, E Orlowski, J Stubbs, EE Gardiner, GA Pietersz, SJ Kent, I Stratov, DR Burton, PM Hogarth
Journal of Immunology | AMER ASSOC IMMUNOLOGISTS | Published : 2014
Abstract
Little is known of the impact of Fc receptor (FcR) polymorphism in macaques on the binding of human (hu)IgG, and nothing is known of this interaction in the pig-tailed macaque (Macaca nemestrina), which is used in preclinical evaluation of vaccines and therapeutic Abs. We defined the sequence and huIgG binding characteristics of the M. nemestrina activating FcγRIIa (mnFcγRIIa) and inhibitory FcγRIIb (mnFcγRIIb) and predicted their structures using the huIgGFc/huFcγRIIa crystal structure. Large differences were observed in the binding of huIgG by mnFcγRIIa and mnFcγRIIb compared with their human FcR counterparts. MnFcγRIIa has markedly impaired binding of huIgG1 and huIgG2 immune complexes co..
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Grants
Awarded by National Institute of Allergy and Infectious Diseases
Funding Acknowledgements
This work was supported by National Health and Medical Research Council Fellowship and Project Grant 1002270 and Program Grant 510448, as well as by the Victorian Operational Infrastructure Support Program.