1. IgG Binding Characteristics of Rhesus Macaque FcγR
- Author
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Rebecca A. Howell, Nana Yaw Osei-Owusu, Andrew R. Crowley, Ying N. Chan, Margaret E. Ackerman, Joshua W. Eckman, Caitlyn H. Linde, Isaac Zentner, Ali Emileh, Joern E. Schmitz, Samantha L. Finstad, Sarah L. Cocklin, Simon Cocklin, Austin W. Boesch, Adam R. Miles, and Galit Alter
- Subjects
0301 basic medicine ,Glycan ,animal diseases ,Immunology ,Receptors, Fc ,Biology ,Article ,03 medical and health sciences ,0302 clinical medicine ,Immunology and Allergy ,Animals ,Humans ,Binding site ,Receptor ,Innate immune system ,Binding Sites ,Genetic Variation ,Translation (biology) ,biology.organism_classification ,Macaca mulatta ,Rhesus macaque ,030104 developmental biology ,IgG binding ,Immunoglobulin G ,biology.protein ,Evolutionary divergence ,030215 immunology - Abstract
Indian rhesus macaques (Macaca mulatta) are routinely used in preclinical studies to evaluate therapeutic Abs and candidate vaccines. The efficacy of these interventions in many cases is known to rely heavily on the ability of Abs to interact with a set of Ab FcγR expressed on innate immune cells. Yet, despite their presumed functional importance, M. mulatta Ab receptors are largely uncharacterized, posing a fundamental limit to ensuring accurate interpretation and translation of results from studies in this model. In this article, we describe the binding characteristics of the most prevalent allotypic variants of M. mulatta FcγR for binding to both human and M. mulatta IgG of varying subclasses. The resulting determination of the affinity, specificity, and glycan sensitivity of these receptors promises to be useful in designing and evaluating studies of candidate vaccines and therapeutic Abs in this key animal model and exposes significant evolutionary divergence between humans and macaques.
- Published
- 2016