The high-affinity receptor for IgG, FcγRI, of humans and non-human primates
| Autor: | Peck-Szee Tan, Alicia M Chenoweth, P. Mark Hogarth, Halina M. Trist, Bruce D. Wines |
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| Rok vydání: | 2015 |
| Předmět: |
Receptor recycling
Primates Immunology Fc receptor Antibody Affinity Macaque Immunoglobulin G Mice biology.animal Leukocytes Immunology and Allergy Animals Humans Primate Protein Interaction Domains and Motifs Amino Acid Sequence Receptor Peptide sequence Binding Sites biology Receptors IgG Virology biology.protein Signal transduction Protein Binding Signal Transduction |
| Zdroj: | Immunological reviews. 268(1) |
| ISSN: | 1600-065X |
| Popis: | Non-human primate (NHP) models, especially involving macaques, are considered important models of human immunity and have been essential in preclinical testing for vaccines and therapeutics. Despite this, much less characterization of macaque Fc receptors has occurred compared to humans or mice. Much of the characterization of macaque Fc receptors so far has focused on the low-affinity Fc receptors, particularly FcγRIIIa. From these studies, it is clear that there are distinct differences between the human and macaque low-affinity receptors and their interaction with human IgG. Relatively little work has been performed on the high-affinity IgG receptor, FcγRI, especially in NHPs. This review will focus on what is currently known of how FcγRI interacts with IgG, from mutation studies and recent crystallographic studies of human FcγRI, and how amino acid sequence differences in the macaque FcγRI may affect this interaction. Additionally, this review will look at the functional consequences of differences in the amino acid sequences between humans and macaques. |
| Databáze: | OpenAIRE |
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