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A striking example of convergent evolution observed for the ggFcR:IgY interaction closely resembling that of mammalian FcR:IgG.

Posted by on in 2012
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Schreiner BViertlboeck BCGöbel TW. 2012. Dev Comp Immunol. 36:566-71. doi: 10.1016/j.dci.2011.09.013. Epub 2011 Oct 1.

Institute for Animal Physiology, Department of Veterinary Sciences, University of Munich, Veterinärstrasse 13, 80539 Munich, Germany.

Abstract

We have recently identified a novel IgY specific chicken FcR (ggFcR) on chromosome 20, a region where no FcR gene is present in mammals. Serially deleted IgY fusion proteins were tested in a reporter assay to identify C(H) domains involved in ggFcR binding. Single C(H) domains did not bind to ggFcR, whereas Fcυ2 to Fcυ4 induced good and the Fcυ3 to Fcυ4 domains moderate activity. When IgY from diverse birds were assayed, only IgY from gallinaceous birds showed binding, which enabled us to pinpoint several potential contact sites by a sequence comparison and molecular modelling. Point mutations of critical residues at these sites revealed the Fcυ2 and Fcυ3 domains as major ggFcR:IgY binding sites similar to mammalian IgG. These results demonstrate that ggFcR has a contact site to IgY which closely resembles that of human IgG bound to FcR.

Copyright © 2011 Elsevier Ltd. All rights reserved.

PMID:
21986582
[PubMed - indexed for MEDLINE]
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