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IgG Fc Receptor III Homologues in Nonhuman Primate Species: Genetic Characterization and Ligand Interactions^1,2

Kenneth A. Rogers^*, Franco Scinicariello and Roberta Attanasio^3,*

^* Department of Biology, Georgia State University, Atlanta, GA 30303; and Division of Toxicology Environmental Medicine, Centers for Disease Control and Prevention, Agency for Toxic Substances and Disease Registry, Atlanta, GA 30341

Ig Fc receptors bind to immune complexes through interactions with the Fc regions of specific Ab subclasses to initiate or inhibit the defense mechanisms of the leukocytes on which they are expressed. The mechanism of action of IgG-based therapeutic molecules, which are routinely evaluated in nonhuman primate models, involves binding to the low-affinity FcRIII (CD16). The premise that IgG/CD16 interactions in nonhuman primates mimic those present in humans has not been evaluated. Therefore, we have identified and characterized CD16 and associated TCR -chain homologues in rhesus macaques, cynomolgus macaques, baboons, and sooty mangabeys. Similar to humans, CD16 expression was detected on a lymphocyte subpopulation, on monocytes, and on neutrophils of sooty mangabeys. However, CD16 was detected only on a lymphocyte subpopulation and on monocytes in macaques and baboons. A nonhuman primate rCD16 generated in HeLa cells interacted with human IgG1 and IgG2. By contrast, human CD16 binds to IgG1 and IgG3. As shown for humans, the mAb 3G8 was able to block IgG binding to nonhuman primate CD16 and inhibition of nonhuman primate CD16 N-glycosylation enhanced IgG binding. Clearly, differences in interaction with IgG subclasses and in cell-type expression should be considered when using these models for in vivo evaluation of therapeutic Abs.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ This work was supported in part by National Institutes of Health Grants RR10755 and RR00165, by the Research Program Enhancement from the Georgia State University Office of Research and Sponsored Programs, and by the Georgia Research Alliance. Support for K.A.R. was provided by the Molecular Basis of Disease program at Georgia State University.

² Disclaimer: The findings and conclusions in this report are those of the author and do not necessarily represent the views of the Agency for Toxic Substances and Disease Registry.

³ Address correspondence and reprint requests to Dr. Roberta Attanasio, Department of Biology, Georgia State University, P.O. Box 4010, Atlanta, GA 30302. E-mail address: rattanasio{at}gsu.edu

⁴ Abbreviations used in this paper: ADCC, Ab-dependent cell-mediated cytotoxicity; MFI, mean fluorescence intensity.

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