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* Department of Biology, Georgia State University, Atlanta, GA 30303; and
Division of Toxicology and Environmental Medicine, Centers of Disease Control and Prevention, Agency for Toxic Substances and Disease Registry, Atlanta, GA 30341
Nonhuman primates are extremely valuable animal models for a variety of human diseases. However, it is now becoming evident that these models, although widely used, are still uncharacterized. The major role that nonhuman primate species play in AIDS research as well as in the testing of Ab-based therapeutics requires the full characterization of structure and function of their Ab molecules. IgA is the Ab class mostly involved in protection at mucosal surfaces. By binding to its specific Fc receptor CD89, IgA plays additional and poorly understood roles in immunity. Therefore, Ig heavy 
(IGHA) constant (C) genes were cloned and sequenced in four different species (rhesus macaques, pig-tailed macaques, baboons, and sooty mangabeys). Sequence analysis confirmed the high degree of intraspecies polymorphism present in nonhuman primates. Individual animals were either homozygous or heterozygous for IGHA genes. Highly variable hinge regions were shared by animals of different geographic origins and were present in different combinations in heterozygous animals. Therefore, it appears that although highly heterogeneous, hinge sequences are present only in limited numbers in various nonhuman primate populations. A macaque recombinant IgA molecule was generated and used to assess its interaction with a recombinant macaque CD89. Macaque CD89 was able to bind its native ligand as well as human IgA1 and IgA2. Presence of Ag enhanced macaque IgA binding and blocking of macaque CD89 N-glycosylation reduced CD89 expression. Together, our results suggest that, despite the presence of IgA polymorphism, nonhuman primates appear suitable for studies that involve the IgA/CD89 system.
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 the National Institutes of Health AIDS Research and Reference Reagent Program, 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 The findings and conclusions in this report are those of the authors and do not necessarily represent the views of the National Institutes of Health and the Agency for Toxic Substances and Disease Registry.
3 Address correspondence and reprint requests to Dr. Roberta Attanasio, Department of Biology, Georgia Sate University, P.O. Box 4010, Atlanta, GA 30302. E-mail address: rattanasio{at}gsu.edu
4 Abbreviations used in this paper: NHP, nonhuman primate; NIP, 5-iodo-4-hydroxy-3-nitrophenacetyl; MFI, mean fluorescence intensity.
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