Chapman, Tara L. and You, Il and Joseph, Ian M. and Bjorkman, Pamela J. and Morrison, Sherie L. and Raghavan, Malini (1999) Characterization of the Interaction between the Herpes Simplex Virus Type I Fc Receptor and Immunoglobulin G. Journal of Biological Chemistry, 274 (11). pp. 6911-6999. ISSN 0021-9258. http://resolver.caltech.edu/CaltechAUTHORS:CHAjbc99
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Herpes simplex virus type I (HSV-1) virions and HSV-1-infected cells bind to human immunoglobulin G (hIgG) via its Fc region. A complex of two surface glycoproteins encoded by HSV-1, gE and gI, is responsible for Fc binding. We have co-expressed soluble truncated forms of gE and gI in Chinese hamster ovary cells. Soluble gE-gI complexes can be purified from transfected cell supernatants using a purification scheme that is based upon the Fc receptor function of gE-gI. Using gel filtration and analytical ultracentrifugation, we determined that soluble gE-gI is a heterodimer composed of one molecule of gE and one molecule of gI and that gE-gI heterodimers bind hIgG with a 1:1 stoichiometry. Biosensor-based studies of the binding of wild type or mutant IgG proteins to soluble gE-gI indicate that histidine 435 at the CH2-CH3 domain interface of IgG is a critical residue for IgG binding to gE-gI. We observe many similarities between the characteristics of IgG binding by gE-gI and by rheumatoid factors and bacterial Fc receptors such as Staphylococcus aureus protein A. These observations support a model for the origin of some rheumatoid factors, in which they represent anti-idiotypic antibodies directed against antibodies to bacterial and viral Fc receptors.
|Additional Information:||Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc. (Received for publication, October 27, 1998) We thank Philip E. Lapinski for doing the cell binding experiments, the flow cytometry core at the University of Michigan for performing the fluorescence-activated cell sorting analyses, the Reproductive Sciences program at the University of Michigan for IgG radiolabeling, Parke-Davis research facility for use of the Biacore for initial characterization of the gE-gI·IgG complex, and the California Institute of Technology Protein/Peptide Micro Analytical Laboratory for protein analysis. We also thank Pak Poon for doing the equilibrium analytical ultracentrifugation experiments. We thank Dr. Oveta J. Fuller and Pak Poon for many helpful discussions. This work was supported by a grant from the American Heart Association (to M. R.), the University of Michigan Multipurpose Arthritis and Musculoskeletal Diseases Center (to M. R.), and a National Defense Science and Engineering Predoctoral Fellowship (to T. L. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.|
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|Deposited On:||23 Jul 2006|
|Last Modified:||26 Dec 2012 08:57|
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