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J Biol Chem, Vol. 274, Issue 11, 6911-6919, March 12, 1999

Characterization of the Interaction between the Herpes Simplex Virus Type I Fc Receptor and Immunoglobulin G

Tara L. Chapman, Il You^§, Ian M. Joseph^§, Pamela J. Bjorkman^¶, Sherie L. Morrison, and Malini Raghavan^§

From the  Division of Biology 156-29 and the ^¶ Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California 91125, the ^§ Department of Microbiology and Immunology, University of Michigan Medical School Ann Arbor, Michigan 48109, and the  Department of Microbiology, Immunology, and Molecular Genetics, UCLA, Los Angeles, California 90095

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 C_H2-C_H3 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.

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