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Anti-Idiotypic Antibodies Mimicking Glycoprotein D of Herpes Simplex Virus Identify a Cellular Protein Required for Virus Spread from Cell to Cell and Virus-Induced Polykaryocytosis
Tianmin Huang and Gabriella Campadelli-Fiume
Proceedings of the National Academy of Sciences of the United States of America
Vol. 93, No. 5 (Mar. 5, 1996), pp. 1836-1840
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/38424
Page Count: 5
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Glycoprotein D (gD) of herpes simplex virus 1 (HSV-1) is required for stable attachment and penetration of the virus into susceptible cells after initial binding. We derived anti-idiotypic antibodies to the neutralizing monoclonal antibody HD1 to gD of HSV-1. These antibodies have the properties expected of antibodies against a gD receptor. Specifically, they bind to the surface of HEp-2, Vero, and HeLa cells susceptible to HSV infection and specifically react with a Mr 62,000 protein in these and other (143TK- and BHK) cell lines. They neutralize virion infectivity, drastically decrease plaque formation by impairing cell-to-cell spread of virions, and reduce polykaryocytosis induced by strain HFEM, which carries a syncytial (syn-) mutation. They do not affect HSV growth in a single-step cycle and plaque formation by an unrelated virus, indicating that they specifically affect the interaction of HSV gD with a cell surface receptor. We conclude that the Mr 62,000 cell surface protein interacts with gD to enable spread of HSV-1 from cell to cell and virus-induced polykaryocytosis.
Proceedings of the National Academy of Sciences of the United States of America © 1996 National Academy of Sciences