ANTIIDIOTYPIC ANTIBODIES MIMICKING GLYCOPROTEIN-D OF HERPES-SIMPLEX VIRUS IDENTIFY A CELLULAR PROTEIN REQUIRED FOR VIRUS SPREAD FROM CELL-TO-CELL AND VIRUS-INDUCED POLYKARYOCYTOSIS

Glycoprotein D (go) 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 neu tralizing monoclonal antibody HD1 to go of HSV-1. These antibodies hav e the properties expected of antibodies against a go receptor. Specifi cally, they bind to the surface of HEp-2, Vero, and HeLa cells suscept ible to HSV infection and specifically react with a M(r) 62,000 protei n in these and other (143TK(-) and BHK) cell lines. They neutralize vi rion infectivity, drastically decrease plaque formation by impairing c ell-to-cell spread of virions, and reduce polykaryocytosis induced by strain HFEM, which carries a syncytial (syn(-)) mutation. They do not affect HSV growth single-step cycle and plaque formation by an unrelat ed virus, Indicating that they specifically affect the interaction of HSV go with a cell surface receptor. We conclude that the M(r) 62,000 cell surface protein interacts with go to enable spread of HSV-1 from cell to cell and virus-induced polykaryocytosis.