Herpesvirus-induced "early" glycoprotein: characterization and possible role in immune cytolysis

Abstract

Glycoprotein GVP-11 (molecular weight, 71,500), induced by bovine herpesvirus type 1, was detected on the external surface of infected cells. It could be categorized as an "early" or "beta" class protein since it was synthesized early in the infectious process and its expression was not dependent upon prior viral DNA replication in the infected cells. Monoclonal antibodies directed against GVP-11 immunoprecipitated that glycoprotein and some low-molecular-weight polypeptides from infected cells labeled with either [35S]methionine or [3H]glucosamine. Immunoprecipitation of extracts from cells surface labeled with 125I yielded an additional 138,000-molecular-weight polypeptide. Tunicamycin- or bromovinyl deoxyuridine-treated infected cells yielded polypeptides that were smaller in size than corresponding glycoproteins in untreated cells. Tunicamycin-sensitive glycosylation appeared to be necessary for the expression of the glycoproteins on the surface of the infected cells. The monoclonal antibodies directed against GVP-11 and serum from an immune cow could participate in antibody- and complement-mediated immunocytolysis of infected cells, and this immunocytolysis could be enhanced by arresting cells in the early phase of viral gene expression by treatment with inhibitors of viral DNA synthesis.