Abstract
The major glycoprotein complex (VP123) of herpes simplex virus type 1 resolved by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis was purified and further fractionated into 2 major and 2 minor components by chromatography of the isolated VP123 region on SDS-hydroxylapatite columns. The 2 major components (gC and gA/gB) were purified free of other polypeptides and used to prepare specific antisera to these glycoproteins. Radioimmune precipitation demonstrated that these antisera were specific for the antigens used in their production. These 2 antisera and an anti-VP123 serum were further characterized by immunoprecipitation, neutralization and membrane immunofluorescence techniques. Both major glycoprotein antigens are expressed on the surface of virions and on the surface of infected cells.

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