Abstract
Herpes simplex virus type 2-specific glycoproteins present in detergent extracts of infected cells were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under conditions designed to permit detection of multimeric forms of these glycoproteins. Two high-molecular-weight glycosylated species were detected when samples were disrupted at lower temperatures or in the absence of any reducing agents. One multimer having an apparent molecular weight of 275,000 was identified as a multimer of the gA or gB glycoprotein or both. The second glycoprotein, having a molecular weight of approximately 230,000, was identified as a multimeric form of the gC glycoprotein. These data indicate that the gC as well as the gA and gB glycoproteins of herpes simplex virus type 2 may exist in a multimeric form.
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