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The structural proteins of herpesvirus sylvilagus, a lymphotropic gamma herpesvirus, were analyzed by sodium dodecyl sulfate and two-dimensional polyacrylamide gel electrophoreses. Modification of the proteins by glycosylation and phosphorylation was shown by the incorporation of [14C]glucosamine or 32Pi into material which comigrated with [35S]methionine-labeled proteins. One-dimensional gel electrophoresis resolved four major glycoproteins and four major phosphoproteins. By two-dimensional gel electrophoresis, 9 glycoproteins and 13 phosphoproteins were identified. Four proteins incorporated all three labels, indicating that these structural proteins may be both glycosylated and phosphorylated.

Modification of viral structural proteins of herpesvirus sylvilagus by glycosylation and phosphorylation