Abstract
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.