Modification of viral structural proteins of herpesvirus sylvilagus by glycosylation and phosphorylation.
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.
D000818:Animals; D006023:Glycoproteins / Q000096:biosynthesis; D006564:Herpesviridae / Q000378:metabolism*; D007526:Isoelectric Point; D008970:Molecular Weight; D010750:Phosphoproteins / Q000096:biosynthesis; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011817:Rabbits / Q000382:microbiology; D014764:Viral Proteins / Q000378:metabolism*
D006023:Glycoproteins; D010750:Phosphoproteins; D014764:Viral Proteins