POSTTRANSLATIONAL MODIFICATION OF THE TEGUMENT PROTEINS (VP13 AND VP14) OF HERPES-SIMPLEX VIRUS TYPE-1 BY GLYCOSYLATION AND PHOSPHORYLATION

VP13 and VP14, major tegument proteins of herpes simplex virus type 1 (HSV-1) and the products of the UL47 gene, have been shown by partial proteolytic mapping to have closely related protein sequences. These proteins are phosphorylated in virus-infected cells, but not in preparations of purified virus. They also contain O-linked oligosaccharide units which include beta-1,4-N-acetyl galactosamine residues, as demonstrated by the binding of Dolichos biflorus lectin. This modification was detected only in purified virus and appears to be restricted to VP13/14 and VP22, another HSV-1 tegument protein.