Sulphated glycoproteins induced by herpes simplex virus.

BHK cells infected with strain 17 syn+ (HSV-1) or HG52 (HSC-2) incorporated inorganic sulphate into polypeptides which co-migrated on SDS-polyacrylamide gels with virus-induced glycoproteins. The major sulphated glycoprotein was glycoprotein E. In addition, less-intense sulphated bands co-migrated with glycoprotein D and HSV-1 glycoprotein A/B/C. Sulphate label co-migrating with HSV-2 glycoprotein A/B/C was occasionally observed. We have investigated which sulphated polypeptides are excreted from infected cells. Major ones of apparent mol. wt. 32000, 34000 and 35000 were excreted from cells infected with syn+. In addition, polypeptides which migrated in the vicinity of glycoprotein D were often excreted from cells infected with either 17 syn+ or HG52. The 32K, 34K and 35K polypeptides were antigenically related to glycoprotein D and over 95% of the total amount synthesized was excreted. Analysis of intracellular sulphated polypeptides using intertypic recombinants mapped glycoprotein E to between 0.832 and 0.950 units of the HSV genome.