Sulphated Glycoproteins Induced by Herpes Simplex Virus

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Abstract
Hamster kidney BHK cells infected with strain 17 syn+ herpes simplex virus type 1 (HSV-1) or with strain HG52 herpes simplex virus type 2 (HSV-2) incorporated inorganic sulfate into polypeptides which co-migrated on sodium dodecyl sulfate-polyacrylamide gels with virus-induced glycoproteins. The major sulfated glycoprotein was glycoprotein E. Less-intense sulfated bands co-migrated with glycoprotein D and HSV-1 glycoprotein A/B/C. Sulfate label co-migrating with HSV-2 glycoprotein A/B/C was occasionally observed. Sulfated polypeptides which excreted from infected cells were investigated. Major ones of apparent MW 32,000 (32k), 34K and 35K were excreted from cells infected with 17 syn+. Polypeptides which migrated in the vicinity of glycoprotein D were often excreted from cells infected with 17 syn+ or HG52. The 32K, 34K and 35K polypeptides were antigenically related to glycoprotein D and > 95% of the total amount synthesized was excreted. Analysis of intracellular sulfated polypeptides using intertypic recombinants mapped glycoprotein E to between 0.832 and 0.950 units of the HSV genome.