Processing of glycoproteins induced by herpes simplex virus type 1: sulphation and nature of the oligosaccharide linkages.
Using the drug tunicamycin we have investigated the nature of the oligosaccharides on herpes simplex virus type 1 (HSV-1)-induced glycoproteins E and Y (gY is a newly identified glycoprotein which has the same apparent mol. wt. as gC but a more basic isoelectric point). Synthesis of both glycoproteins was inhibited by the drug, suggesting they contain N-linked oligosaccharides. Our finding, combined with the previous results of other workers, suggests that all the major HSV-induced glycoproteins have this type of carbohydrate modification. All of the major HSV-1-induced glycoproteins are modified by addition of inorganic sulphate. This modification occurs late in their maturation. Most inorganic sulphate appears to be attached to N-linked oligosaccharides but some is attached to other parts of glycoprotein E. Using HSV-1/HSV-2 intertypic recombinants, the mapping limits of that part of the glycoprotein E gene coding for differences in mobility between the two serotypes have been further narrowed and are located between coordinates 0.886 and 0.935.
D004591:Electrophoresis, Polyacrylamide Gel; D005814:Genes, Viral; D006023:Glycoproteins / Q000032:analysis / Q000096:biosynthesis*; D009844:Oligosaccharides / Q000032:analysis / Q000378:metabolism*; D011995:Recombination, Genetic; D018139:Simplexvirus / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D013431:Sulfates / Q000032:analysis / Q000378:metabolism*; D014415:Tunicamycin / Q000494:pharmacology; D014764:Viral Proteins / Q000032:analysis / Q000096:biosynthesis*
D006023:Glycoproteins; D009844:Oligosaccharides; D013431:Sulfates; D014764:Viral Proteins; D014415:Tunicamycin