Processing of Glycoproteins Induced by Herpes Simplex Virus Type 1: Sulphation and Nature of the Oligosaccharide Linkages

Abstract

Using the drug tunicamycin, 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 MW as gC but a more basic isoelectric point) was studied. Synthesis of both glycoproteins was inhibited by the drug, suggesting they contain N-linked oligosaccharides. Evidently, 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 sulfate. This modification occurs late in their maturation. Most inorganic sulfate 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 2 serotypes have been further narrowed and are located between coordinates 0.886 and 0.935.