In previous reports we have shown that certain nucleoside analogues may be phosphorylated by herpesvirus-specified thymidine kinases, thereby acquiring an ability to act as virus-selective inhibitors of terminal glycosylation. In the present paper we report that the antiviral nucleoside analogue 5-propyl-2′-deoxyuridine induced a pattern of glycosylation inhibition, which resulted in an increased availability of the HSV-1-specified glycoprotein gC-1 for neutralizing antibodies. This effect, which was absent in cells infected with a thymidine kinase-deficient HSV mutant, was correlated with a decrease in the proportion of highly branched N-linked oligosaccharides associated with gC-1.
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