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  • Title: Processing of herpes simplex virus-1 glycans in cells defective in glycosyl transferases of the Golgi system: relationship to cell fusion and virion egress.
    Author: Serafini-Cessi F, Dall'Olio F, Scannavini M, Campadelli-Fiume G.
    Journal: Virology; 1983 Nov; 131(1):59-70. PubMed ID: 6316656.
    Abstract:
    We studied herpes simplex virus-1 (HSV-1) glycan structure and the expression of HSV-1 functions regulated by viral glycoproteins in Ric21 cells (P. VISCHER and R. C. HUGHES, Eur. J. Bioch. 117, 275-284, 1981). This is a line of ricin-resistant mutant BHK cells defective in the enzymes of the Golgi system which add terminal sugars to N-linked glycans. Two kinds of alterations were observed in the glycosylation of HSV glycoproteins in Ric21 cells. First, there was a defective processing of complex glycans leading to a reduction of biantennary and triantennary species and an increase of incompletely processed monosialylated oligosaccharides. Second, there was an overall reduction in the accumulation of HSV-1 glycoproteins. We found that (i) the release of herpesvirions from Ric21 cells was markedly lower than that from BHK cells, possibly reflecting reduced terminal sugar addition which, in turn, might affect the intracellular transport of glycoproteins. (ii) HSV-1 (MP)-infected Ric21 cells fused with a low efficiency. Furthermore, polycaryocytosis was reduced or abolished in BHK and in Ric21 cells exposed to neuraminidase, indicating that the presence of sialic acid residues in the cell surface glycans is essential for cells to interact in a fashion that brings cell fusion. (iii) Although capsid assembly was comparable, the rate of accumulation of infectious virus decreased in Ric21 cells. Infectivity of released virions from Ric21 and BHK cells was similar, in agreement with previous studies showing that complex-type glycans do not appear to be required for herpesvirion infectivity. The decrease in infectious HSV-1 yield seems to correlate with overall reduced ability to synthesize glycoproteins.
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