1887

Abstract

Glycoprotein M (gM) constitutes one of the rare examples of a nonessential glycoprotein conserved throughout all herpesvirus subfamilies. Whereas gM in wild-type pseudorabies virus (PrV) strains carries an M-glycan, gM of the attenuated strain Bartha is not glycosylated due to a point mutation in the -glycosylation motif. Since PrV Bartha lacks glycoproteins E and I and carries a mutated gC, we analysed glycosylation of gM in isogenic PrV glycoprotein deletion mutants. Whereas gM was glycosylated normally in most mutants, two independent gC deletion mutants and a gI mutant expressed a nonglycosylated form of gM. DNA sequence analyses revealed the presence of point mutations in the -glycosylation consensus motif. Surprisingly, mutations in strain Bartha, the two gC- deletion mutants and the gI mutant proved to be different, although all affected the -glycosylation motif. Thus, our data show that different, apparently independent point mutations cause expression of nonglycosylated gM.

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1998-04-01
2022-01-21
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