1887

Abstract

SUMMARY

Prostaglandin A (PGA) inhibits Sendai virus replication at doses non-toxic to uninfected cells. In this report, the antiviral action of PGA was found to be associated with specific alterations of viral protein synthesis. SDS–PAGE analysis of [S]methionine-labelled proteins showed that while the non-glycosylated viral polypeptides (P, NP and M) were normally synthesized in PGA-treated cells, the viral glycoproteins HN and F were not detected. Two new polypeptides of respectively 4000 and 1000 lower than the HN and F proteins were instead detected. The results suggest that these new polypeptides are defectively glycosylated forms of HN and F. In fact PGA was found selectively to inhibit glucosamine incorporation into Sendai virus-infected cells, but not in uninfected cells. Moreover, in infected cells the inhibition of glucosamine incorporation appeared to be selective towards viral polypeptides. This effect was not due to a decreased uptake of glucosamine from the cells after PGA treatment. The results also show that the PGA-induced alteration of the HN protein caused a loss of its biological function and prevented the insertion of this protein into the cell membrane, thereby blocking virus maturation. Finally, a polypeptide of 74K, the synthesis of which was induced by PGA, appeared to be a possible mediator of PGA antiviral action.

Keyword(s): glycosylation , prostaglandins and SV
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1989-04-01
2024-11-05
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