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Inhibition of Virus Protein Glycosylation as the Mechanism of the Antiviral Action of Prostaglandin A in Sendai Virus-infected Cells

¹ Institute of Experimental Medicine, C.N.R.
² Department of Experimental Medicine, II University of Rome, Via O. Raimondo, Rome 00173
and³ Center of Virology, Ente Monteverde 00. RR, Rome 00152, Italy

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 [³⁵S]methionine-labelled proteins showed that while the non-glycosylated viral polypeptides (P, NP and M) were normally synthesized in PGA₁-treated cells, the viral glycoproteins HN and F₀ were not detected. Two new polypeptides of M_r respectively 4000 and 1000 lower than the HN and F₀ proteins were instead detected. The results suggest that these new polypeptides are defectively glycosylated forms of HN and F₀. In fact PGA₁ 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 PGA₁ treatment. The results also show that the PGA₁-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 M_r 74K, the synthesis of which was induced by PGA₁, appeared to be a possible mediator of PGA₁ antiviral action.

Keywords: prostaglandins, SV, glycosylation

Received 8 August 1988; accepted 17 November 1988.

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