1887

Abstract

Summary

G16(I) is a temperature-sensitive () mutant of vesicular stomatitis virus, Indiana serotype, which overproduces polyadenylic acid [poly(A)] in an transcription system due to a mutation in the L protein. Others have reported that --adenosylhomocysteine (S-Ado-Hcy) causes wild-type (wt) virus to overproduce poly(A) . The possibility that G16(I) constitutively expresses a property induced by S-Ado-Hcy in the case of wt virus was found not to be so since polyadenylation by the mutant was still sensitive to S-Ado-Hcy. Indeed, S-Ado-Hcy caused G16(I) to overproduce poly(A) to a greater extent than its parental wt virus. The increase in polyadenylation observed in response to saturating levels of S-Ado-Hcy differed for G16(I), for its parental wt virus and for another wt strain. To characterize which viral protein modulated the polyadenylation response to S-Ado-Hcy, purified virions were fractionated and their phenotypes in homologous and heterologous reconstitution assays were examined. The results indicated that the viral L protein modulated the response in all three stocks of virus. These data provide further evidence to suggest that the L protein of vesicular stomatitis virus plays a role in polyadenylation of the viral mRNA.

Keyword(s): L protein , polyadenylation and VSV
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/content/journal/jgv/10.1099/0022-1317-69-10-2555
1988-10-01
2022-10-04
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