Role of the membrane (M) protein in endogenous inhibition of in vitro transcription by vesicular stomatitis virus.

AUTOR(ES)

Carroll, A R

RESUMO

An endogenous transcriptase inhibitor active at high concentrations of vesicular stomatitis (VS) virus was present in trypsinized whole virions but was absent from ribonucleoprotein cores containing only the L, N, and NS proteins. Poly(L-glutamic acid) effectively reversed the transcriptase inhibition. Transcription under noninhibited, inhibited, and poly(L-glutamic acid)-reversed conditions did not appear to greatly affect the nature of the RNA transcription product. The VS virion matrix (M) protein was purified to greater than 98% homogeneity and was found to have an isoelectric point of approximately 9.0. Purified M protein inhibited transcription by ribonucleoprotein cores, an effect that was partially reversed by poly(L-glutamic acid). Two group III temperature-sensitive (ts) mutants of VS virus (tsO23 and ts G31) with lesions in the M protein exhibited little or no endogenous inhibitor activity compared with two wild-type strains and a group V mutant (tsO45) with a lesion in the G protein. The data presented strongly suggest that the virion M protein is responsible for the endogenous inhibition of in vitro RNA synthesis seen at high concentrations of VS virus.

Documentos Relacionados

• In vitro assembly of the nonglycosylated membrane protein (M) of Sendai virus.
• In vitro RNA transcription by the New Jersey serotype of vesicular stomatitis virus. I. Characterization of the mRNA species.
• Role of matrix protein in cytopathogenesis of vesicular stomatitis virus.
• Inhibition by aurintricarboxylic acid and polyethylene sulfonate of RNA transcription of vesicular stomatitis virus.
• Inhibition of cellular DNA synthesis by vesicular stomatitis virus.