Transcription inhibition site on the M protein of vesicular stomatitis virus located by marker rescue of mutant tsO23(III) with M-gene expression vectors.

AUTOR(ES)

Li, Y

RESUMO

The matrix (M) protein of vesicular stomatitis virus serves as an endogenous inhibitor of viral transcription, a function missing or deficient in M proteins of temperature-sensitive (ts) mutants assigned to complementation group III. Previous studies with mutant tsO23(III) and vaccinia virus M-gene expression vectors revealed that the temperature-sensitive phenotype is due to a mutation leading to substitution of phenylalanine for leucine at amino acid III, whereas loss of the major antigenic determinant (epitope 1) of the mutant M protein results from the substitution of glutamic acid for the wild-type amino acid glycine at position 21 (Y. Li, L. Luo, R. M. Snyder, and R. R. Wagner, J. Virol. 62:3729-3737, 1988). We demonstrate here that transcription inhibition activity is restored to rescued tsO23 virus only when the rescuing vaccinia virus recombinant expresses M protein with glycine and not glutamic acid at amino acid 21. These experiments indicate the importance of the conformational integrity of the amino-terminal domain in determining the capacity of the vesicular stomatitis virus M protein to down regulate endogenous transcription.

Documentos Relacionados

• Expression of the M gene of vesicular stomatitis virus cloned in various vaccinia virus vectors.
• Morphological and biochemical characterization of viral particles produced by the tsO45 mutant of vesicular stomatitis virus at restrictive temperature.
• Role of the membrane (M) protein in endogenous inhibition of in vitro transcription by vesicular stomatitis virus.
• Site-specific mutations in vectors that express antigenic and temperature-sensitive phenotypes of the M gene of vesicular stomatitis virus.
• Inhibition of a Vesicular Stomatitis Virus Mutant by Rifampin