Transcription inhibition site on the M protein of vesicular stomatitis virus located by marker rescue of mutant tsO23(III) with M-gene expression vectors.
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.
Li
Y
Y
Department of Microbiology, University of Virginia School of Medicine, Charlottesville 22908.
Luo
L Z
LZ
Wagner
R R
RR
D015153:Blotting, Western; D005786:Gene Expression Regulation; D005819:Genetic Markers; D005822:Genetic Vectors; D009154:Mutation; D010641:Phenotype; D010957:Plasmids; D013696:Temperature; D014158:Transcription, Genetic; D014162:Transfection; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics*; D014763:Viral Matrix Proteins / Q000235:genetics*
D005819:Genetic Markers; D014763:Viral Matrix Proteins