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J Gen Virol 71 (1990), 991-996; DOI 10.1099/0022-1317-71-4-991
© 1990 Society for General Microbiology

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Genetic evidence for multiple functions of the matrix protein of vesicular stomatitis virus

P. Coulon, V. Deutsch, F. Lafay, C. Martinet-Edelist, F. Wyers, R. C. Herman1 and A. Flamand

Laboratoire de Génétique des Virus, CNRS, 91198 Gif-sur-Yvette Cedex, France
and1 Syntex Research, 3401 Hillview Avenue, Palo Alto, California 94304, U.S.A.

TsO82, a spontaneous temperature-sensitive (ts) mutant of vesicular stomatitis virus (VSV) isolated in chick embryo fibroblasts (CEFs), complements the five prototype ts mutants of the virus. The data presented here indicate that the defect in tsO82 is localized in the M gene. The mutation changed a methionine to an arginine at position 51 of the M protein. Only true revertants could be isolated, and their frequency was low, perhaps due to the type of substitution required to return to the wild-type phenotype. TsO82 does not exhibit hypertranscription, in contrast to the data reported for all of the other ts mutants affected in the M protein. Moreover, tsO82 is conditionally ts, since it grows normally in BHK-21 cells at all temperatures. It exhibits no c.p.e. at the non-permissive temperature in CEFs. Our data argue for multiple functions of the M protein of VSV, the domain affected by the tsO82 mutation possibly being implicated both in the shut-off of cellular RNA synthesis, and for the recognition of a cellular factor required for efficient viral RNA synthesis.

Received 9 October 1989; accepted 3 January 1990.


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