Envelope proteins and replication of vesicular stomatitis virus: in vivo effects of RNA+ temperature-sensitive mutations on viral RNA synthesis.

Temperature-sensitive (ts) mutants of vesicular stomatitis virus belonging to complementation groups III and V were investigated for their in vivo RNA synthesis. The sucrose gradient patterns of the RNA species which they produced at nonpermissive temperature (39.2 degrees C) were systematically compared under different experimental conditions: variation of input multiplicity and of time of infection, superinfection with T particles, and temperature shifts.

Temperature-sensitive defect of vesicular stomatitis virus in complementation group II.

The prototype member of the complementation group II temperature-sensitive (ts) mutants of vesicular stomatitis virus, ts II 052, has been investigated. In ts II 052-infected HeLa cells at the restrictive temperature (39.5 degrees C), reduced viral RNA synthesis was observed by comparison with infections conducted at the permissive temperature (30 degrees C).

Transcription and replication of vesicular stomatitis virus: effects of temperature-sensitive mutations in complementation group IV.

Temperature-sensitive (ts) mutants of vesicular stomatitis virus belonging to the RNA(-) complementation group IV were investigated under various conditions to study both their RNA and protein syntheses. In infected cells maintained at 39.2 C, viral RNA species were recovered only in the 13 to 15S region of the gradient in an amount depending on the ts mutant used.

Temperature-sensitive mutants of vesicular stomatitis virus: synthesis of virus-specific proteins.

Viral proteins synthesized in L cells infected with temperature-sensitive (ts) mutants of vesicular stomatitis (VS) virus at permissive (31 C) and nonpermissive (39 C) temperatures were compared by polyacrylamide gel electrophoresis. Mutant ts 5, deficient in synthesis of viral ribonucleic acid (RNA(-)), failed to synthesize any of the five identifiable viral proteins at 39 C. Each of three RNA(+) mutants, representing three separate complementation groups, showed distinctive patterns of viral protein synthesis at nonpermissive temperature.