Multiple thermolabile and temperature-sensitive lesions in mutant tl17 of vesicular stomatitis virus

The vesicular stomatitis virus thermolabile mutant tl17 contains multiple lesions. The RNA-dependent RNA polymerase is temperature sensitive during primary transcription. The glycoprotein develops Endo H sensitivity more slowly at the nonpermissive temperature. Maturation or incorporation of the glycoprotein into progeny virions is also reduced. When virions of tl17 made at the permissive temperature are incubated in buffered medium at 39 degrees, their glycoprotein is cleaved, resulting in a product that resembles soluble glycoprotein. Compared to another glycoprotein mutant, ts 045, the glycoprotein of tl17 is only partially degraded to soluble G intracellularly and is more thermolabile. These properties of tl17 make it potentially useful for studies on glycoprotein synthesis, processing, and transport as well as for studies on pseudotype formation and viral maturation.