A Temperature-sensitive Mutant of Vesicular Stomatitis Virus with Two Abnormal Virus Proteins

Publisher Website
Google Scholar
Abstract
SUMMARY Mutant ts DI is the only member of complementation group D of vesicular stomatitis virus (VSV), New Jersey serotype (Pringle, Duncan & Stevenson, 197I ). At the non-permissive temperature (39 °C) both virus RNA and structural proteins are synthesized in BHK-21 cells infected with this mutant (Wunner & Pringle, I972b ). Comparison of virus particle and intracellular proteins have shown that poly- peptides G and N of ts DI grown at 3I °C, and intracellular proteins at 39 °C, have altered electrophoretic mobilities in I o % SDS-polyacrylamide gel correspond- ing to mol. wt. differences of 35oo and ~ooo respectively, yet viability at the per- missive temperature was unimpaired. The differences were evident by both contin- uous and discontinuous SDS-polyacrylamide gel electrophoresis. Reversion of the ts phenotype to wild type was accompanied by a restoration of normal mobility to polypeptide N, whereas G retained the abnormal mobility of the mutant. Thus the ts phenotype is directly related to the altered mobility of N. The extent of glycosylation of G in mutant ts D1 appeared to be different from that of group C ts mutants and wild type.

This publication has 0 references indexed in Scilit: