Mutant D1 is the only member of complementation group D of vesicular stomatitis virus (VSV), New Jersey serotype (Pringle, Duncan & Stevenson, 1971). 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, 1972).

Comparison of virus particle and intracellular proteins have shown that polypeptides G and N of D1 grown at 31 °C, and intracellular proteins at 39 °C, have altered electrophoretic mobilities in 10% SDS-polyacrylamide gel corresponding to mol. wt. differences of 3500 and 1000 respectively, yet viability at the permissive temperature was unimpaired. The differences were evident by both continuous and discontinuous SDS-polyacrylamide gel electrophoresis.

Reversion of the 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 phenotype is directly related to the altered mobility of N.

The extent of glycosylation of G in mutant D1 appeared to be different from that of group C mutants and wild type.


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