Characterization of the Major Viral Polypeptide in Cells Transformed by Wild-Type and Temperature-Sensitive Murine Sarcoma Virus

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Abstract
Extracts of Moloney murine sarcoma virus (M-MSV)-transformed rat cells were analyzed by a radioimmunoassay procedure which detects the 30,000-dalton major virus structural polypeptide (p30). With the appropriate choice of antiserum and competing protein, type-specific p30 antigenic determinants of Moloney leukemia virus were detected in extracts of producer and nonproducer M-MSV-transformed cells. The specific antigenic determinants were expressed at permissive and restrictive temperatures in cells transformed by a cold-sensitive M-MSV mutant, suggesting that expression of type-specific p30 antigens is not required for maintenance of the transformed phenotype. In parallel experiments, Rauscher leukemia virus type-specific p30 antigenic determinants were detected in extracts of nonproducer M-MSV-transformed cells superinfected with Rauscher leukemia virus. The intracellular p30 antigen in extracts of wild-type and mutant M-MSV-transformed cells was characterized by Sephadex chromatography and isoelectric focusing. Extracts of M-MSV-transformed cells contained a single peak of p30 antigenic activity with a molecular weight of approximately 30,000 daltons and an isoelectric point of 6.0, suggesting that the polypeptide in cellular extracts was similar in molecular weight and isoelectric point to the corresponding protein isolated from purified Moloney murine sarcoma-leukemia virus.

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