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pubmed:abstractText |
Antisera, raised in rats, containing specificities directed against tumor antigen of polyoma virus also react with several proteins present in the plasma membrane of mouse cells infected with the virus. The main component has an apparent molecular weight of 55,000. The appearance of this protein after infection with early temperature-sensitive A mutants was temperature-dependent like tumor antigen itself. Pulse and chase isotope experiments suggest that this protein originates from a precursor, perhaps by cleavage; its production appears to be facilitated by the A mutation. Two other components with apparent molecular weights of 61,000 and 28,000 were also present but were more variable from experiment to experiment. All proteins were absent from the plasma membranes of cells infected with a transformation-defective mutant, NG-18. Up to four virus-specific proteins could be isolated from the plasma membranes of rat, hamster, and mouse cells transformed by the virus. The possible role of the plasma membrane proteins in cell transformation is discussed.
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