Abstract
An autologous antiserum against simian sarcoma virus-infected nonproducer cells (SSV-NP cells) recognized a SSV transformation-specific glycopeptide (SSV-TrSgp) [ H.-J. Thiel, T. J. Matthews, E. M. Broughton, A. M. Butchko, and D. P. Bolognesi (1981) Virology 112, 642–650]. Gel filtration of this component on a Sephacryl S-200 column indicated an apparent molecular weight at about 200,000 (d). This antigen represented a proteoglycan-like molecule, as evidenced by the size of glycopeptides after Pronase treatment and by incubation with chondroitinases. The antigenicity of the SSV-TrSgp was completely destroyed after exposure to different proteases. On the other hand, incubation with neuraminidase or chondroitinases degraded the molecule to some extent, but did not affect its antigenicity as measured by immunoprecipitation. Trypsin and EDTA treatment of intact pulse-labeled cells, as well as surface iodination, indicated that the SSV-TrSgp represents a cell membrane-associated molecule.
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