Abstract
Cells infected with feline leukemia virus (FeLV) shed viral antigens into cell culture fluids. Immunoprecipitation and SDS-PAGE analyses of radiolabeled antigens show that the major virus-specific protein released is a molecule of 40,000 molecular weight which carries gag gene product antigenic determinants. The 40,000 molecular weight (40K) protein was found to be glycosylated and was precipitable with antisera to FeLV gag proteins p27, p12, and pl0 but not p15. Tryptic peptide mapping confirmed the relatedness of FeLV p27 and the 40K glycosylated protein, which was found to be released from all FeLV-infected cells, including untransformed embryonic fibroblasts and transformed lymphoblastoid cells. These results suggest that the FeLV gag gene proteins, like those of murine leukemia viruses, can be processed in two distinct pathways and that this is independent of cell type.
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