Abstract
Several independent isolates of feline sarcoma virus (FeSV) have been described1–3. Such viruses are apparently derived by genetic recombination between feline leukaemia virus (FeLV) genomic RNA and host cellular genetic sequences with transforming potential4. Two FeSV isolates, one originally described by Gardner and the second by Snyder-Theilen, have been shown to encode polyproteins of around 115,000 molecular weight5–8,18,19. Both polyproteins contain FeLV structural components (p15, p12) at their amino terminus in addition to nonstructural carboxyl terminal components encoded by acquired sequences within the FeSV genome. We have previously shown that Gardner FeSV P115 contains multiple sites of phosphorylation within its nonstructural component and possesses an associated protein kinase activity9. In the present study we describe the expression in cells derived from a number of mammalian species, of a highly conserved cellular phosphoprotein with binding affinity for Gardner FeSV P115. This protein, designated P150, exhibits an associated protein kinase activity and is immunologically and structurally distinct from polyproteins encoded by the Gardner or Snyder-Theilen strains of FeSV.
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Reynolds, F., Van de Ven, W. & Stephenson, J. Feline sarcoma virus polyprotein P115 binds a host phosphoprotein in transformed cells. Nature 286, 409–412 (1980). https://doi.org/10.1038/286409a0
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DOI: https://doi.org/10.1038/286409a0
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