Structural comparisons of wild-type and nuclear transport-defective simian virus 40 large tumor antigens

Donald L. Jarvis, Robert E. Lanford, Janet S. Butel

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    19 Scopus citations

    Abstract

    PARA(nT) is a defective SV40-adenovirus 7 hybrid virus which contains the entire early region of the SV40 genome and codes for the synthesis of SV40 large tumor antigen (T-ag). A transport-defective variant of this hybrid, PARA(cT), encodes T-ag that is not transported to the nucleus, but accumulates in the cytoplasm. The structures of T-ags extracted from wild-type (WT) SV40-, PARA(nT)-, and PARA(cT)-infected cells were compared by peptide mapping. All three types of T-ag underwent considerable degradation when extracted using Tris-buffered Nonidet P-40 at pH 8.0. The addition of 200 μM leupeptin to the extraction buffer significantly inhibited this degradation. Comparison of methionine-containing tryptic peptides revealed no differences among the T-ags, suggesting that their primary structures are similar or identical. Phosphopeptide mapping revealed no differences between SV40- and PARA(nT)-encoded T-ags. In contrast, PARA(cT)-encoded T-ag lacked a prominent phosphopeptide that was present in both of the others. The possible relevance of this difference in phosphorylation to the transport defect is discussed.

    Original languageEnglish (US)
    Pages (from-to)168-176
    Number of pages9
    JournalVirology
    Volume134
    Issue number1
    DOIs
    StatePublished - Apr 15 1984

    ASJC Scopus subject areas

    • Virology

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