Myristic acid is coupled to a structural protein of polyoma virus and SV40

C. H. Streuli, B. E. Griffin

    Research output: Contribution to journalArticlepeer-review

    Abstract

    In the lytic cycle of papova viruses, both uncoating of the viral genome after infection and assembly of functional virions take place in the cell nucleus. The mechanisms by which newly internalized virions are targeted to the nucleus and viral DNA encapsidated into particles are poorly understood. Although the major capsid protein VP1 is involved in endocytosis, and largely defines virion structure, the functions of the minor proteins VP2 and VP3 have remained obscure. Here we show that VP2 from both polyoma virus and simian virus 40 (SV40) is covalently linked to myristic acid; this is the first report of a myristylated protein in the nucleus and of a fatty acid being important in the structure of a non-enveloped virus. We consider the implications of this unusual modification on encapsidation and suggest that VP2 may be a scaffolding protein for virion assembly.
    Original languageEnglish
    Pages (from-to)619-622
    Number of pages3
    JournalNature
    Volume326
    Issue number6113
    Publication statusPublished - 1987

    Keywords

    • Amino Acid Sequence
    • Myristic Acid
    • Myristic Acids/analysis/*metabolism
    • Polyomavirus/*analysis
    • Simian virus 40/*analysis
    • Support, Non-U.S. Gov't
    • Viral Proteins/*analysis/metabolism/physiology
    • Viral Structural Proteins

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