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    Site-specific attachment of palmitate or stearate to cytoplasmic versus transmembrane cysteines is a common feature of viral spike proteins (2010)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Kordyukova, Larisa V
    Serebryakova, Marina V
    Baratova, Ludmila A
    Veit, Michael
    Quelle
    Virology; 398(1) — S. 49–56
    ISSN: 0042-6822
    Sprache
    Englisch
    Verweise
    DOI: 10.1016/j.virol.2009.11.039
    Pubmed: 20006369
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    Institut für Immunologie und Molekularbiologie

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    14163 Berlin
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    Abstract / Zusammenfassung

    Many glycoproteins of enveloped viruses are known to be "palmitoylated" at cysteines located either in the transmembrane region or in the cytoplasmic tail. Although it was recognized early on that "palmitoylation" is not specific for this carbon chain, the exact fatty acid composition of S-acylated proteins has been difficult to determine. Advancements in mass-spectrometry (MS) now allow one to quantify the fatty acids linked to single acylation sites. We report that G of Vesicular Stomatitis virus contains palmitate at a cytoplasmic cysteine, whereas F of Newcastle Disease virus and E1 of Semliki Forest virus (SFV) are stoichiometrically acylated with stearate at a transmembrane cysteine. E2 of SFV contains three molecules of palmitate and one molecule of stearate, the latter probably attached to a transmembrane cysteine. Thus, site-specific attachment of palmitate or stearate, previously described only for HA of influenza virus, is a common feature of viral spike proteins.