Fachbereich Veterinärmedizin



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

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

    Robert-von-Ostertag-Str. 7-13
    Gebäude 35
    14163 Berlin
    +49 30 838 51834

    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.