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    S acylation of the hemagglutinin of influenza viruses:
    mass spectrometry reveals site-specific attachment of stearic acid to a transmembrane cysteine (2008)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Kordyukova, Larisa V
    Serebryakova, Marina V
    Baratova, Ludmila A
    Veit, Michael (WE 5)
    Quelle
    Journal of virology; 82(18) — S. 9288–9292
    ISSN: 0022-538x
    Sprache
    Englisch
    Verweise
    DOI: 10.1128/JVI.00704-08
    Pubmed: 18596092
    Kontakt
    Institut für Virologie

    Robert-von-Ostertag-Str. 7-13
    Gebäude 35
    14163 Berlin
    +49 30 838 51833
    viro@zedat.fu-berlin.de

    Abstract / Zusammenfassung

    S acylation of cysteines located in the transmembrane and/or cytoplasmic region of influenza virus hemagglutinins (HA) contributes to the membrane fusion and assembly of virions. Our results from using mass spectrometry (MS) show that influenza B virus HA possessing two cytoplasmic cysteines contains palmitate, whereas HA-esterase-fusion glycoprotein of influenza C virus having one transmembrane cysteine is stearoylated. HAs of influenza A virus having one transmembrane and two cytoplasmic cysteines contain both palmitate and stearate. MS analysis of recombinant viruses with deletions of individual cysteines, as well as tandem-MS sequencing, revealed the surprising result that stearate is exclusively attached to the cysteine positioned in the transmembrane region of HA.