Fachbereich Veterinärmedizin



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

    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Kordyukova, Larisa V
    Serebryakova, Marina V
    Baratova, Ludmila A
    Veit, Michael
    Journal of virology; 82(18) — S. 9288–9292
    ISSN: 0022-538x
    DOI: 10.1128/JVI.00704-08
    Pubmed: 18596092
    Institut für Immunologie und Molekularbiologie

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    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.