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    Palmitoylation of the Alphacoronavirus TGEV spike protein S is essential for incorporation into virus-like particles but dispensable for S-M interaction (2014)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Gelhaus, Sandra
    Thaa, Bastian
    Eschke, Kathrin (WE 5)
    Veit, Michael (WE 5)
    Schwegmann-Weßels, Christel
    Quelle
    Virology; 464-465 — S. 397–405
    ISSN: 0042-6822
    Sprache
    Englisch
    Verweise
    DOI: 10.1016/j.virol.2014.07.035
    Pubmed: 25113909
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    Abstract / Zusammenfassung

    The spike protein S of coronaviruses contains a highly conserved cytoplasmic cysteine-rich motif adjacent to the transmembrane region. This motif is palmitoylated in the Betacoronaviruses MHV and SARS-CoV. Here, we demonstrate by metabolic labeling with [(3)H]-palmitic acid that the S protein of transmissible gastroenteritis coronavirus (TGEV), an Alphacoronavirus, is palmitoylated as well. This is relevant for TGEV replication as virus growth was compromised by the general palmitoylation inhibitor 2-bromopalmitate. Mutation of individual cysteine clusters in the cysteine-rich motif of S revealed that all cysteines must be replaced to abolish acylation and incorporation of S into virus-like particles (VLP). Conversely, the interaction of S with the M protein, essential for VLP incorporation of S, was not impaired by lack of palmitoylation. Thus, palmitoylation of the S protein of Alphacoronaviruses is dispensable for S-M interaction, but required for the generation of progeny virions.