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    Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide (2013)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Mineev, Konstantin S
    Lyukmanova, Ekaterina N
    Krabben, Ludwig (WE 5)
    Serebryakova, Marina V
    Shulepko, Mikhail A
    Arseniev, Alexander S
    Kordyukova, Larisa V
    Veit, Michael (WE 5)
    Quelle
    Protein engineering, design & selection; 26(9) — S. 547–552
    ISSN: 1741-0134
    Sprache
    Englisch
    Verweise
    DOI: 10.1093/protein/gzt034
    Pubmed: 23873663
    Kontakt
    Institut für Virologie

    Robert-von-Ostertag-Str. 7-13
    Gebäude 35
    14163 Berlin
    Tel. +49 30 838 51833 Fax. +49 30 838 451847
    email:viro@zedat.fu-berlin.de

    Abstract / Zusammenfassung

    Hemagglutinin (HA), the trimeric spike of influenza virus, catalyzes fusion of viral and cellular membranes. We have synthesized the anchoring peptide including the linker, transmembrane region and cytoplasmic tail (HA-TMR-CT) in a cell-free system. Furthermore, to mimic the palmitoylation of three conserved cysteines within the CT, we chemically alkylated HA-TMR-CT using hexadecyl-methanethiosulfonate. While the nuclear magnetic resonance spectroscopy showed pure and refolded peptides, the formation of multiple oligomers of higher order impeded further structural analysis. Circular dichroism spectroscopy of both alkylated and non-alkylated HA-TMR-CT revealed an α-helical secondary structure. No major impact of the fatty acids on the secondary structure was detected.