Publication Database

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

Bandzählung: 26

Heftzählung: 9

Seiten: 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
14163 Berlin
+49 30 838 51833
virologie@vetmed.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.