期刊
PROTEIN ENGINEERING DESIGN & SELECTION
卷 26, 期 9, 页码 547-552出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzt034
关键词
acylation; cytoplasmic tail; hemagglutinin; influenza virus; transmembrane region; palmitoylation
资金
- Russian Foundation for Basic Research [10-04-91333, 12-04-01695]
- Russian Academy of Sciences
- German Research Foundation (DFG) [Ve 141/10, SFB740 TP C1]
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 -helical secondary structure. No major impact of the fatty acids on the secondary structure was detected.
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