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Protein Eng Des Sel. 2013 Sep;26(9):547-52. doi: 10.1093/protein/gzt034. Epub 2013 Jul 19.

Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide.

Author information

1
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Street 16/10, 117997 Moscow, Russia.

Abstract

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.

KEYWORDS:

acylation; cytoplasmic tail; hemagglutinin; influenza virus; palmitoylation; transmembrane region

PMID:
23873663
DOI:
10.1093/protein/gzt034
[Indexed for MEDLINE]

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