tetano
Editor, Senior Moderator
Protein Eng Des Sel. 2013 Jul 19. [Epub ahead of print]
Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide.
Mineev KS, Lyukmanova EN, Krabben L, Serebryakova MV, Shulepko MA, Arseniev AS, Kordyukova LV, Veit M.
Source
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
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23873663
Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide.
Mineev KS, Lyukmanova EN, Krabben L, Serebryakova MV, Shulepko MA, Arseniev AS, Kordyukova LV, Veit M.
Source
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
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/23873663