Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide

被引：24

作者：

Mineev, Konstantin S. ^{[1
]}

Lyukmanova, Ekaterina N. ^{[1
]}

Krabben, Ludwig ^{[2
]}

Serebryakova, Marina V. ^{[3
]}

Shulepko, Mikhail A. ^{[1
]}

Arseniev, Alexander S. ^{[1
]}

Kordyukova, Larisa V. ^{[3
]}

Veit, Michael ^{[2
]}

机构：

[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia

[2] Free Univ Berlin, Fac Vet, Dept Virol, D-14163 Berlin, Germany

[3] Moscow MV Lomonosov State Univ, Belozersky Inst Physicochem Biol, Moscow 119991, Russia

来源：

PROTEIN ENGINEERING DESIGN & SELECTION | 2013年 / 26卷 / 09期

基金：

俄罗斯基础研究基金会;

关键词：

acylation; cytoplasmic tail; hemagglutinin; influenza virus; transmembrane region; palmitoylation; FUSION PORE FORMATION; TRANSMEMBRANE DOMAIN; CYTOPLASMIC TAIL; RECEPTOR-BINDING; PALMITOYLATION; ACYLATION; CYSTEINE; ASSOCIATION; PROTEINS; RESIDUES;

D O I：

10.1093/protein/gzt034

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：547 / 552

页数：6

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