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

共 50 条

[31] The influenza virus hemagglutinin: a model protein in the study of membrane fusion
Ramalho-Santos, J
de Lima, MCP
BIOCHIMICA ET BIOPHYSICA ACTA-REVIEWS ON BIOMEMBRANES, 1998, 1376 (01): : 147 - 154
[32] MEMBRANE-FUSION ACTIVITY OF THE INFLUENZA-VIRUS HEMAGGLUTININ
DOMS, RW
GETHING, MJ
HELENIUS, AH
WHITE, JM
JOURNAL OF CELL BIOLOGY, 1983, 97 (05): : A179 - A179
[33] THE ROLE OF INFLUENZA-VIRUS HEMAGGLUTININ IN MEMBRANE-FUSION
WHARTON, SA
MICROBIOLOGICAL SCIENCES, 1987, 4 (04): : 119 - 124
[34] THE STRUCTURE AND FUNCTION OF THE HEMAGGLUTININ MEMBRANE GLYCOPROTEIN OF INFLUENZA-VIRUS
WILEY, DC
SKEHEL, JJ
ANNUAL REVIEW OF BIOCHEMISTRY, 1987, 56 : 365 - 394
[35] Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
Skehel, JJ
Wiley, DC
ANNUAL REVIEW OF BIOCHEMISTRY, 2000, 69 : 531 - 569
[36] Membrane destabilizing activity of influenza virus hemagglutinin-based synthetic peptide: implications of critical glycine residue in fusion peptide
Matsumoto, T
BIOPHYSICAL CHEMISTRY, 1999, 79 (02) : 153 - 162
[37] Hemagglutinin Palmitoylation Contributes to Membrane Curvature in Influenza a Virus Assembly and Membrane Fusion
Chlanda, Petr
Mekhedov, Elena
Waters, Hang
Sodt, Alexander
Blank, Paul S.
Zimmerberg, Joshua
BIOPHYSICAL JOURNAL, 2017, 112 (03) : 80A - 80A
[38] Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin
Xu, Rui
Wilson, Ian A.
JOURNAL OF VIROLOGY, 2011, 85 (10) : 5172 - 5182
[39] STRUCTURAL BASIS OF IMMUNE RECOGNITION OF INFLUENZA-VIRUS HEMAGGLUTININ
WILSON, IA
COX, NJ
ANNUAL REVIEW OF IMMUNOLOGY, 1990, 8 : 737 - +
[40] Structural basis for the divergent evolution of influenza B virus hemagglutinin
Ni, Fengyun
Kondrashkina, Elena
Wang, Qinghua
VIROLOGY, 2013, 446 (1-2) : 112 - 122

← 1 2 3 4 5 →