学术探索
学术期刊
新闻热点
数据分析
智能评审

Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein

被引：82
作者：
Duquerroy, S
Vigouroux, AN
Rottier, PJM
Rey, FA
Bosch, BJ
机构：
[1] CNRS, INRA, UMR 2472 1157, Lab Virol Mol & Struct, F-91198 Gif Sur Yvette, France
[2] IFR 115, F-91198 Gif Sur Yvette, France
[3] Univ Utrecht, Fac Vet Med, Virol Div, Dept Infect Dis & Immunol, NL-3584 CL Utrecht, Netherlands
[4] Univ Utrecht, Inst Biomembranes, NL-3584 CL Utrecht, Netherlands
来源：
VIROLOGY | 2005年 / 335卷 / 02期
关键词：
SARS; membrane fusion; heptad repeat; spike protein; structure; class I fusion protein; coiled coil; asparagine zipper;
D O I：
10.1016/j.virol.2005.02.022
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 angstrom) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 alpha-helix. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码：276 / 285
页数：10
相关论文
共 25 条
[1]   Buried polar residues in coiled-coil interfaces [J].
Akey, DL ;
Malashkevich, VN ;
Kim, PS .
BIOCHEMISTRY, 2001, 40 (21) :6352-6360
[2]   Structural basis for paramyxovirus-mediated membrane fusion [J].
Baker, KA ;
Dutch, RE ;
Lamb, RA ;
Jardetzky, TS .
MOLECULAR CELL, 1999, 3 (03) :309-319
[3]   Severe acute respiratory syndrome coroavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides [J].
Bosch, BJ ;
Martina, BEE ;
van der Zee, R ;
Lepault, J ;
Haijema, BJ ;
Versluis, C ;
Heck, AJR ;
de Groot, R ;
Osterhaus, ADME ;
Rottier, PJM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (22) :8455-8460
[4]   The coronavirus spike protein is a class I virus fusion protein: Structural and functional characterization of the fusion core complex [J].
Bosch, BJ ;
van der Zee, R ;
de Haan, CAM ;
Rottier, PJM .
JOURNAL OF VIROLOGY, 2003, 77 (16) :8801-8811
[5]   N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA2 subunit to form an N cap that terminates the triple-stranded coiled coil [J].
Chen, J ;
Skehel, JJ ;
Wiley, DC .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (16) :8967-8972
[6]   THE FOURIER TRANSFORM OF A COILED-COIL [J].
CRICK, FHC .
ACTA CRYSTALLOGRAPHICA, 1953, 6 (8-9) :685-689
[7]   EVIDENCE FOR A COILED-COIL STRUCTURE IN THE SPIKE PROTEINS OF CORONAVIRUSES [J].
DEGROOT, RJ ;
LUYTJES, W ;
HORZINEK, MC ;
VANDERZEIJST, BAM ;
SPAAN, WJM ;
LENSTRA, JA .
JOURNAL OF MOLECULAR BIOLOGY, 1987, 196 (04) :963-966
[8]   ASSEMBLY OF CORONAVIRUS SPIKE PROTEIN INTO TRIMERS AND ITS ROLE IN EPITOPE EXPRESSION [J].
DELMAS, B ;
LAUDE, H .
JOURNAL OF VIROLOGY, 1990, 64 (11) :5367-5375
[9]   Retrovirus envelope domain at 1.7 angstrom resolution [J].
Fass, D ;
Harrison, SC ;
Kim, PS .
NATURE STRUCTURAL BIOLOGY, 1996, 3 (05) :465-469
[10]   Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus [J].
Ingallinella, P ;
Bianchi, E ;
Finotto, M ;
Cantoni, G ;
Eckert, DM ;
Supekar, VM ;
Bruckmann, C ;
Carfi, A ;
Pessi, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (23) :8709-8714
123