Crystal Structure of the Low-pH Form of the Vesicular Stomatitis Virus Glycoprotein G

American Association for the Advancement of Science (AAAS) - Tập 313 Số 5784 - Trang 187-191 - 2006
Stéphane Roche1,2, Stéphane Bressanelli1,2, F.A. Rey1,3,2, Yves Gaudin1,2
1Institut Fédératif de Recherche 115 - Génomes, Transcriptomes, Protéomes
2Virologie moléculaire et structurale
3Institut Pasteur, Paris

Tóm tắt

The vesicular stomatitis virus has an atypical membrane fusion glycoprotein (G) exhibiting a pH-dependent equilibrium between two forms at the virus surface. Membrane fusion is triggered during the transition from the high- to low-pH form. The structure of G in its low-pH form shows the classic hairpin conformation observed in all other fusion proteins in their postfusion conformation, in spite of a novel fold combining features of fusion proteins from classes I and II. The structure provides a framework for understanding the reversibility of the G conformational change. Unexpectedly, G is homologous to gB of herpesviruses, which raises important questions on viral evolution.

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Tài liệu tham khảo

10.1038/289366a0

10.1038/371037a0

10.1038/nature04322

10.1073/pnas.0503989102

10.1016/S0969-2126(01)00581-0

10.1038/nsb0596-465

10.1016/S1097-2765(00)80159-8

10.1074/jbc.M403760200

10.1038/375291a0

10.1073/pnas.0832193100

10.1016/S0092-8674(01)00303-8

10.1038/nature02165

10.1038/nature02239

10.1038/sj.emboj.7600064

10.1021/bi00457a028

10.1128/jvi.67.3.1365-1372.1993

10.1128/jvi.68.4.2186-2193.1994

10.1128/jvi.69.3.1435-1443.1995

10.1099/0022-1317-80-5-1221

Y. Gaudin, Subcell. Biochem.34, 379 (2000).

10.1006/viro.1996.0092

10.1128/jvi.65.9.4853-4859.1991

10.1083/jcb.105.5.1957

10.1074/jbc.270.29.17575

10.1021/bi9702851

10.1074/jbc.M008753200

10.1006/viro.2002.1429

10.1016/S0092-8674(00)81710-9

10.1016/S0042-6822(03)00146-6

10.1126/science.1126548

10.1093/bioinformatics/16.6.566

10.1016/0042-6822(86)90328-4

Single-letter abbreviations for the amino acid residues are as follows: A Ala; C Cys; D Asp; E Glu; F Phe; G Gly; H His; I Ile; K Lys; L Leu; M Met; N Asn; P Pro; Q Gln; R Arg; S Ser; T Thr; V Val; W Trp; and Y Tyr.

10.1021/bi00166a015

10.1128/jvi.69.9.5528-5534.1995

10.1128/jvi.70.11.7371-7378.1996

10.1128/JVI.79.6.3578-3585.2005

W. Delano the PyMOL Molecular Graphics System (2002).

We thank A. Flamand for her constant support of this project; J. Lepault R. Ruigrok M. Knossow A. Benmansour C. Tuffereau and D. Blondel for helpful discussions at different stages of this work; C. Maheu for virus purification; and S. Harrison and K. Heldwein for sharing information before publication. Data collection was performed in part at the Swiss Light Source Paul Scherrer Institut Villigen Switzerland and at the European Synchrotron Radiation Facility Grenoble France. We gratefully acknowledge the help in data collection of T. Tomizaki (beamline X06SA SLS); C. Petosa (beamline ID14-1 ESRF); and S. Duquerroy F. Ternois and G. Squires. We thank B. Gigant and I. Gallay for the use of rotating anode sources for crystal testing. We acknowledge support from the CNRS and INRA the CNRS program “Physique et Chimie du Vivant ” the INRA Animal Health Department program “Les virus des animaux et leurs interactions avec la cellule ” the Ministère de l'éducation nationale de la recherche et de la technologie (MENRT) program “ACI blanche ” and the Agence National de la Recherche (ANR) program.