Article
- The EMBO Journal (2004) 23, 728 - 738
- doi:10.1038/sj.emboj.7600064
Published online: 12 February 2004
Subject Categories:
Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
Stéphane Bressanelli1,2, Karin Stiasny2, Steven L Allison2, Enrico A Stura3, Stéphane Duquerroy1, Julien Lescar1,a, Franz X Heinz2 and Félix A Rey1
- Virologie Moléculaire & Structurale, CNRS UMR 2472/INRA UMR 1157, IFR 115 Gif-sur-Yvette, France
- Institute of Virology, University of Vienna, Vienna, Austria
- Departement d'Ingénierie et d'Etudes des Protéines, CEA Saclay, Gif-sur-Yvette, France
Correspondence to:
Franz X Heinz, Institute of Virology, University of Vienna, Kinderspitalgasse 15, A1095, Vienna, Austria. Tel.: +43 1 40490 79510; Fax: +43 1 40490 9795; E-mail: Franz.X.Heinz@univie.ac.at
Félix A Rey, Virologie Moléculaire & Structurale, CNRS UMR 2472/INRA UMR 1157, Avenue de la Terrasse, Gif-sur-Yvette Cedex, France. Tel.: +33 1 6982 3844; Fax: +33 1 6982 4308; E-mail: mem-vms@gv.cnrs-gif.fr
aPresent address: School of Biological Sciences, Nanyang Technological University, 1 Nanyang Walk, Block 5, Singapore 637616, Singapore
Received 24 October 2003; Accepted 4 December 2003
Abstract
Enveloped viruses enter cells via a membrane fusion reaction driven by conformational changes of specific viral envelope proteins. We report here the structure of the ectodomain of the tick-borne encephalitis virus envelope glycoprotein, E, a prototypical class II fusion protein, in its trimeric low-pH-induced conformation. We show that, in the conformational transition, the three domains of the neutral-pH form are maintained but their relative orientation is altered. Similar to the postfusion class I proteins, the subunits rearrange such that the fusion peptide loops cluster at one end of an elongated molecule and the C-terminal segments, connecting to the viral transmembrane region, run along the sides of the trimer pointing toward the fusion peptide loops. Comparison with the low-pH-induced form of the alphavirus class II fusion protein reveals striking differences at the end of the molecule bearing the fusion peptides, suggesting an important conformational effect of the missing membrane connecting segment.
Keywords:
- emerging viruses,
- envelope glycoproteins,
- enveloped viruses,
- flavivirus,
- membrane fusion,
- structure/function relations
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