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Journal of Virology, March 2004, p. 3178-3183, Vol. 78, No. 6
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.6.3178-3183.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of a Membrane-Associated Trimeric Low-pH-Induced Form of the Class II Viral Fusion Protein E from Tick-Borne Encephalitis Virus and Its Crystallization

Karin Stiasny,1* Stéphane Bressanelli,1,2 Jean Lepault,2 Felix A. Rey,2 and Franz X. Heinz1

Institute of Virology, University of Vienna, A1095 Vienna, Austria,1 Laboratoire de Virologie Moléculaire et Structurale, F91198 Gif-sur-Yvette Cedex, France2

Received 22 August 2003/ Accepted 12 November 2003

The interaction of a dimeric membrane anchor-free form of the envelope protein E (sE dimer) from tick-borne encephalitis virus with liposomes at acidic pH levels leads to its conversion into membrane-inserted sE trimers. Electron microscopy shows that these trimers have their long dimensions along the threefold molecular axis, which is oriented perpendicularly to the plane of the membrane, where the protein inserts via the internal fusion peptide. Liposomes containing sE at their surface display paracrystalline arrays of protein in a closely packing arrangement in which each trimer is surrounded by six others, suggesting cooperativity in the insertion process. sE trimers, solubilized with nonionic detergents, yielded three-dimensional crystals suitable for X-ray diffraction analysis.

* Corresponding author. Mailing address: Institute of Virology, University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria. Phone: 43-1-40490, ext. 79539. Fax: 43-1-40490, ext. 9795. E-mail: karin.stiasny{at}univie.ac.at.

Journal of Virology, March 2004, p. 3178-3183, Vol. 78, No. 6
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.6.3178-3183.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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