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Journal of Virology, May 2005, p. 6511-6515, Vol. 79, No. 10
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.10.6511-6515.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Differences in the Postfusion Conformations of Full-Length and Truncated Class II Fusion Protein E of Tick-Borne Encephalitis Virus

Karin Stiasny,* Christian Kössl, and Franz X. Heinz

Institute of Virology, Medical University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria

Received 9 November 2004/ Accepted 19 January 2005

The trimeric postfusion structure of the C-terminally truncated fusion protein E of the flavivirus tick-borne encephalitis virus, a class II viral fusion protein, was previously determined (S. Bressanelli, K. Stiasny, S. L. Allison, E. A. Stura, S. Duquerroy, J. Lescar, F. X. Heinz, and F. A. Rey, EMBO J. 23:728-738, 2004). In this study we compared the properties of this truncated form with the full-length trimer and found that the so-called stem-anchor region not only confers additional stability to the full-length molecule but also structurally modifies the protein domain carrying the fusion peptide loop. These data provide experimental evidence to support the model of a fusion process that leads to the interaction of the stem-anchor region with the fusion peptide loop in the postfusion trimer.

* Corresponding author. Mailing address: Institute of Virology, Medical 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}meduniwien.ac.at.

Journal of Virology, May 2005, p. 6511-6515, Vol. 79, No. 10
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.10.6511-6515.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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