Open AccessDifferences in the Postfusion Conformations of Full-Length and Truncated Class II Fusion Protein E of Tick-Borne Encephalitis Virus
Author(s) -
Karin Stiasny,
Christian Kössl,
Franz X. Heinz
Publication year - 2005
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.79.10.6511-6515.2005
Subject(s) - biology , trimer , flavivirus , fusion protein , virology , tick borne encephalitis virus , fusion , virus , lipid bilayer fusion , microbiology and biotechnology , recombinant dna , encephalitis , genetics , physics , gene , linguistics , dimer , philosophy , nuclear magnetic resonance
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.