Differences in the postfusion conformations of full-length and truncated class II fusion protein E of tick-borne encephalitis virus.
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.
Stiasny
Karin
K
Institute of Virology, Medical University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria. karin.stiasny@meduniwien.ac.at
Kössl
Christian
C
Heinz
Franz X
FX
D004669:Encephalitis Viruses, Tick-Borne / Q000737:chemistry* / Q000502:physiology; D008958:Models, Molecular; D011487:Protein Conformation; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000378:metabolism*; D014779:Virus Replication
D014759:Viral Envelope Proteins; C065696:glycoprotein E, Flavivirus