Crystal Structure of the West Nile Virus Envelope Glycoprotein.
From: Department of Pathology & Immunology, Washington University School of Medicine, Campus Box 8118, 660 South Euclid Avenue, St. Louis, MO 63110-1093, USA.
Journal of virology
- Publish Date: Dec 2006
- ISSN: 0022-538X
- Volume: 80
- Issue: 23
- Pages: 11467-74
- Medium: Print
- Language: English
- Citation (JAMA): Nybakken Grant E, Nelson Christopher A, Chen Beverly R, et al. Crystal Structure of the West Nile Virus Envelope Glycoprotein.. J. Virol. Dec 2006;80:11467-74
Abstract
The envelope glycoprotein (E) of West Nile virus (WNV) undergoes a conformational rearrangement triggered by low pH that results in a class II fusion event required for viral entry. Herein we present the 3.0-A crystal structure of the ectodomain of WNV E, which reveals insights into the flavivirus life cycle. We found that WNV E adopts a three-domain architecture that is shared by the E proteins from dengue and tick-borne encephalitis viruses and forms a rod-shaped configuration similar to that observed in immature flavivirus particles. Interestingly, the single N-linked glycosylation site on WNV E is displaced by a novel alpha-helix, which could potentially alter lectin-mediated attachment. The localization of histidines within the hinge regions of E implicates these residues in pH-induced conformational transitions. Most strikingly, the WNV E ectodomain crystallized as a monomer, in contrast to other flavivirus E proteins, which have crystallized as antiparallel dimers. WNV E assembles in a crystalline lattice of perpendicular molecules, with the fusion loop of one E protein buried in a hydrophobic pocket at the DI-DIII interface of another. Dimeric E proteins pack their fusion loops into analogous pockets at the dimer interface. We speculate that E proteins could pivot around the fusion loop-pocket junction, allowing virion conformational transitions while minimizing fusion loop exposure.
Mesh Headings (Keywords): Animals, Baculoviridae, Cell Line, Viral Envelope Proteins, West Nile virus
Check for Full Text / PubMed Unique Identifier (PMID): 16987985
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