2I69

Crystal structure of the West Nile virus envelope glycoprotein

Summary for 2I69

• Entry DOI: 10.2210/pdb2i69/pdb
• Descriptor: Polyprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: viral membrane fusion protein, receptor binding, antibody epitope, igc, beta sandwich, glycoprotein, viral protein
• Biological source: West Nile virus
• Total number of polymer chains: 1
• Total formula weight: 44073.85

Authors

Kanai, R.,Modis, Y. (deposition date: 2006-08-28, release date: 2006-11-21, Last modification date: 2024-10-30)

Primary citation

Kanai, R.,Kar, K.,Anthony, K.,Gould, L.H.,Ledizet, M.,Fikrig, E.,Marasco, W.A.,Koski, R.A.,Modis, Y.
Crystal structure of west nile virus envelope glycoprotein reveals viral surface epitopes.
J.Virol., 80:11000-11008, 2006

PubMed Abstract: West Nile virus, a member of the Flavivirus genus, causes fever that can progress to life-threatening encephalitis. The major envelope glycoprotein, E, of these viruses mediates viral attachment and entry by membrane fusion. We have determined the crystal structure of a soluble fragment of West Nile virus E. The structure adopts the same overall fold as that of the E proteins from dengue and tick-borne encephalitis viruses. The conformation of domain II is different from that in other prefusion E structures, however, and resembles the conformation of domain II in postfusion E structures. The epitopes of neutralizing West Nile virus-specific antibodies map to a region of domain III that is exposed on the viral surface and has been implicated in receptor binding. In contrast, we show that certain recombinant therapeutic antibodies, which cross-neutralize West Nile and dengue viruses, bind a peptide from domain I that is exposed only during the membrane fusion transition. By revealing the details of the molecular landscape of the West Nile virus surface, our structure will assist the design of antiviral vaccines and therapeutics.

PubMed: 16943291
DOI: 10.1128/JVI.01735-06

Experimental method

X-RAY DIFFRACTION (3.11 Å)