2i69
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Revision as of 07:43, 18 November 2007
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Crystal structure of the West Nile virus envelope glycoprotein
Overview
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.
About this Structure
2I69 is a Single protein structure of sequence from West nile virus. Full crystallographic information is available from OCA.
Reference
Crystal structure of west nile virus envelope glycoprotein reveals viral surface epitopes., Kanai R, Kar K, Anthony K, Gould LH, Ledizet M, Fikrig E, Marasco WA, Koski RA, Modis Y, J Virol. 2006 Nov;80(22):11000-8. Epub 2006 Aug 30. PMID:16943291
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