1ztx

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Revision as of 07:39, 18 November 2007

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spinqualitylabelsall models 1ztx, resolution 2.500Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

West Nile Virus Envelope Protein DIII in complex with neutralizing E16 antibody Fab

Overview

West Nile virus is a mosquito-borne flavivirus closely related to the, human epidemic-causing dengue, yellow fever and Japanese encephalitis, viruses. In establishing infection these icosahedral viruses undergo, endosomal membrane fusion catalysed by envelope glycoprotein rearrangement, of the putative receptor-binding domain III (DIII) and exposure of the, hydrophobic fusion loop. Humoral immunity has an essential protective, function early in the course of West Nile virus infection. Here, we, investigate the mechanism of neutralization by the E16 monoclonal antibody, that specifically binds DIII. Structurally, the E16 antibody Fab fragment, engages 16 residues positioned on four loops of DIII, a consensus, neutralizing epitope sequence conserved in West Nile virus and distinct in, other flaviviruses. The E16 epitope protrudes from the surface of mature, virions in three distinct environments, and docking studies predict Fab, binding will leave five-fold clustered epitopes exposed. We also show that, E16 inhibits infection primarily at a step after viral attachment, potentially by blocking envelope glycoprotein conformational changes., Collectively, our results suggest that a vaccine strategy targeting the, dominant DIII epitope may elicit safe and effective immune responses, against flaviviral diseases.

About this Structure

1ZTX is a Single protein structure of sequence from Mus musculus and West nile virus. Full crystallographic information is available from OCA.

Reference

Structural basis of West Nile virus neutralization by a therapeutic antibody., Nybakken GE, Oliphant T, Johnson S, Burke S, Diamond MS, Fremont DH, Nature. 2005 Sep 29;437(7059):764-9. PMID:16193056

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