Solution Structure of the Envelope Protein Domain III of Dengue-4 Virus

Overview

Journal Virology

Specialty Microbiology

Date 2007 Mar 31

PMID 17395234

Citations 31

Authors

David E Volk

Yi-Chien Lee

Xin Li

Varatharasa Thiviyanathan

Gregory D Gromowski

Li Li

Ashley R Lamb

David W C Beasley

Alan D T Barrett

David G Gorenstein

Affiliations

Soon will be listed here.

Abstract

The disease dengue (DEN) is caused by four serologically related viruses termed DEN1, DEN2, DEN3 and DEN4. The structure of the ectodomain of the envelope protein has been determined previously for DEN2 and DEN3 viruses. Using NMR spectroscopic methods, we solved the solution structure of domain III (ED3), the receptor-binding domain, of the envelope protein of DEN4 virus, human strain 703-4. The structure shows that the nine amino acid changes in ED3 that separate the sylvatic and human DEN4 strains are surface exposed. Important structural differences between DEN4-rED3 and ED3 domains of DEN2, DEN3 and other flaviviruses are discussed.

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