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Virology. Author manuscript; available in PMC 2008 July 20.
Published in final edited form as:
Virology. 2007 July 20; 364(1): 147–154.
Published online 2007 March 29. doi: 10.1016/j.virol.2007.02.023.
PMCID: PMC1950219
NIHMSID: NIHMS25510
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Solution Structure of the Envelope Protein Domain III of dengue-4 virus
David E. Volk,‡ Yi-Chien Lee,‡ Xin Li,‡ Varatharasa Thiviyanathan,‡ Gregory D. Gromowski,£π¢≈ Li Li,£π¢≈ Ashley R.Lamb,# David W. C. Beasley,Δπ¢≈ Alan D. T. Barrett,£π¢≈ and David G. Gorenstein‡
‡ Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555-1157
Δ Department of Microbiology & Immunology, University of Texas Medical Branch, Galveston, TX 77555-1157
£ Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555-1157
Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555-1157
π Center for Biodefense and Emerging Infectious Diseases, University of Texas Medical Branch, Galveston, TX 77555-1157
¢ Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, TX 77555-1157
≈ Sealy Center for Vaccine Development, University of Texas Medical Branch, Galveston, TX 77555-1157
# School of Natural Sciences, University of Texas at Austin, Austin, TX
Address correspondence to David G. Gorenstein, Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555-1157, Tel. 409-747-6800, Fax. 409-747-6850, E-Mail: dggorens/at/utmb.edu
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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 have 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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