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; Li Li; Ashley R. Lamb; David W.C. Beasley; Alan D.T. Barrett; David G. Gorenstein

doi:10.1016/j.virol.2007.02.023

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, Li Li, Ashley R. Lamb, David W.C. Beasley, Alan D.T. Barrett, David G. Gorenstein

Research output: Contribution to journal › Article › peer-review

59 Scopus citations

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.

Original language	English (US)
Pages (from-to)	147-154
Number of pages	8
Journal	Virology
Volume	364
Issue number	1
DOIs	https://doi.org/10.1016/j.virol.2007.02.023
State	Published - Jul 20 2007

Keywords

Dengue
Dengue-4 virus
Envelope protein domain III
Flavivirus
Nuclear magnetic resonance
Structure

ASJC Scopus subject areas

Virology

Access to Document

10.1016/j.virol.2007.02.023

Cite this

@article{3a0b86f5005a4f2e937c1aa5dbb59ec9,

title = "Solution structure of the envelope protein domain III of dengue-4 virus",

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.",

keywords = "Dengue, Dengue-4 virus, Envelope protein domain III, Flavivirus, Nuclear magnetic resonance, Structure",

author = "Volk, {David E.} and Lee, {Yi Chien} and Xin Li and Varatharasa Thiviyanathan and Gromowski, {Gregory D.} and Li Li and Lamb, {Ashley R.} and Beasley, {David W.C.} and Barrett, {Alan D.T.} and Gorenstein, {David G.}",

note = "Funding Information: This work was supported by grants U90CCU618754 from the Centers for Disease Control, a grant from the Pediatric Dengue Vaccine Initiative, U01 AI054827 from NIAID, H1296 from the Welch Foundation, P42296LS0000 from the Defense Advanced Research Projects Agency, DAAD17-01-D-0001 from the Defense Threat Reduction Agency, 004952-0038-2003 from the State of Texas Advanced Technology Program, fellowships from the James W. McLaughlin Fellowship Fund to D.W.C.B., and T32 AI 07526 to G.D.G. ",

year = "2007",

month = jul,

day = "20",

doi = "10.1016/j.virol.2007.02.023",

language = "English (US)",

volume = "364",

pages = "147--154",

journal = "Virology",

issn = "0042-6822",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - Solution structure of the envelope protein domain III of dengue-4 virus

AU - Volk, David E.

AU - Lee, Yi Chien

AU - Li, Xin

AU - Thiviyanathan, Varatharasa

AU - Gromowski, Gregory D.

AU - Li, Li

AU - Lamb, Ashley R.

AU - Beasley, David W.C.

AU - Barrett, Alan D.T.

AU - Gorenstein, David G.

N1 - Funding Information: This work was supported by grants U90CCU618754 from the Centers for Disease Control, a grant from the Pediatric Dengue Vaccine Initiative, U01 AI054827 from NIAID, H1296 from the Welch Foundation, P42296LS0000 from the Defense Advanced Research Projects Agency, DAAD17-01-D-0001 from the Defense Threat Reduction Agency, 004952-0038-2003 from the State of Texas Advanced Technology Program, fellowships from the James W. McLaughlin Fellowship Fund to D.W.C.B., and T32 AI 07526 to G.D.G.

PY - 2007/7/20

Y1 - 2007/7/20

N2 - 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.

AB - 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.

KW - Dengue

KW - Dengue-4 virus

KW - Envelope protein domain III

KW - Flavivirus

KW - Nuclear magnetic resonance

KW - Structure

UR - http://www.scopus.com/inward/record.url?scp=34249651385&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34249651385&partnerID=8YFLogxK

U2 - 10.1016/j.virol.2007.02.023

DO - 10.1016/j.virol.2007.02.023

M3 - Article

C2 - 17395234

AN - SCOPUS:34249651385

SN - 0042-6822

VL - 364

SP - 147

EP - 154

JO - Virology

JF - Virology

IS - 1

ER -

Solution structure of the envelope protein domain III of dengue-4 virus

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this