Structure of yellow fever virus envelope protein domain III

David E. Volk; Fiona J. May; Sai H.A. Gandham; Anjenique Anderson; Jana J. Von Lindern; David W.C. Beasley; Alan D.T. Barrett; David G. Gorenstein

doi:10.1016/j.virol.2009.09.001

Structure of yellow fever virus envelope protein domain III

David E. Volk, Fiona J. May, Sai H.A. Gandham, Anjenique Anderson, Jana J. Von Lindern, David W.C. Beasley, Alan D.T. Barrett, David G. Gorenstein

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27 Scopus citations

Abstract

The structure of recombinant domain III of the envelope protein (rED3) of yellow fever virus (YFV), containing the major neutralization site, was determined using NMR spectroscopy. The amino acid sequence and structure of the YFV-rED3 shows differences from ED3s of other mosquito-borne flaviviruses; in particular, the partially surface-exposed BC loop where methionine-304 and valine-324 were identified as being critical for the structure of the loop. Variations in the structure and surface chemistry of ED3 between flaviviruses affect neutralization sites and may affect host cell receptor interactions and play a role in the observed variations in viral pathogenesis and tissue tropism.

Original language	English (US)
Pages (from-to)	12-18
Number of pages	7
Journal	Virology
Volume	394
Issue number	1
DOIs	https://doi.org/10.1016/j.virol.2009.09.001
State	Published - Nov 10 2009

Keywords

Envelope protein domain III
Flavivirus
Neutralization site
Yellow fever virus

ASJC Scopus subject areas

Virology

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10.1016/j.virol.2009.09.001

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title = "Structure of yellow fever virus envelope protein domain III",

abstract = "The structure of recombinant domain III of the envelope protein (rED3) of yellow fever virus (YFV), containing the major neutralization site, was determined using NMR spectroscopy. The amino acid sequence and structure of the YFV-rED3 shows differences from ED3s of other mosquito-borne flaviviruses; in particular, the partially surface-exposed BC loop where methionine-304 and valine-324 were identified as being critical for the structure of the loop. Variations in the structure and surface chemistry of ED3 between flaviviruses affect neutralization sites and may affect host cell receptor interactions and play a role in the observed variations in viral pathogenesis and tissue tropism.",

keywords = "Envelope protein domain III, Flavivirus, Neutralization site, Yellow fever virus",

author = "Volk, {David E.} and May, {Fiona J.} and Gandham, {Sai H.A.} and Anjenique Anderson and {Von Lindern}, {Jana J.} and Beasley, {David W.C.} and Barrett, {Alan D.T.} and Gorenstein, {David G.}",

note = "Funding Information: This work was supported by the Pediatric Dengue Vaccine Initiative, the Centers for Disease Control ( U90CCU618754 ), the NIAID ( U01 AI054827 ), and the Welch Foundation ( H1296 ). We thank Sean Moran for assistance with the Rice University Varian Inova 600 MHz NMR spectrometer whose Carbon-Enhanced HCN Cold Probe was obtained through the SPRING (Strategic Partnership for Research in Nanotechnology Grant) AFRL (AFOSR) FA9550-04-1-0328 . ",

year = "2009",

month = nov,

day = "10",

doi = "10.1016/j.virol.2009.09.001",

language = "English (US)",

volume = "394",

pages = "12--18",

journal = "Virology",

issn = "0042-6822",

publisher = "Academic Press Inc.",

number = "1",

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T1 - Structure of yellow fever virus envelope protein domain III

AU - Volk, David E.

AU - May, Fiona J.

AU - Gandham, Sai H.A.

AU - Anderson, Anjenique

AU - Von Lindern, Jana J.

AU - Beasley, David W.C.

AU - Barrett, Alan D.T.

AU - Gorenstein, David G.

N1 - Funding Information: This work was supported by the Pediatric Dengue Vaccine Initiative, the Centers for Disease Control ( U90CCU618754 ), the NIAID ( U01 AI054827 ), and the Welch Foundation ( H1296 ). We thank Sean Moran for assistance with the Rice University Varian Inova 600 MHz NMR spectrometer whose Carbon-Enhanced HCN Cold Probe was obtained through the SPRING (Strategic Partnership for Research in Nanotechnology Grant) AFRL (AFOSR) FA9550-04-1-0328 .

PY - 2009/11/10

Y1 - 2009/11/10

N2 - The structure of recombinant domain III of the envelope protein (rED3) of yellow fever virus (YFV), containing the major neutralization site, was determined using NMR spectroscopy. The amino acid sequence and structure of the YFV-rED3 shows differences from ED3s of other mosquito-borne flaviviruses; in particular, the partially surface-exposed BC loop where methionine-304 and valine-324 were identified as being critical for the structure of the loop. Variations in the structure and surface chemistry of ED3 between flaviviruses affect neutralization sites and may affect host cell receptor interactions and play a role in the observed variations in viral pathogenesis and tissue tropism.

AB - The structure of recombinant domain III of the envelope protein (rED3) of yellow fever virus (YFV), containing the major neutralization site, was determined using NMR spectroscopy. The amino acid sequence and structure of the YFV-rED3 shows differences from ED3s of other mosquito-borne flaviviruses; in particular, the partially surface-exposed BC loop where methionine-304 and valine-324 were identified as being critical for the structure of the loop. Variations in the structure and surface chemistry of ED3 between flaviviruses affect neutralization sites and may affect host cell receptor interactions and play a role in the observed variations in viral pathogenesis and tissue tropism.

KW - Envelope protein domain III

KW - Flavivirus

KW - Neutralization site

KW - Yellow fever virus

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DO - 10.1016/j.virol.2009.09.001

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AN - SCOPUS:70350128768

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VL - 394

SP - 12

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JO - Virology

JF - Virology

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ER -

Structure of yellow fever virus envelope protein domain III

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Keywords

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