Plasticity of a critical antigenic determinant in the West Nile virus NY99 envelope protein domain III

Jessica A. Plante, Maricela Torres, Claire Y H Huang, David W C Beasley

Research output: Contribution to journalArticle

Abstract

West Nile virus (WNV) is a mosquito-borne flavivirus that causes febrile illness, encephalitis, and occasionally death in humans. The envelope protein is the main component of the WNV virion surface, and domain III of the envelope protein (EIII) is both a putative receptor binding domain and a target of highly specific, potently neutralizing antibodies. Envelope E-332 (E-332) is known to have naturally occurring variation and to be a key determinant of neutralization for anti-EIII antibodies. A panel of viruses containing all possible amino acid substitutions at E-332 was constructed. E-332 was found to be highly tolerant of mutation, and almost all of these changes had large impacts on antigenicity of EIII but only limited effects on growth or virulence phenotypes.

Original languageEnglish (US)
Pages (from-to)97-105
Number of pages9
JournalVirology
Volume496
DOIs
StatePublished - Sep 1 2016

Fingerprint

Viral Envelope Proteins
West Nile virus
Epitopes
Flavivirus
Encephalitis
Amino Acid Substitution
Neutralizing Antibodies
Culicidae
Virion
Virulence
Anti-Idiotypic Antibodies
Proteins
Fever
Viruses
Phenotype
Mutation
Growth
Protein Domains

Keywords

  • Domain III
  • Envelope
  • Flavivirus
  • West nile virus

ASJC Scopus subject areas

  • Virology

Cite this

Plasticity of a critical antigenic determinant in the West Nile virus NY99 envelope protein domain III. / Plante, Jessica A.; Torres, Maricela; Huang, Claire Y H; Beasley, David W C.

In: Virology, Vol. 496, 01.09.2016, p. 97-105.

Research output: Contribution to journalArticle

Plante, Jessica A. ; Torres, Maricela ; Huang, Claire Y H ; Beasley, David W C. / Plasticity of a critical antigenic determinant in the West Nile virus NY99 envelope protein domain III. In: Virology. 2016 ; Vol. 496. pp. 97-105.
@article{4b284f47343f4d1cabd9102a5ffeba1b,
title = "Plasticity of a critical antigenic determinant in the West Nile virus NY99 envelope protein domain III",
abstract = "West Nile virus (WNV) is a mosquito-borne flavivirus that causes febrile illness, encephalitis, and occasionally death in humans. The envelope protein is the main component of the WNV virion surface, and domain III of the envelope protein (EIII) is both a putative receptor binding domain and a target of highly specific, potently neutralizing antibodies. Envelope E-332 (E-332) is known to have naturally occurring variation and to be a key determinant of neutralization for anti-EIII antibodies. A panel of viruses containing all possible amino acid substitutions at E-332 was constructed. E-332 was found to be highly tolerant of mutation, and almost all of these changes had large impacts on antigenicity of EIII but only limited effects on growth or virulence phenotypes.",
keywords = "Domain III, Envelope, Flavivirus, West nile virus",
author = "Plante, {Jessica A.} and Maricela Torres and Huang, {Claire Y H} and Beasley, {David W C}",
year = "2016",
month = "9",
day = "1",
doi = "10.1016/j.virol.2016.05.024",
language = "English (US)",
volume = "496",
pages = "97--105",
journal = "Virology",
issn = "0042-6822",
publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - Plasticity of a critical antigenic determinant in the West Nile virus NY99 envelope protein domain III

AU - Plante, Jessica A.

AU - Torres, Maricela

AU - Huang, Claire Y H

AU - Beasley, David W C

PY - 2016/9/1

Y1 - 2016/9/1

N2 - West Nile virus (WNV) is a mosquito-borne flavivirus that causes febrile illness, encephalitis, and occasionally death in humans. The envelope protein is the main component of the WNV virion surface, and domain III of the envelope protein (EIII) is both a putative receptor binding domain and a target of highly specific, potently neutralizing antibodies. Envelope E-332 (E-332) is known to have naturally occurring variation and to be a key determinant of neutralization for anti-EIII antibodies. A panel of viruses containing all possible amino acid substitutions at E-332 was constructed. E-332 was found to be highly tolerant of mutation, and almost all of these changes had large impacts on antigenicity of EIII but only limited effects on growth or virulence phenotypes.

AB - West Nile virus (WNV) is a mosquito-borne flavivirus that causes febrile illness, encephalitis, and occasionally death in humans. The envelope protein is the main component of the WNV virion surface, and domain III of the envelope protein (EIII) is both a putative receptor binding domain and a target of highly specific, potently neutralizing antibodies. Envelope E-332 (E-332) is known to have naturally occurring variation and to be a key determinant of neutralization for anti-EIII antibodies. A panel of viruses containing all possible amino acid substitutions at E-332 was constructed. E-332 was found to be highly tolerant of mutation, and almost all of these changes had large impacts on antigenicity of EIII but only limited effects on growth or virulence phenotypes.

KW - Domain III

KW - Envelope

KW - Flavivirus

KW - West nile virus

UR - http://www.scopus.com/inward/record.url?scp=84973137520&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84973137520&partnerID=8YFLogxK

U2 - 10.1016/j.virol.2016.05.024

DO - 10.1016/j.virol.2016.05.024

M3 - Article

VL - 496

SP - 97

EP - 105

JO - Virology

JF - Virology

SN - 0042-6822

ER -