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

Keywords

  • Domain III
  • Envelope
  • Flavivirus
  • West nile virus

ASJC Scopus subject areas

  • Virology

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