Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III

Shuliu Zhang, Evgeniy I. Bovshik, Rodrigo Maillard, Gregory D. Gromowski, David E. Volk, Catherine H. Schein, Claire Y H Huang, David G. Gorenstein, James Lee, Alan Barrett, David Beasley

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20 Scopus citations

Abstract

Site-directed mutagenesis of residues in the BC loop (residues 329-333) of the envelope (E) protein domain III in a West Nile virus (WNV) infectious clone and in plasmids encoding recombinant WNV and dengue type 2 virus domain III proteins demonstrated a critical role for residues in this loop in the function and antigenicity of the E protein. This included a strict requirement for the tyrosine at residue 329 of WNV for virus viability and E domain III folding. The absence of an equivalent residue in this region of yellow fever group viruses and most tick-borne flavivirus suggests there is an evolutionary divergence in the molecular mechanisms of domain III folding employed by different flaviviruses.

Original languageEnglish (US)
Pages (from-to)85-91
Number of pages7
JournalVirology
Volume403
Issue number1
DOIs
StatePublished - Jul 2010

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Keywords

  • Attenuation
  • Envelope protein
  • Flavivirus
  • Neutralization
  • Receptor binding domain
  • West Nile virus

ASJC Scopus subject areas

  • Virology

Cite this

Zhang, S., Bovshik, E. I., Maillard, R., Gromowski, G. D., Volk, D. E., Schein, C. H., Huang, C. Y. H., Gorenstein, D. G., Lee, J., Barrett, A., & Beasley, D. (2010). Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III. Virology, 403(1), 85-91. https://doi.org/10.1016/j.virol.2010.03.038