Biophysical characterization and vector-specific antagonist activity of domain III of the tick-borne flavivirus envelope protein

S. Bhardwaj, M. Holbrook, R. E. Shope, A. D.T. Barrett, S. J. Watowich

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111 Scopus citations


The molecular determinants responsible for flavivirus host cell binding and tissue tropism are largely unknown, although domain III of the envelope protein has been implicated in these functions. We examined the solution properties and antagonist activity of Langat virus domain III. Our results suggest that domain III adopts a stably folded structure that can mediate binding of tick-borne flaviviruses but not mosquito-borne flaviviruses to their target cells. Three clusters of phylogenetically conserved residues are identified that may be responsible for the vector-specific antagonist activity of domain III.

Original languageEnglish (US)
Pages (from-to)4002-4007
Number of pages6
JournalJournal of virology
Issue number8
StatePublished - Apr 10 2001


ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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