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Biophysical Characterization and Vector-Specific Antagonist Activity of Domain III of the Tick-Borne Flavivirus Envelope Protein

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


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

Topics: Structure and Assembly
Publisher: American Society for Microbiology
Year: 2001
DOI identifier: 10.1128/JVI.75.8.4002-4007.2001
OAI identifier: oai:pubmedcentral.nih.gov:114894
Provided by: PubMed Central
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