Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Chlorocebus aethiops
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Circular Dichroism
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Conserved Sequence
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Encephalitis Viruses, Tick-Borne / drug effects*
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Encephalitis Viruses, Tick-Borne / metabolism
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Flavivirus / drug effects
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Flavivirus / metabolism
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / pharmacology
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Protein Structure, Tertiary
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Receptors, Virus / antagonists & inhibitors*
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Receptors, Virus / metabolism
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Sequence Alignment
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Substrate Specificity
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Vero Cells
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Viral Envelope Proteins / chemistry*
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Viral Envelope Proteins / metabolism
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Viral Envelope Proteins / pharmacology*
Substances
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Peptide Fragments
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Receptors, Virus
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Recombinant Fusion Proteins
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Viral Envelope Proteins
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glycoprotein E, Flavivirus