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.
Copyright 2010 Elsevier Inc. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies, Monoclonal / immunology
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Antibodies, Monoclonal / isolation & purification
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Antibodies, Neutralizing / immunology
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Antibodies, Neutralizing / isolation & purification
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Antibodies, Viral / immunology
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Antibodies, Viral / isolation & purification
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Antigens, Viral / genetics
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Antigens, Viral / immunology
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Antigens, Viral / physiology*
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Chlorocebus aethiops
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Female
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Humans
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Mice
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Microbial Viability
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Neutralization Tests
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Protein Folding
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Protein Structure, Tertiary
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Sequence Alignment
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Vero Cells
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Viral Envelope Proteins / genetics
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Viral Envelope Proteins / immunology
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Viral Envelope Proteins / physiology*
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Virus Attachment*
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West Nile virus / genetics
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West Nile virus / immunology
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West Nile virus / physiology*
Substances
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Antibodies, Monoclonal
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Antibodies, Neutralizing
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Antibodies, Viral
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Antigens, Viral
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Viral Envelope Proteins