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


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.

SUBMITTER: Zhang S 

PROVIDER: S-EPMC2897250 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature

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

Zhang Shuliu S   Bovshik Evgeniy I EI   Maillard Rodrigo R   Gromowski Gregory D GD   Volk David E DE   Schein Catherine H CH   Huang Claire Y-H CY   Gorenstein David G DG   Lee James C JC   Barrett Alan D T AD   Beasley David W C DW  

Virology 20100506 1


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 resid  ...[more]

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