Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3425534 | Virology | 2010 | 7 Pages |
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.
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Authors
Shuliu Zhang, Evgeniy I. Bovshik, Rodrigo Maillard, Gregory D. Gromowski, David E. Volk, Catherine H. Schein, Claire Y.-H. Huang, David G. Gorenstein, James C. Lee, Alan D.T. Barrett, David W.C. Beasley,