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

Autor: Zhang S; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA., Bovshik EI, Maillard R, Gromowski GD, Volk DE, Schein CH, Huang CY, Gorenstein DG, Lee JC, Barrett AD, Beasley DW
Jazyk: angličtina
Zdroj: Virology [Virology] 2010 Jul 20; Vol. 403 (1), pp. 85-91. Date of Electronic Publication: 2010 May 06.
DOI: 10.1016/j.virol.2010.03.038
Abstrakt: 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.)
Databáze: MEDLINE
Externí odkaz: