Elsevier

Virus Research

Volume 123, Issue 2, February 2007, Pages 216-218
Virus Research

Short communication
The DE loop of the domain III of the envelope protein appears to be associated with West Nile virus neutralization

https://doi.org/10.1016/j.virusres.2006.09.002Get rights and content

Abstract

The envelope (E) protein of WNV plays an important role in the virus neutralization. Using a mAb 5E8, a neutralizing epitope on the domain III of the E of the New York strain of WN virus was characterized. Results from neutralization-escape mutants and site-directed mutagenesis revealed that the 5E8 epitope is a highly conformation dependent epitope consisting of at least residues E330, E332 and E367 on the domain III. Besides known critical neutralizing epitopes E330 and E332, our results indicate that residue E367, a component of DE loop on the domain III, appeared to be associated with neutralization but little with neuroinvasion of the virus, as reported previously (Beasley et al., 2002).

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Acknowledgment

This study was supported by a grant from National Veterinary Research and Quarantine Service, Ministry of Agriculture and Forestry, Republic of Korea.

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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

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    Structural studies have shown that neutralizing antibodies that bind to epitopes in domain III interact with almost the entire exposed surface of the domain (Nybakken et al., 2005; Wu et al., 2003). However, selection of neutralization resistant variants of WNV using anti-domain III antibodies either in vitro (Beasley and Barrett, 2002; Choi et al., 2007) or in vivo (Zhang et al., 2009) has been associated with mutations at only a limited number of residues in the amino terminal strand (K307), BC loop (T330 and T332) and DE loop (A367), suggesting that structural and functional constraints may significantly limit the potential range of domain III surface mutations that would otherwise facilitate neutralization escape. Consistent with this, none of these mutations has been associated with measurable differences for growth in cell cultures or mouse virulence phenotypes compared to the parental wild-type viruses (Beasley and Barrett, 2002; Zhang et al., 2009).

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