Short communicationThe DE loop of the domain III of the envelope protein appears to be associated with West Nile virus neutralization
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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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Plasticity of a critical antigenic determinant in the West Nile virus NY99 envelope protein domain III
2016, VirologyCitation Excerpt :Phase I and II clinical trials (ClinicalTrials.gov - NCT00515385 and NCT00927953, respectively) of a humanized version of that antibody, under the product name MGAWN1, have been performed, although the phase II trial was terminated early due to low enrollment (MacroGenics, 2009, 2012) and a path forward to licensure of that product is currently unclear. Previous research using wild-type (WT) WNV strains or neutralization escape mutants has identified a small number of residues in EIII that can be altered to prevent antibody-mediated neutralization with little or no effect on virus growth in cell cultures or virulence in animal models (Beasley and Barrett, 2002; Choi et al., 2007; Li et al., 2005; Nybakken et al., 2005; Oliphant et al., 2005; Volk et al., 2004). Residue 332 (E-332), in particular, appears to be a major antigenic determinant.
Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III
2010, VirologyCitation Excerpt :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).
Progress on the development of therapeutics against West Nile virus
2009, Antiviral ResearchMAVS regulates the quality of the antibody response to West-Nile Virus
2020, PLoS PathogensMosaic RNA phage VLPs carrying domain III of the West Nile virus E protein
2014, Molecular Biotechnology