Plante Jessica A, Torres Maricela, Huang Claire Y-H, Beasley David W C
Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA; Sealy Center for Vaccine Development, University of Texas Medical Branch, Galveston, TX 77555, USA.
Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Virology. 2016 Sep;496:97-105. doi: 10.1016/j.virol.2016.05.024. Epub 2016 Jun 7.
West Nile virus (WNV) is a mosquito-borne flavivirus that causes febrile illness, encephalitis, and occasionally death in humans. The envelope protein is the main component of the WNV virion surface, and domain III of the envelope protein (EIII) is both a putative receptor binding domain and a target of highly specific, potently neutralizing antibodies. Envelope E-332 (E-332) is known to have naturally occurring variation and to be a key determinant of neutralization for anti-EIII antibodies. A panel of viruses containing all possible amino acid substitutions at E-332 was constructed. E-332 was found to be highly tolerant of mutation, and almost all of these changes had large impacts on antigenicity of EIII but only limited effects on growth or virulence phenotypes.
西尼罗河病毒（WNV）是一种由蚊子传播的黄病毒，可导致人类发热性疾病、脑炎，偶尔还会致人死亡。包膜蛋白是WNV病毒粒子表面的主要成分，包膜蛋白的结构域III（EIII）既是假定的受体结合结构域，也是高度特异性、强效中和抗体的靶点。已知包膜E-332（E-332）存在自然变异，并且是抗EIII抗体中和作用的关键决定因素。构建了一组在E-332处包含所有可能氨基酸替代的病毒。发现E-332对突变具有高度耐受性，几乎所有这些变化对EIII的抗原性都有很大影响，但对生长或毒力表型的影响有限。
