西尼罗河病毒包膜蛋白受体结合域 III 结构、功能和抗原性中 BC 环残基的作用。
Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III.
机构信息
Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
出版信息
Virology. 2010 Jul 20;403(1):85-91. doi: 10.1016/j.virol.2010.03.038. Epub 2010 May 6.
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.
摘要
对西尼罗河病毒（WNV）感染性克隆和编码重组 WNV 和登革热 2 型病毒结构域 III 蛋白的质粒中包膜（E）蛋白结构域 III 的 BC 环（残基 329-333）中的残基进行定点突变，证明该环中的残基在 E 蛋白的功能和抗原性中起关键作用。这包括 WNV 残基 329 处的酪氨酸对病毒活力和 E 结构域 III 折叠的严格要求。黄病毒组病毒和大多数蜱传黄病毒在该区域没有等效的残基，这表明不同黄病毒采用的结构域 III 折叠的分子机制存在进化上的差异。
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