新城疫病毒 F 蛋白在融合后构象中的结构。
Structure of the Newcastle disease virus F protein in the post-fusion conformation.
机构信息
Howard Hughes Medical Institute, USA.
出版信息
Virology. 2010 Jul 5;402(2):372-9. doi: 10.1016/j.virol.2010.03.050. Epub 2010 May 2.
Abstract
The paramyxovirus F protein is a class I viral membrane fusion protein which undergoes a significant refolding transition during virus entry. Previous studies of the Newcastle disease virus, human parainfluenza virus 3 and parainfluenza virus 5 F proteins revealed differences in the pre- and post-fusion structures. The NDV Queensland (Q) F structure lacked structural elements observed in the other two structures, which are key to the refolding and fusogenic activity of F. Here we present the NDV Australia-Victoria (AV) F protein post-fusion structure and provide EM evidence for its folding to a pre-fusion form. The NDV AV F structure contains heptad repeat elements missing in the previous NDV Q F structure, forming a post-fusion six-helix bundle (6HB) similar to the post-fusion hPIV3 F structure. Electrostatic and temperature factor analysis of the F structures points to regions of these proteins that may be functionally important in their membrane fusion activity.
摘要
副粘病毒 F 蛋白是一类 I 型病毒膜融合蛋白，在病毒进入过程中会发生显著的重折叠转变。先前对新城疫病毒、人副流感病毒 3 和副流感病毒 5 F 蛋白的研究揭示了融合前和融合后结构的差异。NDV Queensland（Q）F 结构缺乏其他两种结构中观察到的结构元素，这些元素是 F 蛋白重折叠和融合活性的关键。在这里，我们展示了 NDV 澳大利亚-维多利亚（AV）F 蛋白的融合后结构，并提供了其折叠为融合前形式的 EM 证据。NDV AV F 结构包含先前 NDV Q F 结构中缺失的七肽重复元件，形成类似于融合后 hPIV3 F 结构的融合后六螺旋束（6HB）。F 结构的静电和温度因子分析指出了这些蛋白质中可能在其膜融合活性中具有功能重要性的区域。
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