Intermediate conformations during viral fusion glycoprotein structural transition.
Intermediate conformations during viral fusion glycoprotein structural transition.
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DOI：
10.1016/j.coviro.2013.03.006
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发表时间：
2013-04
影响因子：
5.9
通讯作者：
Gaudin Y
中科院分区：
文献类型：
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作者：
Baquero E;Albertini AA;Vachette P;Lepault J;Bressanelli S;Gaudin Y
迄今为止，已经确定了三类融合糖蛋白。它们的核聚变前态和核聚变后态的结构显示出巨大的构象变化。结构转变过程中的中间结构最近得到了表征。已发表的数据与“前发夹”中间体的存在一致。包膜病毒进入细胞需要病毒和细胞膜的融合，由病毒糖蛋白的构象变化驱动。迄今为止，基于共同的结构元素，已经确定了三种不同类型的病毒融合蛋白。晶体结构提供了这些蛋白质融合前和融合后构象的静态图像，并揭示了分子的戏剧性重组，但过渡途径仍然难以捉摸。在这篇综述中，我们将重点介绍旨在表征构象变化过程中的中间结构的最新数据。所有这些数据都支持发夹前中间体的存在，但其寡聚状态仍然是一个有争议的问题。
Three classes of fusion glycoproteins have been hitherto identified. Structures of their pre-fusion and post-fusion states have revealed a huge conformational change. Intermediate structures during the structural transition have been recently characterized. Published data are consistent with the existence of a ‘pre-hairpin’ intermediate. Entry of enveloped viruses into cells requires the fusion of viral and cellular membranes, driven by conformational changes in viral glycoproteins. Three different classes of viral fusion proteins have been hitherto identified based on common structural elements. Crystal structures have provided static pictures of pre-fusion and post-fusion conformations of these proteins and have revealed the dramatic reorganization of the molecules, but the transition pathway remains elusive. In this review, we will focus on recent data aiming to characterize intermediate structures during the conformational change. All these data support the existence of a pre-hairpin intermediate, but its oligomeric status is still a matter of debate.
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