Structure, Function, and Evolution of Coronavirus Spike Proteins.
Structure, Function, and Evolution of Coronavirus Spike Proteins.
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DOI：
10.1146/annurev-virology-110615-042301
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发表时间：
2016-09-29
影响因子：
11.3
通讯作者：
Li F
中科院分区：
文献类型：
--
作者：
Li F
冠状病毒刺突蛋白是介导冠状病毒进入宿主细胞的多功能分子机器。它首先通过其S1亚基与宿主细胞表面的受体结合，然后通过其S2亚基融合病毒和宿主细胞膜。来自不同冠状病毒的S1中的两个结构域识别多种宿主受体，导致病毒附着。刺突蛋白存在于两种结构不同的构象，融合前和融合后。必须触发刺突蛋白从融合前到融合后构象的转变，从而导致膜融合。本文综述了冠状病毒刺突蛋白的结构和功能，说明了两个S1结构域如何识别不同的受体，以及刺突蛋白是如何被调节进行构象转变的。我进一步讨论了这两个关键功能的冠状病毒刺突蛋白，受体识别和膜融合，在其他病毒和宿主细胞的相应功能的背景下的演变。
The coronavirus spike protein is a multifunctional molecular machine that mediates coronavirus entry into host cells. It first binds to a receptor on the host cell surface through its S1 subunit and then fuses viral and host membranes through its S2 subunit. Two domains in S1 from different coronaviruses recognize a variety of host receptors, leading to viral attachment. The spike protein exists in two structurally distinct conformations, prefusion and postfusion. The transition from prefusion to postfusion conformation of the spike protein must be triggered, leading to membrane fusion. This article reviews current knowledge about the structures and functions of coronavirus spike proteins, illustrating how the two S1 domains recognize different receptors and how the spike proteins are regulated to undergo conformational transitions. I further discuss the evolution of these two critical functions of coronavirus spike proteins, receptor recognition and membrane fusion, in the context of the corresponding functions from other viruses and host cells.