Distinct conformational states of SARS-CoV-2 spike protein
Distinct conformational states of SARS-CoV-2 spike protein
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DOI：
10.1101/2020.05.16.099317
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发表时间：
2020-09-25
期刊：
影响因子：
56.9
通讯作者：
Chen, Bing
中科院分区：
文献类型：
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作者：
Cai, Yongfei;Zhang, Jun;Chen, Bing
为了控制严重急性呼吸综合征冠状病毒2型（SARS-CoV-2）的流行，迫切需要采取干预策略。三聚体病毒刺突（S）蛋白催化病毒和靶细胞膜之间的融合以引发感染。在这里，我们报告两个冷冻电子显微镜结构来自全长S蛋白的制备，代表其融合前（2.9埃分辨率）和融合后（3.0埃分辨率）的构象，分别。融合后状态的自发转变不依赖于靶细胞。融合前三聚体具有三个受体结合结构域，其被邻近融合肽的区段夹持。融合后的结构是战略性的N-连接的聚糖装饰，这表明可能对宿主免疫反应和恶劣的外部条件的保护作用。这些发现推进了我们对SARS-CoV-2进入的理解，并可能指导疫苗和治疗方法的开发。
Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.