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DOI | 10.1126/science.abd4251 |
Distinct conformational states of SARS-CoV-2 spike protein | |
Yongfei Cai; Jun Zhang; Tianshu Xiao; Hanqin Peng; Sarah M. Sterling; Richard M. Walsh; Shaun Rawson; Sophia Rits-Volloch; Bing Chen | |
2020-09-25 | |
发表期刊 | Science
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出版年 | 2020 |
英文摘要 | Efforts to protect human cells against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have focused on the trimeric spike (S) protein. Several structures have shown a stabilized ectodomain of the spike in its prefusion conformation. Cai et al. now provide insight into the structural changes in the S protein that result in the fusion of the viral and host cell membranes. They purified full-length S protein and determined cryo–electron microscopy structures of both the prefusion and postfusion conformations. These structures add to our understanding of S protein function and could inform vaccine design. Science , this issue p. [1586][1] 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. [1]: /lookup/doi/10.1126/science.abd4251 |
领域 | 气候变化 ; 资源环境 |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/296499 |
专题 | 气候变化 资源环境科学 |
推荐引用方式 GB/T 7714 | Yongfei Cai,Jun Zhang,Tianshu Xiao,et al. Distinct conformational states of SARS-CoV-2 spike protein[J]. Science,2020. |
APA | Yongfei Cai.,Jun Zhang.,Tianshu Xiao.,Hanqin Peng.,Sarah M. Sterling.,...&Bing Chen.(2020).Distinct conformational states of SARS-CoV-2 spike protein.Science. |
MLA | Yongfei Cai,et al."Distinct conformational states of SARS-CoV-2 spike protein".Science (2020). |
条目包含的文件 | 条目无相关文件。 |
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