7WSH
Cryo-EM structure of SARS-CoV-2 spike receptor-binding domain in complex with sea lion ACE2
7WSH の概要
| エントリーDOI | 10.2210/pdb7wsh/pdb |
| EMDBエントリー | 32758 |
| 分子名称 | Angiotensin-converting enzyme, Spike protein S1, ZINC ION, ... (4 entities in total) |
| 機能のキーワード | complex, viral protein |
| 由来する生物種 | Mammalia (mammals) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 115169.93 |
| 構造登録者 | |
| 主引用文献 | Li, S.,Yang, R.,Zhang, D.,Han, P.,Xu, Z.,Chen, Q.,Zhao, R.,Zhao, X.,Qu, X.,Zheng, A.,Wang, L.,Li, L.,Hu, Y.,Zhang, R.,Su, C.,Niu, S.,Zhang, Y.,Qi, J.,Liu, K.,Wang, Q.,Gao, G.F. Cross-species recognition and molecular basis of SARS-CoV-2 and SARS-CoV binding to ACE2s of marine animals. Natl Sci Rev, 9:nwac122-nwac122, 2022 Cited by PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has an extremely broad host range that includes hippopotami, which are phylogenetically closely related to whales. The cellular ACE2 receptor is one of the key determinants of the host range. Here, we found that ACE2s from several marine mammals and hippopotami could efficiently bind to the receptor-binding domain (RBD) of both SARS-CoV and SARS-CoV-2 and facilitate the transduction of SARS-CoV and SARS-CoV-2 pseudoviruses into ACE2-expressing cells. We further resolved the cryo-electron microscopy complex structures of the minke whale ACE2 and sea lion ACE2, respectively, bound to the RBDs, revealing that they have similar binding modes to human ACE2 when it comes to the SARS-CoV-2 RBD and SARS-CoV RBD. Our results indicate that marine mammals could potentially be new victims or virus carriers of SARS-CoV-2, which deserves further careful investigation and study. It will provide an early warning for the prospective monitoring of marine mammals. PubMed: 36187898DOI: 10.1093/nsr/nwac122 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.89 Å) |
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