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-Structure paper
タイトル | Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. |
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ジャーナル・号・ページ | PLoS Pathog, Vol. 14, Issue 8, Page e1007236, Year 2018 |
掲載日 | 2018年8月13日 |
著者 | Wenfei Song / Miao Gui / Xinquan Wang / Ye Xiang / |
PubMed 要旨 | The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion ...The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding "up" conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment. However, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition. |
リンク | PLoS Pathog / PubMed:30102747 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 - 30.5 Å |
構造データ | EMDB-9583: EMDB-9584: EMDB-9585: EMDB-9586: EMDB-9587: EMDB-9588, PDB-6acc: EMDB-9589, PDB-6acd: EMDB-9591, PDB-6acg: EMDB-9593, PDB-6acj: EMDB-9594, PDB-6ack: EMDB-9595: EMDB-9596: EMDB-9597: EMDB-9598: |
由来 |
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キーワード | VIRAL PROTEIN / SARS-CoV / spike / glycoprotein / Class I fusion protein / membrane fusion / VIRAL PROTEIN/HYDROLASE / VIRAL PROTEIN-HYDROLASE complex |