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Distinct conformational states of SARS-CoV-2 spike protein
Intervention strategies are urgently needed to control the SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here we report two cryo-EM structures, derived from a...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7464562/ https://www.ncbi.nlm.nih.gov/pubmed/32694201 http://dx.doi.org/10.1126/science.abd4251 |
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author | Cai, Yongfei Zhang, Jun Xiao, Tianshu Peng, Hanqin Sterling, Sarah M. Walsh, Richard M. Rawson, Shaun Rits-Volloch, Sophia Chen, Bing |
author_facet | Cai, Yongfei Zhang, Jun Xiao, Tianshu Peng, Hanqin Sterling, Sarah M. Walsh, Richard M. Rawson, Shaun Rits-Volloch, Sophia Chen, Bing |
author_sort | Cai, Yongfei |
collection | PubMed |
description | Intervention strategies are urgently needed to control the SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here we report two cryo-EM structures, derived from a preparation of the full-length S protein, representing its prefusion (2.9Å resolution) and postfusion (3.0Å 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 development of vaccines and therapeutics. |
format | Online Article Text |
id | pubmed-7464562 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-74645622020-09-02 Distinct conformational states of SARS-CoV-2 spike protein Cai, Yongfei Zhang, Jun Xiao, Tianshu Peng, Hanqin Sterling, Sarah M. Walsh, Richard M. Rawson, Shaun Rits-Volloch, Sophia Chen, Bing Science Research Articles Intervention strategies are urgently needed to control the SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here we report two cryo-EM structures, derived from a preparation of the full-length S protein, representing its prefusion (2.9Å resolution) and postfusion (3.0Å 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 development of vaccines and therapeutics. American Association for the Advancement of Science 2020-07-21 /pmc/articles/PMC7464562/ /pubmed/32694201 http://dx.doi.org/10.1126/science.abd4251 Text en Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY). http://creativecommons.org/licenses/by/4.0/ https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Research Articles Cai, Yongfei Zhang, Jun Xiao, Tianshu Peng, Hanqin Sterling, Sarah M. Walsh, Richard M. Rawson, Shaun Rits-Volloch, Sophia Chen, Bing Distinct conformational states of SARS-CoV-2 spike protein |
title | Distinct conformational states of SARS-CoV-2 spike protein |
title_full | Distinct conformational states of SARS-CoV-2 spike protein |
title_fullStr | Distinct conformational states of SARS-CoV-2 spike protein |
title_full_unstemmed | Distinct conformational states of SARS-CoV-2 spike protein |
title_short | Distinct conformational states of SARS-CoV-2 spike protein |
title_sort | distinct conformational states of sars-cov-2 spike protein |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7464562/ https://www.ncbi.nlm.nih.gov/pubmed/32694201 http://dx.doi.org/10.1126/science.abd4251 |
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