Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Cai, Yongfei, Zhang, Jun, Xiao, Tianshu, Peng, Hanqin, Sterling, Sarah M., Walsh, Richard M., Rawson, Shaun, Rits-Volloch, Sophia, Chen, Bing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2020
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
_version_ 1783577394157715456
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
work_keys_str_mv AT caiyongfei distinctconformationalstatesofsarscov2spikeprotein
AT zhangjun distinctconformationalstatesofsarscov2spikeprotein
AT xiaotianshu distinctconformationalstatesofsarscov2spikeprotein
AT penghanqin distinctconformationalstatesofsarscov2spikeprotein
AT sterlingsarahm distinctconformationalstatesofsarscov2spikeprotein
AT walshrichardm distinctconformationalstatesofsarscov2spikeprotein
AT rawsonshaun distinctconformationalstatesofsarscov2spikeprotein
AT ritsvollochsophia distinctconformationalstatesofsarscov2spikeprotein
AT chenbing distinctconformationalstatesofsarscov2spikeprotein