Open Access
Nature Communications, volume 11, issue 1, publication number 3618
Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein
1
National Laboratory of Biomacromolecules, CAS Center for excellence in biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
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3
Center for Biological Imaging, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
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Publication type: Journal Article
Publication date: 2020-07-17
Journal:
Nature Communications
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 16.6
ISSN: 20411723, 20411723
General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy
Abstract
Global emergencies caused by the severe acute respiratory syndrome coronavirus (SARS-CoV), Middle-East respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV-2 significantly endanger human health. The spike (S) glycoprotein is the key antigen and its conserved S2 subunit contributes to viral entry by mediating host-viral membrane fusion. However, structural information of the post-fusion S2 from these highly pathogenic human-infecting coronaviruses is still lacking. We used single-particle cryo-electron microscopy to show that the post-fusion SARS-CoV S2 forms a further rotated HR1-HR2 six-helix bundle and a tightly bound linker region upstream of the HR2 motif. The structures of pre- and post-fusion SARS-CoV S glycoprotein dramatically differ, resembling that of the Mouse hepatitis virus (MHV) and other class I viral fusion proteins. This structure suggests potential targets for the development of vaccines and therapies against a wide range of SARS-like coronaviruses. The spike (S) protein of coronaviruses is responsible for receptor recognition and the fusion between the viral membrane and the of cell host membrane. Here the authors report a cryo-EM structure of SARS-CoV post-fusion S2 trimer, providing insights into the fusion mechanism that could be useful for therapeutic development against coronaviruses.
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Citations by publishers
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35
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Cold Spring Harbor Laboratory
32 publications, 18.6%
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Elsevier
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1 publication, 0.58%
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Biophysical Society
1 publication, 0.58%
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Oxford University Press
1 publication, 0.58%
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Walter de Gruyter
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Proceedings of the National Academy of Sciences (PNAS)
1 publication, 0.58%
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1 publication, 0.58%
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Bioscientifica
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- We do not take into account publications without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Fan X. et al. Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein // Nature Communications. 2020. Vol. 11. No. 1. 3618
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Fan X., Cao D., Kong L., Zhang X. Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein // Nature Communications. 2020. Vol. 11. No. 1. 3618
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TY - JOUR
DO - 10.1038/s41467-020-17371-6
UR - https://doi.org/10.1038/s41467-020-17371-6
TI - Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein
T2 - Nature Communications
AU - Fan, Xiaoyi
AU - Cao, Duanfang
AU - Kong, Lingfei
AU - Zhang, Xinzheng
PY - 2020
DA - 2020/07/17 00:00:00
PB - Springer Nature
IS - 1
VL - 11
SN - 2041-1723
SN - 2041-1723
ER -
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@article{2020_Fan,
author = {Xiaoyi Fan and Duanfang Cao and Lingfei Kong and Xinzheng Zhang},
title = {Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein},
journal = {Nature Communications},
year = {2020},
volume = {11},
publisher = {Springer Nature},
month = {jul},
url = {https://doi.org/10.1038/s41467-020-17371-6},
number = {1},
doi = {10.1038/s41467-020-17371-6}
}