Cited by 1,060SARS-CoV-2 and COVID-19 ResearchAdvanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and Function

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Molecular Architecture of the SARS-CoV-2 Virus

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Yao, Hangping, Song, Yutong, Chen, Yong, Wu, Nanping, Xu, Jialu, Sun, Chujie, Zhang, Jiaxing, Weng, Tianhao, Zhang, Zheyuan, Wu, Zhigang, Cheng, Linfang, Shi, Danrong, Lu, Xiangyun, Lei, Jianlin, Crispin, Max, Shi, Yigong, Li, Lanjuan, Li, Sai·2020·Cell

DOI 10.1016/j.cell.2020.09.018PMC PMC7474903

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Abstract

SARS-CoV-2 is an enveloped virus responsible for the COVID-19 pandemic. Despite recent advances in the structural elucidation of SARS-CoV-2 proteins, the detailed architecture of the intact virus remains to be unveiled. Here we report the molecular assembly of the authentic SARS-CoV-2 virus using cryoelectron tomography (cryo-ET) and subtomogram averaging (STA). Native structures of the S proteins in pre- and postfusion conformations were determined to average resolutions of 8.7-11 Å. Compositions of the N-linked glycans from the native spikes were analyzed by mass spectrometry, which revealed overall processing states of the native glycans highly similar to that of the recombinant glycoprotein glycans. The native conformation of the ribonucleoproteins (RNPs) and their higher-order assemblies were revealed. Overall, these characterizations revealed the architecture of the SARS-CoV-2 virus in exceptional detail and shed light on how the virus packs its ∼30-kb-long single-segmented RNA in the ∼80-nm-diameter lumen.

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Additional file 1 of Human ACE2 protein is a molecular switch controlling the mode of SARS-CoV-2 transmission
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Additional file 2 of Human ACE2 protein is a molecular switch controlling the mode of SARS-CoV-2 transmission
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Additional file 3 of Human ACE2 protein is a molecular switch controlling the mode of SARS-CoV-2 transmission
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Rapid In-Vitro Inactivation of Various SARS-CoV-2 Strains Using Ionizing Radiation: New Inactivation Patterns and Mechanistic Insights
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β-Coronavirus Nsp6 hijacks host ER translocation machineries into viral replication centersPreprint
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Authors: Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., Cheng, L., Shi, D., Lu, X., Lei, J., Crispin, M., Shi, Y., Li, L., & Li, S.
Affiliations: First Affiliated Hospital Zhejiang University (CN)
Tsinghua University (CN)
Center for Life Sciences (CN)
University of Southampton (GB)
Westlake University (CN)
Corresponding author: Li, Lanjuan
Li, Sai
ORCID: Yao, Hangping
Song, Yutong
Chen, Yong
Wu, Nanping
Xu, Jialu
Zhang, Jiaxing
Zhang, Zheyuan
Wu, Zhigang
Lu, Xiangyun
Lei, Jianlin
Crispin, Max
Shi, Yigong
Li, Lanjuan
Li, Sai
Venue: Cell
Publisher: Elsevier BV
Published: 2020-10
Volume: 183
Issue: 3
Pages: 730-738.e13
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2020.09.018
PMC: PMC7474903
OpenAlex: W3083130172
Cited by: 1,060
References: 82
Citations by year: 2026: 78 · 2025: 98 · 2024: 157 · 2023: 201 · 2022: 236 · 2021: 252 · 2020: 38
FWCI: 23.88
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 393 d)
Locations: Cell (publishedVersion)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
SSRN Electronic Journal (acceptedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
ePrints Soton (University of Southampton) (acceptedVersion)
Funders: Zhejiang University
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: SARS-CoV-2, spike protein, N-glycans, ribonucleoprotein, viral RNA packaging, viral assembly
MeSH terms: Betacoronavirus, SARS-CoV-2, Animals, Chlorocebus aethiops, Humans, Models, Molecular, Protein Conformation, Mass Spectrometry, Vero Cells, Viral Proteins, Virus Cultivation, Virus Assembly, Cryoelectron Microscopy

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