The DOI matches its Crossref record; 76 of the 82 references it cites were found in a registry or an index.
Molecular Architecture of the SARS-CoV-2 Virus
Open accessPublished version of a preprint
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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“Therefore, the S protein is considered the main antigen for vaccine design.228–230”
From Advances in COVID-19 mRNA vaccine development (2022) · cites this paper as [228]
In the citing paper
“The trimeric S protein on the surface of SARS-CoV-2 plays a key role in mediating host cell invasion.”
From Advances in COVID-19 mRNA vaccine development (2022) · cites this paper as [228]
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Cites
VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952 · cited 1×
“PDB: 6XR8 was prepared in VMD (Humphrey et al., 1996) for the MDFF, which was performed in vacuum ll”
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,047 · cited 2×
“Fitting Atomic models (PDB accession code 6XR8, 6VYB, 6XRA) of the pre- and postfusion S were rigidly fitted to the corresponding densities using the Fit in Map tool (Pettersen et al., 2004).”
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969 · cited 3×
“The causative pathogen, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel b-coronavirus (Lu et al., 2020; Wu et al., 2020; Zhou et al., 2020).”
Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286 · cited 2×
“The S protein binds to the cellular surface receptor angiotensin-converting enzyme 2 (ACE2) through the receptor binding domain (RBD), an essential step for membrane fusion (Hoffmann et al., 2020; Lan et al., 2020; Shang et al., 2020; Wang et al., 2020; Yan et al., 2020; Zhou et al., 2020).”
BackgroundSelf-citationScalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914 · cited 1×
“12 (Phillips et al., 2005) and the CHARMM36 force field (MacKerell et al.”
All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins
MacKerell, A. D., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., et al. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp973084f · Cited by 14,429 · cited 1×
“, 2005) and the CHARMM36 force field (MacKerell et al., 1998).”
Lu, R., Zhao, X., Li, J., Niu, P., Yang, B., Wu, H., Wang, W., Song, H., Huang, B., Zhu, N., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30251-8 · Cited by 11,907 · cited 2×
“The causative pathogen, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel b-coronavirus (Lu et al., 2020; Wu et al., 2020; Zhou et al., 2020).”
A new coronavirus associated with human respiratory disease in China
Wu, F., Zhao, S., Yu, B., Chen, Y.-M., Wang, W., Song, Z.-G., Hu, Y., Tao, Z.-W., Tian, J.-H., Pei, Y.-Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2008-3 · Cited by 11,688 · cited 2×
“The causative pathogen, SARS-CoV-2, is a novel β-coronavirus (Lu et al., 2020; Wu et al., 2020; Zhou et al., 2020).”
Self-citationCryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897 · cited 12×
“Several prefusion conformations have been resolved for the S protein, where the three RBDs display distinct orientations: up or down (Walls et al., 2020; Wrapp et al., 2020).”
BackgroundInfluentialStructure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586 · cited 12×
“Native Structures of S in the Prefusion Conformation The native structures of S in the ‘‘RBD down’’ and ‘‘one RBD up’’ conformations were similar to the rigidly fitted recombinant protein structures (PDB: 6XR8, 6VYB; Cai et al., 2020; Walls et al., 2020), except for the N terminus domain (NTD).”
Influential
Research works printed but not linked: 1
- Yao, 2020, Patient-derived mutations impact pathogenicity of SARS-CoV-2, medRxiv
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Liang, J., Peng, C., Song, Y. S., Zhang, Z., Yu, J., Wang, X., & Li, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.02.697259
“In highly pathogenic betacoronaviruses such as SARS-CoV-2, a substantial fraction of prefusion S adopt RBD-up conformations 33 , likely contributing to enhanced infectivity and transmissibility 42 .”
InfluentialSelf-citation
Metadata
- 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
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-10
- Volume
- 183
- Issue
- 3
- Pages
- 730-738.e13
- ISSN
- 0092-8674 (ISSN-L)
- 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
- 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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