Cited by 1,221SARS-CoV-2 and COVID-19 ResearchProtein Structure and DynamicsEnzyme Structure and Function

Distinct conformational states of SARS-CoV-2 spike protein

Open access
Cai, Yongfei, Zhang, Jun, Xiao, Tianshu, Peng, Hanqin, Sterling, Sarah M., Walsh, Richard M., Rawson, Shaun, Rits-Volloch, Sophia +1 more·2020·Science

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Abstract

A dynamic viral spike: Efforts to protect human cells against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have focused on the trimeric spike (S) protein. Several structures have shown a stabilized ectodomain of the spike in its prefusion conformation. Cai et al. now provide insight into the structural changes in the S protein that result in the fusion of the viral and host cell membranes. They purified full-length S protein and determined cryo–electron microscopy structures of both the prefusion and postfusion conformations. These structures add to our understanding of S protein function and could inform vaccine design. Science , this issue p. 1586

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  • The S2 subunit comprises FP, HR, CH, CD, TMD, CT, and is responsible for mediating fusion between virus and host cell membrane.

    “The S2 subunit comprises the fusion peptide (FP), double heptad repeat (HR), central helix region (CH), connector domain (CD), transmembrane domain (TMD), and cytoplasmic tail (CT), and the S2 subunit is responsible for mediating the fusion between the virus and the host cell membrane233–236”

    From Advances in COVID-19 mRNA vaccine development (2022) · cites this paper as [236]

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Authors
Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B.
Affiliations
  • Boston Children's Hospital (US)
  • Harvard University (US)
  • Division of Molecular Medicine, Boston Children’s Hospital, Boston, MA 02115, USA.
Corresponding author
Chen, Bing
Venue
Science
Published
2020-09-25
Volume
369
Issue
6511
Pages
1586-1592
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W3042332408
Cited by
1,221
References
68
Citations by year
2026: 67 · 2025: 109 · 2024: 139 · 2023: 187 · 2022: 293 · 2021: 331 · 2020: 92 · 2018: 1
FWCI
29.61
Type
journal article
Language
en
Open access
Locations
  • Science (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (submittedVersion)
Funders
National Institutes of Health (AI147884, AI14788401A1S1)
Topics
  • Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
SARS-CoV-2, spike protein, postfusion conformation, membrane fusion, receptor binding domain, fusion peptide, N-glycans, viral entry, vaccine design, antiviral agents

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