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

Keywords

EctodomainSpike (software development)Lipid bilayer fusionSpike ProteinBiophysicsProtein structureSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)CoronavirusCryo-electron microscopyVirologyChemistryCell biologyBiologyCoronavirus disease 2019 (COVID-19)VirusBiochemistryComputer scienceMedicine

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Publication Info

Year
2020
Type
article
Volume
369
Issue
6511
Pages
1586-1592
Citations
1318
Access
Closed

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Cite This

Yongfei Cai, Jun Zhang, Tianshu Xiao et al. (2020). Distinct conformational states of SARS-CoV-2 spike protein. Science , 369 (6511) , 1586-1592. https://doi.org/10.1126/science.abd4251

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DOI
10.1126/science.abd4251