Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein

Linhua Tai, Guoliang Zhu, Minnan Yang, Lei Cao, Xiaorui Xing, Guoliang Yin, Chun Chan, Chengfeng Qin, Zihe Rao, Xiangxi Wang, Fei Sun, Yun Zhu

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in β-propiolactone-inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation.

Original languageEnglish
Article numbere2112703118
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number48
StatePublished - 30 Nov 2021
Externally publishedYes


  • Cryo-electron tomography
  • Postfusion state
  • SARS-CoV-2
  • Spike protein
  • Subtomogram analysis


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