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TitleNanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 48, Year 2021
Publish dateNov 30, 2021
AuthorsLinhua Tai / Guoliang Zhu / Minnan Yang / Lei Cao / Xiaorui Xing / Guoliang Yin / Chun Chan / Chengfeng Qin / Zihe Rao / Xiangxi Wang / Fei Sun / Yun Zhu /
PubMed AbstractThe 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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:34782481
MethodsEM (subtomogram averaging)
Resolution10.9 Å
Structure data

EMDB-31037, PDB-7e9t:
Nanometer resolution in situ structure of SARS-CoV-2 post-fusion spike
Method: EM (subtomogram averaging) / Resolution: 10.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • severe acute respiratory syndrome coronavirus 2
  • 2019-nCoV, SARS-CoV-2
KeywordsVIRUS / SARS-CoV-2 / in situ / post-fusion / spike / cryo-STA

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