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TitleCryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 3618, Year 2020
Publish dateJul 17, 2020
AuthorsXiaoyi Fan / Duanfang Cao / Lingfei Kong / Xinzheng Zhang /
PubMed AbstractGlobal emergencies caused by the severe acute respiratory syndrome coronavirus (SARS-CoV), Middle-East respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV-2 significantly endanger human health. ...Global emergencies caused by the severe acute respiratory syndrome coronavirus (SARS-CoV), Middle-East respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV-2 significantly endanger human health. The spike (S) glycoprotein is the key antigen and its conserved S2 subunit contributes to viral entry by mediating host-viral membrane fusion. However, structural information of the post-fusion S2 from these highly pathogenic human-infecting coronaviruses is still lacking. We used single-particle cryo-electron microscopy to show that the post-fusion SARS-CoV S2 forms a further rotated HR1-HR2 six-helix bundle and a tightly bound linker region upstream of the HR2 motif. The structures of pre- and post-fusion SARS-CoV S glycoprotein dramatically differ, resembling that of the Mouse hepatitis virus (MHV) and other class I viral fusion proteins. This structure suggests potential targets for the development of vaccines and therapies against a wide range of SARS-like coronaviruses.
External linksNat Commun / PubMed:32681106 / PubMed Central
MethodsEM (single particle)
Resolution3.9 Å
Structure data

30072

6m3w

EMDB-30072, PDB-6m3w:
Post-fusion structure of SARS-CoV spike glycoprotein
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • SARS coronavirus
  • human sars coronavirus
KeywordsVIRAL PROTEIN / spike / post-fusion / SARS-CoV / coronavirus / glycoprotein / trimer

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