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| Title | Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 3070, Year 2020 |
| Publish date | Jun 17, 2020 |
Authors | Jinfang Yu / Shuyuan Qiao / Runyu Guo / Xinquan Wang / ![]() |
| PubMed Abstract | Porcine coronavirus SADS-CoV has been identified from suckling piglets with severe diarrhea in southern China in 2017. The SADS-CoV genome shares ~95% identity to that of bat α-coronavirus HKU2, ...Porcine coronavirus SADS-CoV has been identified from suckling piglets with severe diarrhea in southern China in 2017. The SADS-CoV genome shares ~95% identity to that of bat α-coronavirus HKU2, suggesting that SADS-CoV may have emerged from a natural reservoir in bats. Here we report the cryo-EM structures of HKU2 and SADS-CoV spike (S) glycoprotein trimers at 2.38 Å and 2.83 Å resolution, respectively. We systematically compare the domains of HKU2 spike with those of α-, β-, γ-, and δ-coronavirus spikes, showing that the S1 subunit N- and C-terminal domains of HKU2/SADS-CoV are ancestral domains in the evolution of coronavirus spike proteins. The connecting region after the fusion peptide in the S2 subunit of HKU2/SADS-CoV adopts a unique conformation. These results structurally demonstrate a close evolutionary relationship between HKU2/SADS-CoV and β-coronavirus spikes and provide insights into the evolution and cross-species transmission of coronaviruses. |
External links | Nat Commun / PubMed:32555182 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.38 - 2.83 Å |
| Structure data | EMDB-30037, PDB-6m15: EMDB-30038, PDB-6m16: |
| Chemicals | ![]() ChemComp-NAG: ![]() ChemComp-HOH: |
| Source |
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Keywords | VIRAL PROTEIN |
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rhinolophus bat coronavirus hku2
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