6M15

Cryo-EM structures of HKU2 spike glycoproteins

Summary for 6M15

• Entry DOI: 10.2210/pdb6m15/pdb
• EMDB information: 30037
• Descriptor: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: viral protein
• Biological source: Rhinolophus bat coronavirus HKU2
• Total number of polymer chains: 3
• Total formula weight: 388951.50

Authors

Wang, X.,Yu, J.,Qiao, S.,Guo, R. (deposition date: 2020-02-24, release date: 2020-05-27, Last modification date: 2024-11-06)

Primary citation

Yu, J.,Qiao, S.,Guo, R.,Wang, X.
Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution.
Nat Commun, 11:3070-3070, 2020

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, 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.

PubMed: 32555182
DOI: 10.1038/s41467-020-16876-4

Experimental method

ELECTRON MICROSCOPY (2.38 Å)