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-Structure paper
Title | Bat and pangolin coronavirus spike glycoprotein structures provide insights into SARS-CoV-2 evolution. |
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Journal, issue, pages | Nat Commun, Vol. 12, Issue 1, Page 1607, Year 2021 |
Publish date | Mar 11, 2021 |
Authors | Shuyuan Zhang / Shuyuan Qiao / Jinfang Yu / Jianwei Zeng / Sisi Shan / Long Tian / Jun Lan / Linqi Zhang / Xinquan Wang / |
PubMed Abstract | In recognizing the host cellular receptor and mediating fusion of virus and cell membranes, the spike (S) glycoprotein of coronaviruses is the most critical viral protein for cross-species ...In recognizing the host cellular receptor and mediating fusion of virus and cell membranes, the spike (S) glycoprotein of coronaviruses is the most critical viral protein for cross-species transmission and infection. Here we determined the cryo-EM structures of the spikes from bat (RaTG13) and pangolin (PCoV_GX) coronaviruses, which are closely related to SARS-CoV-2. All three receptor-binding domains (RBDs) of these two spike trimers are in the "down" conformation, indicating they are more prone to adopt the receptor-binding inactive state. However, we found that the PCoV_GX, but not the RaTG13, spike is comparable to the SARS-CoV-2 spike in binding the human ACE2 receptor and supporting pseudovirus cell entry. We further identified critical residues in the RBD underlying different activities of the RaTG13 and PCoV_GX/SARS-CoV-2 spikes. These results collectively indicate that tight RBD-ACE2 binding and efficient RBD conformational sampling are required for the evolution of SARS-CoV-2 to gain highly efficient infection. |
External links | Nat Commun / PubMed:33707453 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.5 - 2.93 Å |
Structure data | EMDB-30416, PDB-7cn4: EMDB-30418, PDB-7cn8: |
Chemicals | ChemComp-NAG: ChemComp-EIC: |
Source |
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Keywords | VIRAL PROTEIN / spike |