Bat and pangolin coronavirus spike glycoprotein structures provide insights into SARS-CoV-2 evolution

Shuyuan Zhang, Shuyuan Qiao, Jinfang Yu, Jianwei Zeng, Sisi Shan, Long Tian, Jun Lan, Linqi Zhang and Xinquan Wang ()
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Shuyuan Zhang: Tsinghua University
Shuyuan Qiao: Tsinghua University
Jinfang Yu: Tsinghua University
Jianwei Zeng: Tsinghua University
Sisi Shan: Tsinghua University
Long Tian: Tsinghua University
Jun Lan: Tsinghua University
Linqi Zhang: Tsinghua University
Xinquan Wang: Tsinghua University

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: 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 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.

Date: 2021
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DOI: 10.1038/s41467-021-21767-3

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