Bat and pangolin coronavirus spike glycoprotein structures provide insights into SARS-CoV-2 evolution.
Nat Commun
; 12(1): 1607, 2021 03 11.
Article
em En
| MEDLINE
| ID: mdl-33707453
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.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Quirópteros
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Coronavirus
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Glicoproteína da Espícula de Coronavírus
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Pangolins
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SARS-CoV-2
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COVID-19
Limite:
Animals
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Humans
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article