Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2

Antoni G. Wrobel (), Donald J. Benton (), Pengqi Xu, Lesley J. Calder, Annabel Borg, Chloë Roustan, Stephen R. Martin, Peter B. Rosenthal, John J. Skehel and Steven J. Gamblin ()
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Antoni G. Wrobel: Francis Crick Institute, NW1 1AT
Donald J. Benton: Francis Crick Institute, NW1 1AT
Pengqi Xu: Francis Crick Institute, NW1 1AT
Lesley J. Calder: Francis Crick Institute, NW1 1AT
Annabel Borg: Francis Crick Institute, NW1 1AT
Chloë Roustan: Francis Crick Institute, NW1 1AT
Stephen R. Martin: Francis Crick Institute, NW1 1AT
Peter B. Rosenthal: Francis Crick Institute, NW1 1AT
John J. Skehel: Francis Crick Institute, NW1 1AT
Steven J. Gamblin: Francis Crick Institute, NW1 1AT

Nature Communications, 2021, vol. 12, issue 1, 1-6

Abstract: Abstract Coronaviruses of bats and pangolins have been implicated in the origin and evolution of the pandemic SARS-CoV-2. We show that spikes from Guangdong Pangolin-CoVs, closely related to SARS-CoV-2, bind strongly to human and pangolin ACE2 receptors. We also report the cryo-EM structure of a Pangolin-CoV spike protein and show it adopts a fully-closed conformation and that, aside from the Receptor-Binding Domain, it resembles the spike of a bat coronavirus RaTG13 more than that of SARS-CoV-2.

Date: 2021
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DOI: 10.1038/s41467-021-21006-9

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