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

Wrobel, Antoni G; Benton, Donald J; Xu, Pengqi; Calder, Lesley J; Borg, Annabel; Roustan, Chloë; Martin, Stephen R; Rosenthal, Peter B; Skehel, John J; Gamblin, Steven J

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

journal contribution

posted on 2021-02-10, 11:02 authored by Antoni G Wrobel, Donald J Benton, Pengqi Xu, Lesley J Calder, Annabel Borg, Chloë Roustan, Stephen R Martin, Peter B Rosenthal, John J Skehel, Steven J Gamblin

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.