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

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journal contribution
posted on 10.02.2021, 11:02 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.

Funding

Crick (Grant ID: 10015, Grant title: STP Structural Biology) Crick (Grant ID: 10143, Grant title: Rosenthal FC001143) Crick (Grant ID: 10078, Grant title: Gamblin FC001078)

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