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

tetano

Editor, Senior Moderator
Nat Commun


. 2021 Feb 5;12(1):837.
doi: 10.1038/s41467-021-21006-9.
Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2


Antoni G Wrobel[SUP] #[/SUP][SUP] 1 [/SUP], Donald J Benton[SUP] #[/SUP][SUP] 2 [/SUP], Pengqi Xu[SUP] 3 4 [/SUP], Lesley J Calder[SUP] 5 [/SUP], Annabel Borg[SUP] 6 [/SUP], Chlo? Roustan[SUP] 6 [/SUP], Stephen R Martin[SUP] 3 [/SUP], Peter B Rosenthal[SUP] 5 [/SUP], John J Skehel[SUP] 3 [/SUP], Steven J Gamblin[SUP] 7 [/SUP]



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Free article

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.
 
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