Author: 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.
Title: Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2 Cord-id: gpfkk2yj Document date: 2021_2_5
ID: gpfkk2yj
Snippet: 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.
Document: 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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