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

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.

SUBMITTER: Wrobel AG

PROVIDER: S-EPMC7864994 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

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

Wrobel Antoni G AG Benton Donald J DJ Xu Pengqi P Calder Lesley J LJ Borg Annabel A Roustan Chloë C Martin Stephen R SR Rosenthal Peter B PB Skehel John J JJ Gamblin Steven J SJ

Nature communications 20210205 1

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. ...[more]

PMID: 33547281

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