We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2.
- Authors
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.
- 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. It has been suggested that pangolin coronaviruses may be the origin of SARS-CoV-2. Here the authors show that the Pangolin-CoV spike is structurally closely related to the closed form of SARS-CoV-2 spike and exhibits similar binding properties to human and pangolin ACE2; although neither spike binds bat ACE2.
- Subjects
SARS-CoV-2; ANGIOTENSIN converting enzyme; COVID-19; CORONAVIRUSES; PANGOLINS
- Publication
Nature Communications, 2021, Vol 12, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-021-21006-9