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

Nat Commun. 2021 Feb 5;12(1):837. doi: 10.1038/s41467-021-21006-9.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme 2 / metabolism
  • Animals
  • Binding, Competitive
  • COVID-19 / epidemiology
  • COVID-19 / prevention & control*
  • COVID-19 / virology
  • Cryoelectron Microscopy
  • Evolution, Molecular*
  • Humans
  • Models, Molecular
  • Pandemics
  • Pangolins / virology
  • Protein Binding
  • Protein Domains
  • SARS-CoV-2 / genetics*
  • SARS-CoV-2 / metabolism
  • SARS-CoV-2 / physiology
  • Spike Glycoprotein, Coronavirus / chemistry
  • Spike Glycoprotein, Coronavirus / genetics*
  • Spike Glycoprotein, Coronavirus / metabolism

Substances

  • Spike Glycoprotein, Coronavirus
  • spike protein, SARS-CoV-2
  • ACE2 protein, human
  • Angiotensin-Converting Enzyme 2