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

Antoni G Wrobel1 Donald J Benton2 Pengqi Xu3,4 Lesley J Calder5 Annabel Borg6 Chloë Roustan6 Stephen R Martin3 Peter B Rosenthal5 John J Skehel3 Steven J Gamblin7
Affiliations 7 institutions
  1. Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK. [email protected].
  2. Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK. [email protected].
  3. Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK.
  4. Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, Guangdong, China.
  5. Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, NW1 1AT, London, UK.
  6. Structural Biology Science Technology Platform, Francis Crick Institute, NW1 1AT, London, UK.
  7. Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK. [email protected].
Active Last checked 2026-10-05 03:30:31 Source: NCBI PubMed

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.

Supporting text Virus Host Location
Evolution, Molecular 178 Angiotensin-Converting Enzyme 2 178 Animals 1981 Binding, Competitive 4 COVID-19 427 Cryoelectron Microscopy 37 Humans 1455 Models, Molecular 99 Pandemics 109 Pangolins 29 Protein Binding 194 Protein Domains 45 SARS-CoV-2 456 Spike Glycoprotein, Coronavirus 276 ACE2 protein, human 87 spike protein, SARS-CoV-2 158

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Functional Mechanism
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