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  3. Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor

Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor

  • Nat Commun. 2020 Sep 11;11(1):4541. doi: 10.1038/s41467-020-18319-6.
Jinsung Yang  # 1,  Simon J L Petitjean  # 1,  Melanie Koehler 1,  Qingrong Zhang 1,  Andra C Dumitru 1,  Wenzhang Chen 2,  Sylvie Derclaye 1,  Stéphane P Vincent 2,  Patrice Soumillion 1,  David Alsteens 3 4
Affiliations

Affiliations

  • 1 Louvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
  • 2 Départment de Chimie, Laboratoire de Chimie Bio-Organique, University of Namur, Namur, Belgium.
  • 3 Louvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Louvain-la-Neuve, Belgium. david.alsteens@uclouvain.be.
  • 4 Walloon Excellence in Life sciences and Biotechnology (WELBIO), 1300, Wavre, Belgium. david.alsteens@uclouvain.be.
  • # Contributed equally.
PMID: 32917884 DOI: 10.1038/s41467-020-18319-6
Abstract

Study of the interactions established between the viral glycoproteins and their host receptors is of critical importance for a better understanding of virus entry into cells. The novel coronavirus SARS-CoV-2 entry into host cells is mediated by its spike glycoprotein (S-glycoprotein), and the angiotensin-converting Enzyme 2 (ACE2) has been identified as a cellular receptor. Here, we use atomic force microscopy to investigate the mechanisms by which the S-glycoprotein binds to the ACE2 receptor. We demonstrate, both on model surfaces and on living cells, that the receptor binding domain (RBD) serves as the binding interface within the S-glycoprotein with the ACE2 receptor and extract the kinetic and thermodynamic properties of this binding pocket. Altogether, these results provide a picture of the established interaction on living cells. Finally, we test several binding inhibitor Peptides targeting the virus early attachment stages, offering new perspectives in the treatment of the SARS-CoV-2 Infection.

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