A tethered ligand assay to probe SARS-CoV-2:ACE2 interactions

Proc Natl Acad Sci U S A. 2022 Apr 5;119(14):e2114397119. doi: 10.1073/pnas.2114397119. Epub 2022 Mar 21.

Abstract

SignificanceIn the dynamic environment of the airways, where SARS-CoV-2 infections are initiated by binding to human host receptor ACE2, mechanical stability of the viral attachment is a crucial fitness advantage. Using single-molecule force spectroscopy techniques, we mimic the effect of coughing and sneezing, thereby testing the force stability of SARS-CoV-2 RBD:ACE2 interaction under physiological conditions. Our results reveal a higher force stability of SARS-CoV-2 binding to ACE2 compared to SARS-CoV-1, causing a possible fitness advantage. Our assay is sensitive to blocking agents preventing RBD:ACE2 bond formation. It will thus provide a powerful approach to investigate the modes of action of neutralizing antibodies and other agents designed to block RBD binding to ACE2 that are currently developed as potential COVID-19 therapeutics.

Keywords: AFM; SARS-CoV-2; force spectroscopy; host–pathogen interactions; magnetic tweezers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme 2 / chemistry
  • Angiotensin-Converting Enzyme 2 / metabolism*
  • COVID-19 / diagnosis
  • COVID-19 / metabolism*
  • COVID-19 / virology*
  • Disease Susceptibility
  • Host-Pathogen Interactions*
  • Humans
  • Protein Binding
  • SARS-CoV-2 / physiology*

Substances

  • Angiotensin-Converting Enzyme 2