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


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
05 04 2022
Historique:
entrez: 21 3 2022
pubmed: 22 3 2022
medline: 2 4 2022
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 35312342
doi: 10.1073/pnas.2114397119
pmc: PMC9168514
doi:

Substances chimiques

Angiotensin-Converting Enzyme 2 EC 3.4.17.23

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e2114397119

Subventions

Organisme : Deutsche Forschungsgemeinschaft (DFG)
ID : 386143268
Organisme : Deutsche Forschungsgemeinschaft (DFG)
ID : 111166240
Organisme : European Molecular Biology Organization (EMBO)
ID : ALTF 1047-2019
Organisme : Auburn University (AU)
Organisme : Spanish Ministry of Science, Innovation and Universities for the Spanish State Research Agency Retos Grant
ID : RTI2018-099318-B-I00
Organisme : Cofunded by the European Regional Development Fund (FEDER)
Organisme : Physics Department of the LMU Munich

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Auteurs

Magnus S Bauer (MS)

Department of Physics, LMU Munich, 80799 Munich, Germany.
Center for NanoScience, LMU Munich, 80799 Munich, Germany.
Department of Chemical Engineering, Stanford University, Stanford, CA 94305.

Sophia Gruber (S)

Department of Physics, LMU Munich, 80799 Munich, Germany.
Center for NanoScience, LMU Munich, 80799 Munich, Germany.

Adina Hausch (A)

Department of Physics, LMU Munich, 80799 Munich, Germany.
Center for NanoScience, LMU Munich, 80799 Munich, Germany.

Priscila S F C Gomes (PSFC)

Department of Physics, Auburn University, Auburn, AL 36849.

Lukas F Milles (LF)

Department of Biochemistry, University of Washington, Seattle, WA 98195.
Institute for Protein Design, University of Washington, Seattle, WA 98195.

Thomas Nicolaus (T)

Department of Physics, LMU Munich, 80799 Munich, Germany.
Center for NanoScience, LMU Munich, 80799 Munich, Germany.

Leonard C Schendel (LC)

Department of Physics, LMU Munich, 80799 Munich, Germany.
Center for NanoScience, LMU Munich, 80799 Munich, Germany.

Pilar López Navajas (PL)

Centro de Investigaciones Biológicas Margarita Salas, Spanish National Research Council, 28040 Madrid, Spain.

Erik Procko (E)

Department of Biochemistry, University of Illinois, Urbana, IL 61801.
Cancer Center at Illinois, University of Illinois, Urbana, IL 61801.

Daniel Lietha (D)

Centro de Investigaciones Biológicas Margarita Salas, Spanish National Research Council, 28040 Madrid, Spain.

Marcelo C R Melo (MCR)

Department of Physics, Auburn University, Auburn, AL 36849.

Rafael C Bernardi (RC)

Department of Physics, Auburn University, Auburn, AL 36849.

Hermann E Gaub (HE)

Department of Physics, LMU Munich, 80799 Munich, Germany.
Center for NanoScience, LMU Munich, 80799 Munich, Germany.

Jan Lipfert (J)

Department of Physics, LMU Munich, 80799 Munich, Germany.
Center for NanoScience, LMU Munich, 80799 Munich, Germany.

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