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            <funder>This project received funding from the Human Frontier Science Program (HFSP, grant number RGP0056/2018 to F.R.), the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (grant agreement number 772257 to F.R.), the European Union’s Horizon 2020 research and innovation programme (Marie Skłodowska-Curie grant number 895819 to C.V.), the Turing Centre for Living Systems (Centuri), PSL-Valorisation (grant J-DNA 2 to C.G. and T.S.), Labex IBEID (grant ANR-10-LABX-62-IBEID to F.A.R.), ANRS-MIE project EMERGEN (grant ANRS0151 to F.A.R.) and the Pasteur Coronavirus Task-Force (grants Allospike and TooLab to F.A.R.). The Molecular Motors and Machines team at IBENS has received a ‘Coup d’élan’ from the Fondation Bettencourt Schueller and is also an ‘Equipe labellisée’ by the Ligue Nationale Contre le Cancer. D.K. was supported by the PSL Institut de Convergence QLife. F. Stransky benefited from a doctoral fellowship from the Ministère de l’Enseignement Supérieur et de la Recherche. The project leading to this publication received funding from France 2030, the French Government programme managed by the French National Research Agency (ANR-16-CONV-0001), and from Excellence Initiative of Aix-Marseille University—A*MIDEX.</funder>
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              <p>The first step of SARS-CoV-2 infection involves the interaction between the viral trimeric spike protein (S) and the host angiotensin-converting enzyme 2 (ACE2). The receptor-binding domain (RBD) of S adopts two conformations: open and closed, respectively accessible and inaccessible to ACE2. Although these changes surely affect ACE2 binding, a quantitative description of the underlying mechanisms has remained elusive. Here we visualize RBD opening and closing using high-speed atomic force microscopy, gaining access to the corresponding transition rates. We also probe the S/ACE2 interaction at the ensemble level with biolayer interferometry and at the single-molecule level with atomic force microscopy and magnetic tweezers, evidencing that RBD dynamics hinder ACE2 binding but have no effect on unbinding. The resulting modulation is quantitatively predicted by a conformational selection model in which each S protomer behaves independently. Our work thus reveals a molecular mechanism by which RBD accessibility and binding strength can be tuned separately, providing hints to better understand the joint evolution of immune evasion and infectivity.</p>
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