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This interaction is mediated by the receptor-binding domain (RBD) of the viral spike (S) glycoprotein. Structural and dynamic data have shown that S can adopt multiple conformations, which controls the exposure of the ACE2-binding site in the RBD. Here, using single-molecule F\u00f6rster resonance energy transfer (smFRET) imaging, we report the effects of ACE2 and antibody binding on the conformational dynamics of S from the Wuhan-1 strain and in the presence of the D614G mutation. We find that D614G modulates the energetics of the RBD position in a manner similar to ACE2 binding. We also find that antibodies that target diverse epitopes, including those distal to the RBD, stabilize the RBD in a position competent for ACE2 binding. Parallel solution-based binding experiments using fluorescence correlation spectroscopy (FCS) indicate antibody-mediated enhancement of ACE2 binding. These findings inform on novel strategies for therapeutic antibody cocktails.<\/jats:p>","DOI":"10.7554\/elife.75433","type":"journal-article","created":{"date-parts":[[2022,3,18]],"date-time":"2022-03-18T08:15:43Z","timestamp":1647591343000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.75433","source":"Crossref","is-referenced-by-count":99,"title":["Conformational dynamics and allosteric modulation of the SARS-CoV-2 spike"],"prefix":"10.7554","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2983-0123","authenticated-orcid":true,"given":"Marco A","family":"D\u00edaz-Salinas","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0464eyp60","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Microbiology and Physiological Systems, University of Massachusetts Chan Medical School","place":["Worcester, United 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