{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Diaz-Salinas MA"],"funding":["UMass Chan Medical School COVID-19 Pandemic Relief Fund","NIAID NIH HHS","Evergrande COVID-19 Response Fund","NCI NIH HHS","Massachusetts Consortium on Pathogen Readiness","National Institutes of Health","NIH HHS","Worcester Foundation for Biomedical Research"],"pagination":["e75433"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8963877"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11"],"pubmed_abstract":["Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infects cells through binding to angiotensin-converting enzyme 2 (ACE2). 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 Förster 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 t"],"journal":["eLife"],"pubmed_title":["Conformational dynamics and allosteric modulation of the SARS-CoV-2 spike."],"pmcid":["PMC8963877"],"funding_grant_id":["K22 CA241362","R37 AI047868","K22CA241362","R37AI147868","R37 AI147868","R01AI148784","R01 AI148784"],"pubmed_authors":["Yurkovetskiy L","Shen K","Diaz-Salinas MA","Luban J","Munro JB","Li Q","Wang Y","Ejemel M"],"additional_accession":[]},"is_claimable":false,"name":"Conformational dynamics and allosteric modulation of the SARS-CoV-2 spike.","description":"Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infects cells through binding to angiotensin-converting enzyme 2 (ACE2). 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 Förster 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 t","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2026-05-31T06:00:59.06Z","creation":"2025-02-19T01:54:34.735Z"},"accession":"S-EPMC8963877","cross_references":{"pubmed":["35323111"],"doi":["10.7554/eLife.75433"]}}