{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["McCallum M"],"funding":["NIAID NIH HHS","Wellcome Trust","NIGMS NIH HHS","NIH HHS"],"pagination":["864-868"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9427005"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["375(6583)"],"pubmed_abstract":["The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern evades antibody-mediated immunity that comes from vaccination or infection with earlier variants due to accumulation of numerous spike mutations. To understand the Omicron antigenic shift, we determined cryo-electron microscopy and x-ray crystal structures of the spike protein and the receptor-binding domain bound to the broadly neutralizing sarbecovirus monoclonal antibody (mAb) S309 (the parent mAb of sotrovimab) and to the human ACE2 receptor. We provide a blueprint for understanding the marked reduction of binding of other therapeutic mAbs that leads to dampened neutralizing activity. Remodeling of interactions between the Omicron receptor-binding domain and human ACE2 likely explains the enhanced affinity for the host receptor relative to the ancestral virus."],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement."],"pmcid":["PMC9427005"],"funding_grant_id":["S10 OD023476","DP1 AI158186","HHSN272201700059C","T32 GM008268","P30 GM124169","R01 GM120553","209407/Z/17/Z"],"pubmed_authors":["Veesler D","Rosen LE","Joshi A","Walls AC","Dillen JR","Snell G","Powell AE","Hauser K","McCallum M","Czudnochowski N","Croll TI","Corti D","Stewart C","Bowen JE","Nix J","Zepeda SK","Virgin HW"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement.","description":"The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern evades antibody-mediated immunity that comes from vaccination or infection with earlier variants due to accumulation of numerous spike mutations. To understand the Omicron antigenic shift, we determined cryo-electron microscopy and x-ray crystal structures of the spike protein and the receptor-binding domain bound to the broadly neutralizing sarbecovirus monoclonal antibody (mAb) S309 (the parent mAb of sotrovimab) and to the human ACE2 receptor. We provide a blueprint for understanding the marked reduction of binding of other therapeutic mAbs that leads to dampened neutralizing activity. Remodeling of interactions between the Omicron receptor-binding domain and human ACE2 likely explains the enhanced affinity for the host receptor relative to the ancestral virus.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Feb","modification":"2026-05-27T23:24:06.959Z","creation":"2026-04-08T01:59:39.217Z"},"accession":"S-EPMC9427005","cross_references":{"pubmed":["35076256"],"doi":["10.1126/science.abn8652"]}}