{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hastie KM"],"funding":["Swiss National Science Foundation","NIAID NIH HHS"],"pagination":["472-478"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9302186"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["374(6566)"],"pubmed_abstract":["Antibody-based therapeutics and vaccines are essential to combat COVID-19 morbidity and mortality after severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Multiple mutations in SARS-CoV-2 that could impair antibody defenses propagated in human-to-human transmission and spillover or spillback events between humans and animals. To develop prevention and therapeutic strategies, we formed an international consortium to map the epitope landscape on the SARS-CoV-2 spike protein, defining and structurally illustrating seven receptor binding domain (RBD)–directed antibody communities with distinct footprints and competition profiles. Pseudovirion-based neutralization assays reveal spike mutations, individually and clustered together in variants, that affect antibody function among the communities. Key classes of RBD-targeted antibodies maintain neutralization activity against these emerging SARS-CoV-2 variants. These results provide a framework for selecting antibody treatment cocktails and understanding how viral variants might affect antibody therapeutic efficacy."],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study."],"pmcid":["PMC9302186"],"funding_grant_id":["U19 AI142790","195680","R01 AI147870","T32 AI125179"],"pubmed_authors":["Sato AK","Lan F","Peters B","Lujan Hernandez AG","Lu Y","Ingraham J","Rikhtegaran Tehrani Z","Hastie KM","Shen B","Zhang Q","Lang G","Bedinger D","Olmedillas E","Huang KA","Sajadi MM","Li H","Enriquez A","Parekh D","Sanders RW","Hui S","Horn GQ","Aldon Y","Shaffer K","Yuan TZ","Leung CL","Cobb RR","Li K","Snitselaar JL","Buck T","Ho DD","Tan Y","Federman RS","Saphire EO","Kim C","Lee S","Liu J","CoVIC-DB team1","Glanville J","Abraha M","Rabbitts TH","Dennison SM","Yu J","Kim M","Diaz Avalos R","Tomic MT","Stamatatos L","Youssef S","Jiang W","Zyla D","Aracic S","Yu X","Germann T","Feeney E","Ali H","Kim HM","Hariharan C","Rayaprolu V","Zandonatti M","Seo J","Fernandez JM","McGuire AT","Kong C","Schendel SL","Kellam P","van Gils MJ","Palser AL","Green R","MacCamy A","Mann C","Krebs SJ","Tomaras GD","Grigoryan G","Schweizer L","Yin J"],"additional_accession":[]},"is_claimable":false,"name":"Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study.","description":"Antibody-based therapeutics and vaccines are essential to combat COVID-19 morbidity and mortality after severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Multiple mutations in SARS-CoV-2 that could impair antibody defenses propagated in human-to-human transmission and spillover or spillback events between humans and animals. To develop prevention and therapeutic strategies, we formed an international consortium to map the epitope landscape on the SARS-CoV-2 spike protein, defining and structurally illustrating seven receptor binding domain (RBD)–directed antibody communities with distinct footprints and competition profiles. Pseudovirion-based neutralization assays reveal spike mutations, individually and clustered together in variants, that affect antibody function among the communities. Key classes of RBD-targeted antibodies maintain neutralization activity against these emerging SARS-CoV-2 variants. These results provide a framework for selecting antibody treatment cocktails and understanding how viral variants might affect antibody therapeutic efficacy.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Oct","modification":"2026-05-27T22:50:17.767Z","creation":"2026-04-08T01:56:23.712Z"},"accession":"S-EPMC9302186","cross_references":{"pubmed":["34554826"],"doi":["10.1126/science.abh2315"]}}