{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sankhala RS"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["131-147.e7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11145656"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(2)"],"pubmed_abstract":["Given the continuous emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VoCs), immunotherapeutics that target conserved epitopes on the spike (S) glycoprotein have therapeutic advantages. Here, we report the crystal structure of the SARS-CoV-2 S receptor-binding domain (RBD) at 1.95 Å and describe flexibility and distinct conformations of the angiotensin-converting enzyme 2 (ACE2)-binding site. We identify a set of SARS-CoV-2-reactive monoclonal antibodies (mAbs) with broad RBD cross-reactivity including SARS-CoV-2 Omicron subvariants, SARS-CoV-1, and other sarbecoviruses and determine the crystal structures of mAb-RBD complexes with Ab246 and CR3022 mAbs targeting the class IV site, WRAIR-2134, which binds the recently designated class V epitope"],"journal":["Structure (London, England : 1993)"],"pubmed_title":["Antibody targeting of conserved sites of vulnerability on the SARS-CoV-2 spike receptor-binding domain."],"pmcid":["PMC11145656"],"funding_grant_id":["R01 AI155983","P41 GM103403"],"pubmed_authors":["Peterson CE","Swafford I","Sankhala RS","Rolland M","Polonis VR","Choe M","Tran U","Gromowski GD","Kuklis C","Rajan S","King J","Dussupt V","Currier JR","Corbitt C","Wieczorek L","Bai H","Lal KG","de Val N","Yan L","van Dyk D","Joyce MG","Smith C","Broder CC","Zemil M","Townsley SM","Mendez-Rivera L","Sterling SL","Esser MT","Rees PA","Chang WC","Soman S","Green EC","Jensen JL","Laing ED","Britton Z","Modjarrad K","Loo YM","Chen WH","Krebs SJ","Hajduczki A","Michael NL","Paquin-Proulx D","Donofrio GC","Martinez EJ","McTamney PM"],"additional_accession":[]},"is_claimable":false,"name":"Antibody targeting of conserved sites of vulnerability on the SARS-CoV-2 spike receptor-binding domain.","description":"Given the continuous emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VoCs), immunotherapeutics that target conserved epitopes on the spike (S) glycoprotein have therapeutic advantages. Here, we report the crystal structure of the SARS-CoV-2 S receptor-binding domain (RBD) at 1.95 Å and describe flexibility and distinct conformations of the angiotensin-converting enzyme 2 (ACE2)-binding site. We identify a set of SARS-CoV-2-reactive monoclonal antibodies (mAbs) with broad RBD cross-reactivity including SARS-CoV-2 Omicron subvariants, SARS-CoV-1, and other sarbecoviruses and determine the crystal structures of mAb-RBD complexes with Ab246 and CR3022 mAbs targeting the class IV site, WRAIR-2134, which binds the recently designated class V epitope","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Feb","modification":"2026-06-02T11:58:34.401Z","creation":"2025-04-03T23:23:39.469Z"},"accession":"S-EPMC11145656","cross_references":{"pubmed":["38157856"],"doi":["10.1016/j.str.2023.11.015"]}}