8C0Y
SARS-CoV2 Omicron BA.1 RBD in complex with CAB-A17 antibody
Summary for 8C0Y
Entry DOI | 10.2210/pdb8c0y/pdb |
EMDB information | 16375 |
Descriptor | Spike protein S2', CAB-A17 antibody (variable) (3 entities in total) |
Functional Keywords | antibody, spike, complex, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 More |
Total number of polymer chains | 3 |
Total formula weight | 46177.57 |
Authors | Das, H.,Hallberg, B.M. (deposition date: 2022-12-19, release date: 2024-06-19, Last modification date: 2024-11-13) |
Primary citation | Sheward, D.J.,Pushparaj, P.,Das, H.,Greaney, A.J.,Kim, C.,Kim, S.,Hanke, L.,Hyllner, E.,Dyrdak, R.,Lee, J.,Dopico, X.C.,Dosenovic, P.,Peacock, T.P.,McInerney, G.M.,Albert, J.,Corcoran, M.,Bloom, J.D.,Murrell, B.,Karlsson Hedestam, G.B.,Hallberg, B.M. Structural basis of broad SARS-CoV-2 cross-neutralization by affinity-matured public antibodies. Cell Rep Med, 5:101577-101577, 2024 Cited by PubMed Abstract: Descendants of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant now account for almost all SARS-CoV-2 infections. The Omicron variant and its sublineages have spike glycoproteins that are highly diverged from the pandemic founder and first-generation vaccine strain, resulting in significant evasion from monoclonal antibody therapeutics and vaccines. Understanding how commonly elicited antibodies can broaden to cross-neutralize escape variants is crucial. We isolate IGHV3-53, using "public" monoclonal antibodies (mAbs) from an individual 7 months post infection with the ancestral virus and identify antibodies that exhibit potent and broad cross-neutralization, extending to the BA.1, BA.2, and BA.4/BA.5 sublineages of Omicron. Deep mutational scanning reveals these mAbs' high resistance to viral escape. Structural analysis via cryoelectron microscopy of a representative broadly neutralizing antibody, CAB-A17, in complex with the Omicron BA.1 spike highlights the structural underpinnings of this broad neutralization. By reintroducing somatic hypermutations into a germline-reverted CAB-A17, we delineate the role of affinity maturation in the development of cross-neutralization by a public class of antibodies. PubMed: 38761799DOI: 10.1016/j.xcrm.2024.101577 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.68 Å) |
Structure validation
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