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TitleStructural basis of broad SARS-CoV-2 cross-neutralization by affinity-matured public antibodies.
Journal, issue, pagesCell Rep Med, Page 101577, Year 2024
Publish dateMay 15, 2024
AuthorsDaniel J Sheward / Pradeepa Pushparaj / Hrishikesh Das / Allison J Greaney / Changil Kim / Sungyong Kim / Leo Hanke / Erik Hyllner / Robert Dyrdak / Jimin Lee / Xaquin Castro Dopico / Pia Dosenovic / Thomas P Peacock / Gerald M McInerney / Jan Albert / Martin Corcoran / Jesse D Bloom / Ben Murrell / Gunilla B Karlsson Hedestam / B Martin Hällberg /
PubMed AbstractDescendants 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 ...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.
External linksCell Rep Med / PubMed:38761799
MethodsEM (single particle)
Resolution2.68 Å
Structure data

16375

8c0y

EMDB-16375, PDB-8c0y:
SARS-CoV2 Omicron BA.1 RBD in complex with CAB-A17 antibody
Method: EM (single particle) / Resolution: 2.68 Å

42970

8v4f

EMDB-42970, PDB-8v4f:
Model and map from local refinement of a CAB-A17 - Omicron Ba.1 spike complex
Method: EM (single particle) / Resolution: 2.68 Å

Source
  • severe acute respiratory syndrome coronavirus 2
  • Enterobacteria phage T4 (virus)
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / Antibody / Spike / Complex / VIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / RBD / Fab / VIRAL PROTEIN-IMMUNE SYSTEM complex

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