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TitleBispecific antibodies targeting the N-terminal and receptor binding domains potently neutralize SARS-CoV-2 variants of concern.
Journal, issue, pagesSci Transl Med, Vol. 17, Issue 788, Page eadq5720, Year 2025
Publish dateMar 5, 2025
AuthorsAdonis A Rubio / Viren A Baharani / Bernadeta Dadonaite / Megan Parada / Morgan E Abernathy / Zijun Wang / Yu E Lee / Michael R Eso / Jennie Phung / Israel Ramos / Teresia Chen / Gina El Nesr / Jesse D Bloom / Paul D Bieniasz / Michel C Nussenzweig / Christopher O Barnes /
PubMed AbstractThe ongoing emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) that reduce the effectiveness of antibody therapeutics necessitates development of ...The ongoing emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) that reduce the effectiveness of antibody therapeutics necessitates development of next-generation antibody modalities that are resilient to viral evolution. Here, we characterized amino-terminal domain (NTD)- and receptor binding domain (RBD)-specific monoclonal antibodies previously isolated from coronavirus disease 2019 (COVID-19) convalescent donors for their activity against emergent SARS-CoV-2 VOCs. Among these, the NTD-specific antibody C1596 displayed the greatest breadth of binding to VOCs, with cryo-electron microscopy structural analysis revealing recognition of a distinct NTD epitope outside of the site i antigenic supersite. Given C1596's favorable binding profile, we designed a series of bispecific antibodies (bsAbs), termed CoV2-biRNs, that featured both NTD and RBD specificities. Two of the C1596-inclusive bsAbs, CoV2-biRN5 and CoV2-biRN7, retained potent in vitro neutralization activity against all Omicron variants tested, including XBB.1.5, BA.2.86, and JN.1, contrasting the diminished potency of parental antibodies delivered as monotherapies or as a cocktail. Furthermore, prophylactic delivery of CoV2-biRN5 reduced the viral load within the lungs of K18-hACE2 mice after challenge with SARS-CoV-2 XBB.1.5. In conclusion, NTD-RBD bsAbs offer promising potential for the design of resilient, next-generation antibody therapeutics against SARS-CoV-2 VOCs.
External linksSci Transl Med / PubMed:40043139
MethodsEM (single particle)
Resolution2.8 - 3.4 Å
Structure data

44627

9bj2

EMDB-44627, PDB-9bj2:
Structure of the SARS-CoV-2 S 6P trimer complex with the human neutralizing antibody Fab fragment, C1533 (local refinement of NTD and C1533)
Method: EM (single particle) / Resolution: 2.8 Å

44628

9bj3

EMDB-44628, PDB-9bj3:
Structure of the SARS-CoV-2 S 6P trimer complex with the human neutralizing antibody Fab fragment, C1596
Method: EM (single particle) / Resolution: 3.04 Å

44629

9bj4

EMDB-44629, PDB-9bj4:
Structure of the SARS-CoV-2 S 6P trimer complex with the human neutralizing antibody Fab fragment, C952
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / ANTIVIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex / SARS-CoV-2 / Antibody

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