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TitleA multi-specific, multi-affinity antibody platform neutralizes sarbecoviruses and confers protection against SARS-CoV-2 in vivo.
Journal, issue, pagesSci Transl Med, Vol. 15, Issue 697, Page eadf4549, Year 2023
Publish dateMay 24, 2023
AuthorsClare Burn Aschner / Krithika Muthuraman / Iga Kucharska / Hong Cui / Katherine Prieto / Manoj S Nair / Maple Wang / Yaoxing Huang / Natasha Christie-Holmes / Betty Poon / Jessica Lam / Azmiri Sultana / Robert Kozak / Samira Mubareka / John L Rubinstein / Edurne Rujas / Bebhinn Treanor / David D Ho / Arif Jetha / Jean-Philippe Julien /
PubMed AbstractSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), has been responsible for a global pandemic. Monoclonal antibodies (mAbs) have ...Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), has been responsible for a global pandemic. Monoclonal antibodies (mAbs) have been used as antiviral therapeutics; however, these therapeutics have been limited in efficacy by viral sequence variability in emerging variants of concern (VOCs) and in deployment by the need for high doses. In this study, we leveraged the multi-specific, multi-affinity antibody (Multabody, MB) platform, derived from the human apoferritin protomer, to enable the multimerization of antibody fragments. MBs were shown to be highly potent, neutralizing SARS-CoV-2 at lower concentrations than their corresponding mAb counterparts. In mice infected with SARS-CoV-2, a tri-specific MB targeting three regions within the SARS-CoV-2 receptor binding domain was protective at a 30-fold lower dose than a cocktail of the corresponding mAbs. Furthermore, we showed in vitro that mono-specific MBs potently neutralize SARS-CoV-2 VOCs by leveraging augmented avidity, even when corresponding mAbs lose their ability to neutralize potently, and that tri-specific MBs expanded the neutralization breadth beyond SARS-CoV-2 to other sarbecoviruses. Our work demonstrates how avidity and multi-specificity combined can be leveraged to confer protection and resilience against viral diversity that exceeds that of traditional monoclonal antibody therapies.
External linksSci Transl Med / PubMed:37224226
MethodsEM (single particle) / X-ray diffraction
Resolution2.09 - 3.12 Å
Structure data

EMDB-28067: CryoEM reconstruction of tri-specific 298-52-80 Multabody (no symmetry applied)
Method: EM (single particle) / Resolution: 2.35 Å

EMDB-28068: CryoEM reconstruction of the tri-specific 298-52-80 Multabody (octahedral symmetry applied)
Method: EM (single particle) / Resolution: 2.09 Å

PDB-8dnn:
Crystal structure of neutralizing antibody 80 in complex with SARS-CoV-2 receptor binding domain
Method: X-RAY DIFFRACTION / Resolution: 3.12 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsIMMUNE SYSTEM/VIRAL PROTEIN / SARS-CoV-2 / ANTIBODY / VIRAL GLYCOPROTEIN / IMMUNE SYSTEM / IMMUNE SYSTEM-VIRAL PROTEIN complex

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