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TitleMultivalency transforms SARS-CoV-2 antibodies into ultrapotent neutralizers.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 3661, Year 2021
Publish dateJun 16, 2021
AuthorsEdurne Rujas / Iga Kucharska / Yong Zi Tan / Samir Benlekbir / Hong Cui / Tiantian Zhao / Gregory A Wasney / Patrick Budylowski / Furkan Guvenc / Jocelyn C Newton / Taylor Sicard / Anthony Semesi / Krithika Muthuraman / Amy Nouanesengsy / Clare Burn Aschner / Katherine Prieto / Stephanie A Bueler / Sawsan Youssef / Sindy Liao-Chan / Jacob Glanville / Natasha Christie-Holmes / Samira Mubareka / Scott D Gray-Owen / John L Rubinstein / Bebhinn Treanor / Jean-Philippe Julien /
PubMed AbstractSARS-CoV-2, the virus responsible for COVID-19, has caused a global pandemic. Antibodies can be powerful biotherapeutics to fight viral infections. Here, we use the human apoferritin protomer as a ...SARS-CoV-2, the virus responsible for COVID-19, has caused a global pandemic. Antibodies can be powerful biotherapeutics to fight viral infections. Here, we use the human apoferritin protomer as a modular subunit to drive oligomerization of antibody fragments and transform antibodies targeting SARS-CoV-2 into exceptionally potent neutralizers. Using this platform, half-maximal inhibitory concentration (IC) values as low as 9 × 10 M are achieved as a result of up to 10,000-fold potency enhancements compared to corresponding IgGs. Combination of three different antibody specificities and the fragment crystallizable (Fc) domain on a single multivalent molecule conferred the ability to overcome viral sequence variability together with outstanding potency and IgG-like bioavailability. The MULTi-specific, multi-Affinity antiBODY (Multabody or MB) platform thus uniquely leverages binding avidity together with multi-specificity to deliver ultrapotent and broad neutralizers against SARS-CoV-2. The modularity of the platform also makes it relevant for rapid evaluation against other infectious diseases of global health importance. Neutralizing antibodies are a promising therapeutic for SARS-CoV-2.
External linksNat Commun / PubMed:34135340 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.95 - 6.2 Å
Structure data

EMDB-22738:
CryoEM reconstruction of SARS-CoV-2 receptor binding domain in complex with the Fab fragment of neutralizing antibody 46
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-22739:
CryoEM reconstruction of SARS-CoV-2 Spike in complex with the Fab fragment of neutralizing antibody 80.
Method: EM (single particle) / Resolution: 6.2 Å

EMDB-22740:
CryoEM reconstruction of SARS-CoV-2 Spike in complex with the Fab fragment of neutralizing antibody 298
Method: EM (single particle) / Resolution: 6.2 Å

EMDB-22741:
CryoEM reconstruction of SARS-CoV-2 Spike in complex with the Fab fragment of neutralizing antibody 324
Method: EM (single particle) / Resolution: 6.0 Å

PDB-7k9z:
Crystal structure of SARS-CoV-2 receptor binding domain in complex with the Fab fragments of neutralizing antibodies 298 and 52
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

Chemicals

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

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsIMMUNE SYSTEM / SARS-CoV-2 / Receptor Binding Domain / Neutralizing antibodies

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