ArticleNature communications2021
Multivalency transforms SARS-CoV-2 antibodies into ultrapotent neutralizers.
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Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46citing papers in PubMed
4.0field-weighted citation impact, top 5% of its field
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Who cites it
46 citing papers in PubMed, 75 citations in OpenAlex.
- Human antibody targeting of coronavirus spike S2 subunit is associated with protection mediated by Fc effector functions.Journal of virology · 2025Article
- Engineering a multivalent antibody nanoparticle to overcome SARS-CoV-2 Omicron immune evasion.PLoS pathogens · 2025Article
- Characterization of Nanobody Binding to Distinct Regions of the SARS-CoV-2 Spike Protein by Flow Virometry.Viruses · 2025Article
- Persistence and decay of neutralizing antibody responses elicited by SARS-CoV-2 infection and hybrid immunity in a Canadian cohort.Microbiology spectrum · 2025Article
- Targeting Bottlenecks in Malaria Transmission: Antibody-Epitope Descriptions Guide the Design of Next-Generation Biomedical Interventions.Immunological reviews · 2025Review
- Structural basis of different neutralization capabilities of monoclonal antibodies against H7N9 virus.Journal of virology · 2025Article
- Affinity maturation endows potent activity onto class 6 SARS-CoV-2 broadly neutralizing antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Target-mediated drug disposition model for drugs with N > 2 binding sites that bind to a target with one binding site.Journal of pharmacokinetics and pharmacodynamics · 2024Article
- General quasi-equilibrium multivalent binding model to study diverse and complex drug-receptor interactions of biologics.Journal of pharmacokinetics and pharmacodynamics · 2024Article
- Protein Cage Directed Assembly of Binary Nanoparticle Superlattices.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Computational design of non-porous pH-responsive antibody nanoparticles.Nature structural & molecular biology · 2024Article
- Applying Flow Virometry to Study the HIV Envelope Glycoprotein and Differences Across HIV Model Systems.Viruses · 2024Article
- Avidity engineering of human heavy-chain-only antibodies mitigates neutralization resistance of SARS-CoV-2 variants.Frontiers in immunology · 2023Article
- Exploring the Structural Variability of Dynamic Biological Complexes by Single-Particle Cryo-Electron Microscopy.Micromachines · 2022Review
- ACE2 decoy receptor generated by high-throughput saturation mutagenesis efficiently neutralizes SARS-CoV-2 and its prevalent variants.Emerging microbes & infections · 2022Article
- Engineering Self-Assembling Protein Nanoparticles for Therapeutic Delivery.Bioconjugate chemistry · 2022Review
- Critical parameters for design and development of multivalent nanoconstructs: recent trends.Drug delivery and translational research · 2022Review
- Multivalent ACE2 engineering-A promising pathway for advanced coronavirus nanomedicine development.Nano today · 2022Review
- Native, engineered and de novo designed ligands targeting the SARS-CoV-2 spike protein.Biotechnology advances · 2022Review
- SARS-CoV-2 Delta and Omicron variants evade population antibody response by mutations in a single spike epitope.Nature microbiology · 2022Article
Corrections and comments
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Authors and funding
26 authors at 4 institutions in 2 countries.
Edurne RujasProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Iga KucharskaProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Yong Zi TanProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.ORCID http://orcid.org/0000-0001-6656-6320
Samir BenlekbirProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Hong CuiProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Tiantian ZhaoDepartment of Immunology, University of Toronto, Toronto, ON, Canada.
Gregory A WasneyProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Patrick BudylowskiCombined Containment Level 3 Unit, University of Toronto, Toronto, ON, Canada.
Furkan GuvencCombined Containment Level 3 Unit, University of Toronto, Toronto, ON, Canada.
Jocelyn C NewtonProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Taylor SicardProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Anthony SemesiProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Krithika MuthuramanProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Amy NouanesengsyProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Clare Burn AschnerProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.ORCID http://orcid.org/0000-0001-8940-5423
Katherine PrietoProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Stephanie A BuelerProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Sawsan YoussefDistributed Bio, South San Francisco, CA, USA.
Sindy Liao-ChanDistributed Bio, South San Francisco, CA, USA.
Jacob GlanvilleDistributed Bio, South San Francisco, CA, USA.
Natasha Christie-HolmesCombined Containment Level 3 Unit, University of Toronto, Toronto, ON, Canada.
Samira MubarekaDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Scott D Gray-OwenDepartment of Molecular Genetics, University of Toronto, Toronto, ON, Canada.ORCID http://orcid.org/0000-0002-1477-3616
John L RubinsteinProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada.ORCID http://orcid.org/0000-0003-0566-2209
Bebhinn TreanorDepartment of Immunology, University of Toronto, Toronto, ON, Canada.ORCID http://orcid.org/0000-0002-8626-5944
Jean-Philippe JulienProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, Canada. jean-philippe.julien@sickkids.ca.ORCID http://orcid.org/0000-0001-7602-3995
Hospital for Sick Children · CAUniversity of Toronto · CASunnybrook Health Science Centre · CAUniversity of the Basque Country · ES
Funding
High-Speed High-Sensitivity Detector for X-ray Micro-Crystallography at GM/CA@APSS10OD012289 · OD · UNIVERSITY OF CHICAGO · PI FISCHETTI, ROBERT F. · 2014 to 2014
$2.0MNIAID NIH HHS HHSN272201400008CNIH HHS S10 OD012289
Abstract
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
Indexed as
AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralAntibody SpecificityApoferritinsBiological AvailabilityEpitope MappingHumansImmunoglobulin GMaleMiceMice, Inbred BALB CMice, Inbred C57BLProtein EngineeringProtein SubunitsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralApoferritinsImmunoglobulin GProtein SubunitsSpike Glycoprotein, Coronavirus
Identifiers
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LicenceCC BY
Read underepoch 390
Registered trials
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.