ArticleeLife2021
Highly synergistic combinations of nanobodies that target SARS-CoV-2 and are resistant to escape.
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Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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49citing papers in PubMed
3.8field-weighted citation impact, top 5% of its field
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Who cites it
49 citing papers in PubMed, 70 citations in OpenAlex.
- Article
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- High-Resolution Quantification of Two-Way Nanobody Synergy Using Automated Liquid Handling and Computational Modeling.Bio-protocol · 2026Article
- Multivalent Protein Nanorings for Broad and Potent SARS-CoV-2 Neutralization.Advanced healthcare materials · 2026Article
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- Spike conformational and glycan heterogeneity associated with furin cleavage causes incomplete neutralization of SARS-CoV-2.Nature communications · 2025Article
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- Unique mechanisms to increase structural stability and enhance antigen binding in nanobodies.Structure (London, England : 1993) · 2025Article
- Nanobody engineering: computational modelling and design for biomedical and therapeutic applications.FEBS open bio · 2025Review
- Production of Plant Virus-Derived Hybrid Nanoparticles Decorated with Different Nanobodies.ACS nano · 2024Article
- Nanobodies: From High-Throughput Identification to Therapeutic Development.Molecular & cellular proteomics : MCP · 2024Review
- Article
- Discovery of nanobodies: a comprehensive review of their applications and potential over the past five years.Journal of nanobiotechnology · 2024Review
- Suppressing the background of LC-ESI-MS analysis of permethylated glycans using the active background ion reduction device.Electrophoresis · 2024Article
- Broad sarbecovirus neutralization by combined memory B cell antibodies to ancestral SARS-CoV-2.iScience · 2024Article
Corrections and comments
- Update of
Authors and funding
29 authors at 7 institutions in 1 country.
Fred D Mast *Center for Global Infectious Disease Research, Seattle Children's Research Institute, Seattle, United States.ORCID https://orcid.org/0000-0002-2177-6647
Peter C Fridy *Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, United States.ORCID https://orcid.org/0000-0002-8208-9154
Natalia E Ketaren *Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, United States.ORCID https://orcid.org/0000-0002-7869-6162
Junjie Wang *Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, United States.
Erica Y Jacobs *Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, United States.ORCID https://orcid.org/0000-0002-5018-0711
Jean Paul Olivier *Center for Global Infectious Disease Research, Seattle Children's Research Institute, Seattle, United States.ORCID https://orcid.org/0000-0002-2197-271X
Tanmoy SanyalDepartment of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, United States.ORCID https://orcid.org/0000-0002-6009-9431
Kelly R MolloyLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, United States.
Fabian SchmidtLaboratory of Retrovirology, The Rockefeller University, New York, United States.
Magdalena RutkowskaLaboratory of Retrovirology, The Rockefeller University, New York, United States.
Yiska WeisblumLaboratory of Retrovirology, The Rockefeller University, New York, United States.ORCID https://orcid.org/0000-0002-9249-1745
Lucille M RichCenter for Immunity and Immunotherapies, Seattle Children's Research Institute, Seattle, United States.
Elizabeth R VanderwallCenter for Immunity and Immunotherapies, Seattle Children's Research Institute, Seattle, United States.
Nicholas DambrauskasCenter for Global Infectious Disease Research, Seattle Children's Research Institute, Seattle, United States.
Vladimir VigdorovichCenter for Global Infectious Disease Research, Seattle Children's Research Institute, Seattle, United States.ORCID https://orcid.org/0000-0003-4195-4858
Sarah KeeganInstitute for Systems Genetics and Department of Biochemistry and Molecular Pharmacology, NYU Grossman School of Medicine, New York, United States.
Jacob B JilerLaboratory of Cellular and Structural Biology, The Rockefeller University, New York, United States.ORCID https://orcid.org/0000-0002-4566-6098
Milana E SteinLaboratory of Cellular and Structural Biology, The Rockefeller University, New York, United States.
Paul Dominic B OlinaresLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, United States.ORCID https://orcid.org/0000-0002-3429-6618
Louis HerlandsAbOde Therapeutics Inc, Woods Hole, United States.
Theodora HatziioannouLaboratory of Retrovirology, The Rockefeller University, New York, United States.
D Noah SatherCenter for Global Infectious Disease Research, Seattle Children's Research Institute, Seattle, United States.ORCID https://orcid.org/0000-0002-9128-172X
Jason S DebleyCenter for Immunity and Immunotherapies, Seattle Children's Research Institute, Seattle, United States.
David FenyöInstitute for Systems Genetics and Department of Biochemistry and Molecular Pharmacology, NYU Grossman School of Medicine, New York, United States.ORCID https://orcid.org/0000-0001-5049-3825
Andrej SaliDepartment of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, United States.ORCID https://orcid.org/0000-0003-0435-6197
Paul D BieniaszLaboratory of Retrovirology, The Rockefeller University, New York, United States.ORCID https://orcid.org/0000-0002-2368-3719
John D AitchisonCenter for Global Infectious Disease Research, Seattle Children's Research Institute, Seattle, United States.ORCID https://orcid.org/0000-0002-9153-6497
Brian T ChaitLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, United States.ORCID https://orcid.org/0000-0003-3524-557X
Michael P RoutLaboratory of Cellular and Structural Biology, The Rockefeller University, New York, United States.ORCID https://orcid.org/0000-0003-2010-706X
Rockefeller University · USInfectious Disease Research Institute · USInstitute for Systems Biology · USQB3 · USHoward Hughes Medical Institute · USSeattle Children's Hospital · USSt. John's School · US
Funding
TR&D Project 4. The Imaging Stage: Multiscale Spatiotemporal Modeling of Macromolecular Systems in Cellular NeighborhoodsP41GM109824 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2014 to 2023
$18.8MOvercoming Host Restriction Factors to Develop Better Animal Models for HIV/AIDS.R01AI078788 · NIAID · ROCKEFELLER UNIVERSITY · PI HATZIIOANNOU, THEODORA · 2008 to 2021
$9.3MRegulation of the Innate Immune Response by the Epithelium in AsthmaU19AI125378 · NIAID · BENAROYA RESEARCH INST AT VIRGINIA MASON · PI HALLSTRAND, TEAL S · 2016 to 2020
$9.2MStructure-Function Mapping of the Nuclear Pore Complex-RenewalR01GM112108 · NIGMS · ROCKEFELLER UNIVERSITY · PI JOHN D. AITCHISON, MICHAEL P ROUT · 2015 to 2026
$9.1MSynergistic Nanobodies for Pandemic PreparednessR01AI189657 · NIAID · ROCKEFELLER UNIVERSITY · PI JOHN D. AITCHISON, MICHAEL P ROUT · 2025 to 2026
$1.7MImpact of Heterogeneous Airway Epithelial ACE2 Expression and Interferon Responses on SARS-CoV2 Infectivity and ReplicationK24AI150991 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI DEBLEY, JASON S · 2020 to 2024
$1.2MHoward Hughes Medical InstituteNIAID NIH HHS K24 AI150991NIAID NIH HHS R01 AI078788NIAID NIH HHS R01 AI189657NIAID NIH HHS U19 AI125378NIGMS NIH HHS P41 GM109824NIGMS NIH HHS R01 GM112108
Abstract
The emergence of SARS-CoV-2 variants threatens current vaccines and therapeutic antibodies and urgently demands powerful new therapeutics that can resist viral escape. We therefore generated a large nanobody repertoire to saturate the distinct and highly conserved available epitope space of SARS-CoV-2 spike, including the S1 receptor binding domain, N-terminal domain, and the S2 subunit, to identify new nanobody binding sites that may reflect novel mechanisms of viral neutralization. Structural mapping and functional assays show that indeed these highly stable monovalent nanobodies potently inhibit SARS-CoV-2 infection, display numerous neutralization mechanisms, are effective against emerging variants of concern, and are resistant to mutational escape. Rational combinations of these nanobodies that bind to distinct sites within and between spike subunits exhibit extraordinary synergy and suggest multiple tailored therapeutic and prophylactic strategies.
Indexed as
AnimalsAntibodies, NeutralizingAntibodies, ViralBinding SitesCamelids, New WorldCOVID-19EpitopesHEK293 CellsHumansMaleNeutralization TestsSARS-CoV-2Single-Domain AntibodiesSpike Glycoprotein, CoronavirusAntibodies, NeutralizingAntibodies, ViralEpitopesSingle-Domain AntibodiesSpike Glycoprotein, Coronavirushumaninfectious diseasemicrobiologynanobodiesSARS-CoV-2single-domain antibodiesspike glycoproteinsynergyvariants of concern
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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.