ArticleFrontiers in immunology2017
Bivalent Llama Single-Domain Antibody Fragments against Tumor Necrosis Factor Have Picomolar Potencies due to Intramolecular Interactions.
Article in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
55 citing papers in PubMed, 1 synthesis or guideline pooled it, 86 citations in OpenAlex.
- Research Progress and Applications of Multivalent, Multispecific and Modified Nanobodies for Disease Treatment.Frontiers in immunology · 2021Pooled it
- Long-term safety and efficacy of anti-TNF multivalent VHH antibodies ozoralizumab in patients with rheumatoid arthritis.RMD open · 2024Trial
- Phase II/III Results of a Trial of Anti-Tumor Necrosis Factor Multivalent NANOBODY Compound Ozoralizumab in Patients With Rheumatoid Arthritis.Arthritis & rheumatology (Hoboken, N.J.) · 2022Trial
- Peptide Aptamer-Enabled Nanoplasmonic Digital Immunoassay for Ultrasensitive Cytokine Sensing in Early Inflammation and Immune Modulation.ACS sensors · 2026Article
- Computational nanobody design using graph neural networks and Metropolis Monte Carlo sampling.Briefings in bioinformatics · 2026Article
- A yeast synthetic biotic platform for delivery of therapeutic nanobodies to ameliorate gastrointestinal inflammation.Disease models & mechanisms · 2026Article
- Article
- The structural basis for the selective antagonism of soluble TNF-alpha by shark variable new antigen receptors.Nature communications · 2025Article
- Design of minibinder proteins as universal antagonists against canine and human TNFα.Communications biology · 2025Article
- BoltzGen: Toward Universal Binder Design.bioRxiv : the preprint server for biology · 2025Article
- Identification of a nanobody able to catalyze the destruction of the spike-trimer of SARS-CoV-2.Frontiers of medicine · 2025Article
- Improving the production and stability of nanobodies.Protein engineering, design & selection : PEDS · 2025Article
- A molecular toolkit for heterologous protein secretion across Bacteroides species.Nature communications · 2024Article
- Single-domain antibodies as therapeutics for solid tumor treatment.Acta pharmaceutica Sinica. B · 2024Review
- Nanobodies in the fight against infectious diseases: repurposing nature's tiny weapons.World journal of microbiology & biotechnology · 2024Review
- Next-Generation Anti-TNFα Agents: The Example of Ozoralizumab.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2024Review
- Novel bispecific nanobody mitigates experimental intestinal inflammation in mice by targeting TNF-α and IL-23p19 bioactivities.Clinical and translational medicine · 2024Article
- A molecular toolkit for heterologous protein secretion acrossbioRxiv : the preprint server for biology · 2023Article
- Nanobody-based pannexin1 channel inhibitors reduce inflammation in acute liver injury.Journal of nanobiotechnology · 2023Article
- Co-administration of an effector antibody enhances the half-life and therapeutic potential of RNA-encoded nanobodies.Scientific reports · 2023Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activity of tumor necrosis factor (TNF), a cytokine involved in inflammatory pathologies, can be inhibited by antibodies or trap molecules. Herein, llama-derived variable heavy-chain domains of heavy-chain antibody (VHH, also called Nanobodies™) were generated for the engineering of bivalent constructs, which antagonize the binding of TNF to its receptors with picomolar potencies. Three monomeric VHHs (VHH#1, VHH#2, and VHH#3) were characterized in detail and found to bind TNF with sub-nanomolar affinities. The crystal structures of the TNF-VHH complexes demonstrate that VHH#1 and VHH#2 share the same epitope, at the center of the interaction area of TNF with its TNFRs, while VHH#3 binds to a different, but partially overlapping epitope. These structures rationalize our results obtained with bivalent constructs in which two VHHs were coupled
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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.