ArticlemAbs
A novel IgE-neutralizing antibody for the treatment of severe uncontrolled asthma.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The trial behind it
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
29 citing papers in PubMed, 52 citations in OpenAlex.
- Antibodies targeting a shared epitope exploit IgE allostery to drive distinct functional outcomes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Therapeutic Applications of Immunobiologics in Autoimmune and Inflammatory Diseases.Pharmaceutics · 2026Review
- Computational Procedure for Predicting Excipient Effects on Protein-Protein Affinities.Journal of chemical theory and computation · 2024Article
- Mast cell stabilizers: from pathogenic roles to targeting therapies.Frontiers in immunology · 2024Review
- New insights into the pathophysiology and therapeutic targets of asthma and comorbid chronic rhinosinusitis with or without nasal polyposis.Clinical science (London, England : 1979) · 2023Review
- Immunologic, genetic, and ecological interplay of factors involved in allergic diseases.Frontiers in allergy · 2023Review
- IgE-neutralizing UB-221 mAb, distinct from omalizumab and ligelizumab, exhibits CD23-mediated IgE downregulation and relieves urticaria symptoms.The Journal of clinical investigation · 2022Article
- Bispecific T-Cell Engagers Targeting Membrane-Bound IgE.Biomedicines · 2021Article
- Tuning IgE: IgE-Associating Molecules and Their Effects on IgE-Dependent Mast Cell Reactions.Cells · 2021Review
- Past, present, and future of anti-IgE biologics.Allergy · 2020Review
- Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab.Nature communications · 2020Article
- Phage Display Derived Monoclonal Antibodies: From Bench to Bedside.Frontiers in immunology · 2020Review
- Review
- Mast Cell-Mediated Orchestration of the Immune Responses in Human Allergic Asthma: Current Insights.Clinical reviews in allergy & immunology · 2019Review
- IgE Antibodies: From Structure to Function and Clinical Translation.Antibodies (Basel, Switzerland) · 2019Review
- Article
- Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody.Scientific reports · 2018Article
- Biologic agents for severe asthma patients: clinical perspectives and implications.Internal and emergency medicine · 2018Review
- Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction.Nature communications · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
26 authors at 7 institutions in 6 countries.
Funding
Abstract
The critical role played by IgE in allergic asthma is well-documented and clinically precedented, but some patients in whom IgE neutralization may still offer clinical benefit are excluded from treatment with the existing anti-IgE therapy, omalizumab, due to high total IgE levels or body mass. In this study, we sought to generate a novel high affinity anti-IgE antibody (MEDI4212) with potential to treat a broad severe asthma patient population. Analysis of body mass, total and allergen-specific IgE levels in a cohort of severe asthmatics was used to support the rationale for development of a high affinity IgE-targeted antibody therapeutic. Phage display technology was used to generate a human IgG1 lead antibody, MEDI4212, which was characterized in vitro using binding, signaling and functional assay systems. Protein crystallography was used to determine the details of the interaction between MEDI4212 and IgE. MEDI4212 bound human IgE with an affinity of 1.95 pM and was shown to target critical residues in the IgE Cε3 domain critical for interaction with FcεRI. MEDI4212 potently inhibited responses through FcεRI and also prevented the binding of IgE to CD23. When used ex vivo at identical concentration, MEDI4212 depleted free-IgE from human sera to levels ~1 log lower than omalizumab. Our results thus indicate that MEDI4212 is a novel, high affinity antibody that binds specifically to IgE and prevents IgE binding to its receptors. MEDI4212 effectively depleted free-IgE from human sera ex vivo to a level (1 IU/mL) anticipated to provide optimal IgE suppression in severe asthma patients.
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Registered trials
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.