ArticleCellular & molecular immunology2016
Development of an antibody that neutralizes soluble IgE and eliminates IgE expressing B cells.
Article in Cellular & molecular immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 54 citations in OpenAlex.
- Therapeutic Applications of Immunobiologics in Autoimmune and Inflammatory Diseases.Pharmaceutics · 2026Review
- Inflammatory memory: the core mechanism driving allergic asthma recurrence and chronicity.Journal of thoracic disease · 2026Review
- Reduction of circulating IgE and allergens by a pH-sensitive antibody with enhanced FcγRIIb binding.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- Single-Domain Antibodies-Novel Tools to Study and Treat Allergies.International journal of molecular sciences · 2024Review
- Mast cell stabilizers: from pathogenic roles to targeting therapies.Frontiers in immunology · 2024Review
- Article
- Sustained silencing peanut allergy by xanthopurpurin is associated with suppression of peripheral and bone marrow IgE-producing B cell.Frontiers in immunology · 2024Article
- EDIII-Fc induces protective immune responses against the Zika virus in mice and rhesus macaque.PLoS neglected tropical diseases · 2023Article
- Research Advances in Mast Cell Biology and Their Translation Into Novel Therapies for Anaphylaxis.The journal of allergy and clinical immunology. In practice · 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
- Relevance of Fc Gamma Receptor Polymorphisms in Cancer Therapy With Monoclonal Antibodies.Frontiers in oncology · 2022Review
- Bispecific T-Cell Engagers Targeting Membrane-Bound IgE.Biomedicines · 2021Article
- Effectiveness and Response Predictors of Omalizumab in Treating Patients with Seasonal Allergic Rhinitis: A Real-World Study.Journal of asthma and allergy · 2021Article
- Anti-Inflammatory Properties and Gut Microbiota Modulation ofAntioxidants (Basel, Switzerland) · 2020Article
- Past, present, and future of anti-IgE biologics.Allergy · 2020Review
- Der p 1-based immunotoxin as potential tool for the treatment of dust mite respiratory allergy.Scientific reports · 2020Article
- The Expression and Function of CD300 Molecules in the Main Players of Allergic Responses: Mast Cells, Basophils and Eosinophils.International journal of molecular sciences · 2020Review
- The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab.Nature communications · 2020Article
- Targeting the FcεRI Pathway as a Potential Strategy to Prevent Food-Induced Anaphylaxis.Frontiers in immunology · 2020Review
- Review
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immunoglobulin E (IgE) plays a key role in allergic asthma and is a clinically validated target for monoclonal antibodies. Therapeutic anti-IgE antibodies block the interaction between IgE and the Fc epsilon (Fcε) receptor, which eliminates or minimizes the allergic phenotype but does not typically curtail the ongoing production of IgE by B cells. We generated high-affinity anti-IgE antibodies (MEDI4212) that have the potential to both neutralize soluble IgE and eliminate IgE-expressing B-cells through antibody-dependent cell-mediated cytotoxicity. MEDI4212 variants were generated that contain mutations in the Fc region of the antibody or alterations in fucosylation in order to enhance the antibody's affinity for FcγRIIIa. All MEDI4212 variants bound to human IgE with affinities comparable to the wild-type (WT) antibody. Each variant was shown to inhibit the interaction between IgE and FcεRI, which translated into potent inhibition of FcγRI-mediated function responses. Importantly, all variants bound similarly to IgE at the surface of membrane IgE expressing cells. However, MEDI4212 variants demonstrated enhanced affinity for FcγRIIIa including the polymorphic variants at position 158. The improvement in FcγRIIIa binding led to increased effector function in cell based assays using both engineered cell lines and class switched human IgE B cells. Through its superior suppression of IgE, we anticipate that effector function enhanced MEDI4212 may be able to neutralize high levels of soluble IgE and provide increased long-term benefit by eliminating the IgE expressing B cells before they differentiate and become IgE secreting plasma cells.
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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.