ArticleThe Journal of allergy and clinical immunology2024
Widespread monoclonal IgE antibody convergence to an immunodominant, proanaphylactic Ara h 2 epitope in peanut allergy.
Article in The Journal of allergy and clinical immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- Immunization with Virus-Like Particles Displaying Ara h 2‑Derived Peptides to Mitigate Peanut Allergy.ACS nano medicine · 2026Article
- Human monoclonal antibodies targeting α-Gal restrict IgE engagement of α-Gal syndrome allergens.The Journal of clinical investigation · 2026Article
- Magnetic Beads-Based Electrochemical Label-Free DNA-Bioassay for the Detection of Peanut Allergen Ara h2 in Food Matrices.Biosensors · 2026Article
- A Case for Anti-IgE Vaccination.Allergy · 2026Review
- Structural Basis for Trivalent Cross-Linking of a Patient-Derived IgE Antibody by the Major Peanut Allergen Ara h 2.0201.Allergy · 2026Article
- Mixed Signals: T Cells as Architects of IgE Immunity.Immunological reviews · 2026Review
- A Human Monoclonal Antibody Displays Promiscuous Binding to Multiple Type 1 nsLTP Allergens.Journal of investigational allergology & clinical immunology · 2026Article
- Allergen-specific human IgE isolated through an allergen-agnostic pipeline-understanding immune response and allergen recognition.Communications biology · 2026Article
- Efficacy of the 4 Subclasses of IgG for Interacting With CD32b/a on Human Basophils.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2025Article
- Epitope-Specific Antibodies in Allergic Disease and Clinical Tolerance.Immunological reviews · 2025Review
- Advances in Food Allergy Immunotherapy: Current Strategies and Role of Antibodies Isotypes.Cells · 2025Review
- Germline-encoded recognition of peanut underlies development of convergent antibodies in humans.Science translational medicine · 2025Article
- Structural determinants of peanut-induced anaphylaxis.The Journal of allergy and clinical immunology · 2025Article
- LuLIPLEX: A Fast, Highly Sensitive, and Multiplexed Method for the Detection of IgE Against Major Allergens.Allergy · 2025Article
- Emerging diagnostic and therapeutic opportunities in food allergy.Frontiers in immunology · 2025Review
- The Potential of Human Monoclonal IgE Antibodies to Establish Biological Potency and Stability of Allergen Extracts.Current allergy and asthma reports · 2024Review
- Defining the cross-reactivity between peanut allergens Ara h 2 and Ara h 6 using monoclonal antibodies.Clinical and experimental immunology · 2024Article
- Precision engineering for localization, validation, and modification of allergenic epitopes.The Journal of allergy and clinical immunology · 2024Review
- Article
- A human monoclonal antibody based immunoenzymetric assay to measure Fel d 1 concentrations in cat hair and pelt allergenic extracts.Frontiers in allergy · 2024Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundDespite their central role in peanut allergy, human monoclonal IgE antibodies have eluded characterization.
objectiveWe sought to define the sequences, affinities, clonality, and functional properties of human monoclonal IgE antibodies in peanut allergy.
methodsWe applied our single-cell RNA sequencing-based SEQ SIFTER discovery platform to samples from allergic individuals who varied by age, sex, ethnicity, and geographic location in order to understand commonalities in the human IgE response to peanut allergens. Select antibodies were then recombinantly expressed and characterized for their allergen and epitope specificity, affinity, and functional properties.
resultsWe found striking convergent evolution of IgE monoclonal antibodies (mAbs) from several clonal families comprising both memory B cells and plasmablasts. These antibodies bound with subnanomolar affinity to the immunodominant peanut allergen Ara h 2, specifically a linear, repetitive motif. Further characterization of these mAbs revealed their ability to single-handedly cause affinity-dependent degranulation of human mast cells and systemic anaphylaxis on peanut allergen challenge in humanized mice. Finally, we demonstrated that these mAbs, reengineered as IgGs, inhibit significant, but variable, amounts of Ara h 2- and peanut-mediated degranulation of mast cells sensitized with allergic plasma.
conclusionsConvergent evolution of IgE mAbs in peanut allergy is a common phenomenon that can reveal immunodominant epitopes on major allergenic proteins. Understanding the functional properties of these molecules is key to developing therapeutics, such as competitive IgG inhibitors, that are able to stoichiometrically outcompete endogenous IgE for allergen and thereby prevent allergic cascade in cases of accidental allergen exposure.
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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.