ArticleThe Journal of allergy and clinical immunology2022
Immunodominant conformational and linear IgE epitopes lie in a single segment of Ara h 2.
Article in The Journal of allergy and clinical immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT02192866 (Blood Samples for the Study of Peanut, Tree Nut and Other Food Allergies), which is not on this map. Cited by 19 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Blood Samples for the Study of Peanut, Tree Nut and Other Food Allergies
Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.
- Current utilization trend of immortalized mast cell lines in allergy research: a systematic review.Immunologic research · 2025Pooled it
- Advances in Food Processing Techniques for Allergenicity Reduction and Allergen Identification.Foods (Basel, Switzerland) · 2025Review
- Phenylglyoxal-induced Ana o 3 Modification Reduces Antibody Binding with Minimal Alteration in Protein Structure.Journal of agricultural and food chemistry · 2025Article
- Fine resolution of the N-terminal IgE-binding epitope of Ara h 2: Discovery of variants with enhanced IgE binding.The Journal of allergy and clinical immunology · 2025Article
- Epitope-Specific Antibodies in Allergic Disease and Clinical Tolerance.Immunological reviews · 2025Review
- Heating Differentiates Pecan Allergen Stability: Car i 4 Is More Heat Labile Than Car i 1 and Car i 2.Food science & nutrition · 2025Article
- Impact of recombinant expression inFrontiers in immunology · 2025Article
- Pre-clinical allergenicity assessment of IgE epitope-targeted Der p 2 mutants demonstrate potential as hypoallergenic AIT candidates.Frontiers in immunology · 2025Article
- The Potential of Human Monoclonal IgE Antibodies to Establish Biological Potency and Stability of Allergen Extracts.Current allergy and asthma reports · 2024Review
- Isolation, Characterization and IgE Binding of Two 2S Albumins of Pomegranate Seeds.Foods (Basel, Switzerland) · 2024Article
- 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
- Feast for thought: A comprehensive review of food allergy 2021-2023.The Journal of allergy and clinical immunology · 2024Review
- Widespread monoclonal IgE antibody convergence to an immunodominant, proanaphylactic Ara h 2 epitope in peanut allergy.The Journal of allergy and clinical immunology · 2024Article
- Design of an Ara h 2 hypoallergen from conformational epitopes.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2024Article
- Alanine Scanning of the Unstructured Region of Ara h 2 and of a Related Mimotope Reveals Critical Amino Acids for IgE Binding.Molecular nutrition & food research · 2023Article
- IgE cross-inhibition between Ara h 1 and Ara h 2 is explained by complex formation of both major peanut allergens.The Journal of allergy and clinical immunology · 2023Article
- Immunotherapy-induced neutralizing antibodies disrupt allergen binding and sustain allergen tolerance in peanut allergy.The Journal of clinical investigation · 2023Article
- IgE and IgG4 epitopes of the peanut allergens shift following oral immunotherapy.Frontiers in allergy · 2023Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundContribution of conformational epitopes to the IgE reactivity of peanut allergens Ara h 2 and Ara h 6 is at least as important as that of the linear epitopes. However, little is known about these conformational IgE-binding epitopes.
objectiveWe investigated the distribution of conformational epitopes on chimeric 2S-albumins.
methodsRecombinant chimeras were generated by exchanging structural segments between Ara h 2 and Ara h 6. Well-refolded chimeras, as verified by circular dichroism analysis, were then used to determine the epitope specificity of mAbs by performing competitive inhibition of IgG binding. Furthermore, we delineated the contribution of each segment to the overall IgE reactivity of both 2S-albumins by measuring the chimeras' IgE-binding capacity with sera from 21 patients allergic to peanut. We finally assessed chimeras' capacity to trigger mast cell degranulation.
resultsConfiguration of the conformational epitopes was preserved in the chimeras. Mouse IgG mAbs, raised against natural Ara h 6, and polyclonal human IgE antibodies recognized different conformational epitopes distributed all along Ara h 6. In contrast, we identified human IgG mAbs specific to different Ara h 2 linear or conformational epitopes located in all segments except the C-terminal one. The major conformational IgE-binding epitope of Ara h 2 was located in a segment located between residues 33 and 81 that also contains the major linear hydroxyproline-containing epitope. Accordingly, this segment is critical for the capacity of Ara h 2 to induce mast cell degranulation.
conclusionsChimeric 2S-albumins provide new insights on the conformational IgE-binding epitopes of Ara h 2 and Ara h 6. Proximity of the immunodominant linear and conformational IgE-binding epitopes probably contributes to the high allergenic potency of Ara h 2.
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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.