Trial reportClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology2019
Variable IgE cross-reactivity between peanut 2S-albumins: The case for measuring IgE to both Ara h 2 and Ara h 6.
Trial report in Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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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
14 citing papers in PubMed, 26 citations in OpenAlex.
- The "Survivor Peptide" Hypothesis: Structural Resilience and Immunological Persistence of Food Allergens in the Gut-Mammary Axis.Nutrients · 2026Review
- Research Advancements in Peanut Proteins, Their Allergenic Potentials, and the Approaches to Mitigate Peanut Allergenicity.Nutrients · 2025Review
- Evaluating clinical importance of sensitization to Ara h 6 quantitively in Japanese children.The World Allergy Organization journal · 2024Article
- Defining the cross-reactivity between peanut allergens Ara h 2 and Ara h 6 using monoclonal antibodies.Clinical and experimental immunology · 2024Article
- A novel peanut allergy immunotherapy: Plant-based enveloped Ara h 2 Bioparticles activate dendritic cells and polarize T cell responses to Th1.The World Allergy Organization journal · 2023Article
- IgE+ plasmablasts predict the onset of clinical allergy.Frontiers in immunology · 2023Article
- Immunodominant conformational and linear IgE epitopes lie in a single segment of Ara h 2.The Journal of allergy and clinical immunology · 2022Article
- Real world use of peanut component testing among children in the Chicago metropolitan area.Allergy and asthma proceedings · 2022Article
- The Effector Function of Allergens.Frontiers in allergy · 2022Review
- Distinction between peanut allergy and tolerance by characterization of B cell receptor repertoires.Allergy · 2021Article
- Peanut components measured by ISAC: comparison with ImmunoCap and clinical relevance in peanut allergic children.Clinical and molecular allergy : CMA · 2021Article
- Diagnostic accuracy of Ara h 2 for detecting peanut allergy in children.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2021Article
- The importance of the 2S albumins for allergenicity and cross-reactivity of peanuts, tree nuts, and sesame seeds.The Journal of allergy and clinical immunology · 2021Review
- Ara h 2 is the dominant peanut allergen despite similarities with Ara h 6.The Journal of allergy and clinical immunology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
background2S-albumins Ara h 2 and Ara h 6 are the most potent peanut allergens and levels of specific immunoglobulin E (IgE) towards these proteins are good predictors of clinical reactivity. Because of structural homologies, Ara h 6 is generally considered to cross-react extensively with Ara h 2.
objectiveWe aimed to quantify the IgE cross-reactivity between Ara h 2 and Ara h 6.
methodsPeanut 2S-albumins were purified from raw peanuts. The IgE cross-reactivity between Ara h 2 and Ara h 6 was evaluated with 32 sera from French and US peanut-allergic patients by measuring the residual IgE-binding to one 2S-albumin after depletion of IgE antibodies recognizing the other 2S-albumin. The IgE cross-reactivity between Ara h 2 and Ara h 6 was further investigated by competitive inhibition of IgE-binding and by a model of mast cell degranulation.
resultsA highly variable level of IgE cross-reactivity was revealed among the patients. The mean fraction of cross-reactive IgE antibodies represented only 17.1% of 2S-albumins-specific IgE antibodies and was lower than the mean fraction of IgE specific to Ara h 2 (57.4%) or to Ara h 6 (25.5%). The higher level of Ara h 2-specific IgE was principally due to the IgE-binding capacity of an insertion containing the repeated immunodominant linear epitope DPYSP CONCLUSIONS & CLINICAL RELEVANCE: Immunoglobulin E antibodies specific to peanut 2S-albumins are mainly non-cross-reactive, but low-affinity cross-reactivity can affect diagnostic accuracy. Testing IgE-binding to a mixture of 2S-albumins rather than to each separately may enhance diagnostic performance.
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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.