ArticleClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology2016
Conformational IgE epitopes of peanut allergens Ara h 2 and Ara h 6.
Article in Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 58 citations in OpenAlex.
- Variable IgE cross-reactivity between peanut 2S-albumins: The case for measuring IgE to both Ara h 2 and Ara h 6.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2019Trial
- Microbial fermentation as a strategy for the abatement of peanut allergens.Applied and environmental microbiology · 2026Review
- Oral and Skin Sensitisation to Peanut Show Different Immunological Features in Brown Norway Rats.Scandinavian journal of immunology · 2025Article
- Research Advancements in Peanut Proteins, Their Allergenic Potentials, and the Approaches to Mitigate Peanut Allergenicity.Nutrients · 2025Review
- Epitope-Specific Antibodies in Allergic Disease and Clinical Tolerance.Immunological reviews · 2025Review
- Characterization of IgE cross-reactivity and allergenicity of peanut allergens.ImmunoHorizons · 2025Article
- Investigation of Co-Assembly of Peanut Protein and Rice Protein: Effects on Protein Conformation and Immunoglobulin E Binding Capacity.Foods (Basel, Switzerland) · 2025Article
- Linear and conformational epitopes of vicilin-buried peptides as a model for improved nut allergy diagnostics.Frontiers in allergy · 2025Article
- Impact of recombinant expression inFrontiers in immunology · 2025Article
- Pollen-Food Allergy Syndrome: From Food Avoidance to Deciphering the Potential Cross-Reactivity between Pru p 3 and Ole e 7.Nutrients · 2024Article
- Special Issue "Molecular and Cellular Advances in Atopic Diseases".International journal of molecular sciences · 2024Article
- Precision engineering for localization, validation, and modification of allergenic epitopes.The Journal of allergy and clinical immunology · 2024Review
- 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
- The updated Structural Database of Allergenic Proteins (SDAP 2.0) provides 3D models for allergens and incorporated bioinformatics tools.The journal of allergy and clinical immunology. Global · 2023Article
- 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
- Targeting type 2 immunity and the future of food allergy treatment.The Journal of experimental medicine · 2023Review
- Peanut Allergenicity: An Insight into Its Mitigation Using Thermomechanical Processing.Foods (Basel, Switzerland) · 2023Review
- Immunodominant conformational and linear IgE epitopes lie in a single segment of Ara h 2.The Journal of allergy and clinical immunology · 2022Article
- The Effector Function of Allergens.Frontiers in allergy · 2022Review
- 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
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundCross-linking of IgE antibody by specific epitopes on the surface of mast cells is a prerequisite for triggering symptoms of peanut allergy. IgE epitopes are frequently categorized as linear or conformational epitopes. Although linear IgE-binding epitopes of peanut allergens have been defined, little is known about conformational IgE-binding epitopes.
objectiveTo identify clinically relevant conformational IgE epitopes of the two most important peanut allergens, Ara h 2 and Ara h 6, using phage peptide library.
methodsA phage 12mer peptide library was screened with allergen-specific IgE from 4 peanut-allergic patients. Binding of the mimotopes to IgE from a total of 29 peanut-allergic subjects was measured by ELISA. The mimotope sequences were mapped on the surface areas of Ara h 2 and Ara h 6 using EpiSearch.
resultsForty-one individual mimotopes were identified that specifically bind anti- Ara h 2/Ara h 6 IgE as well as rabbit anti-Ara h 2 and anti-Ara h 6 IgG. Sequence alignment showed that none of the mimotope sequences match a linear segment of the Ara h 2 or Ara h 6 sequences. EpiSearch analysis showed that all the mimotopes mapped to surface patches of Ara h 2 and Ara h 6. Eight of the mimotopes were recognized by more than 90% of the patients, suggesting immunodominance. Each patient had distinct IgE recognition patterns but the recognition frequency was not correlated to the concentration of peanut specific IgE or to clinical history.
conclusionsThe mimotopes identified in this study represent conformational epitopes. Identification of similar surface patches on Ara h 2 and Ara h 6 further underscores the similarities between these two potent allergens.
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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.