ArticleClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology2015
Epitope analysis of Ara h 2 and Ara h 6: characteristic patterns of IgE-binding fingerprints among individuals with similar clinical histories.
Article in Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 70 citations in OpenAlex.
- Evolution of epitope-specific IgE and IgGThe Journal of allergy and clinical immunology · 2021Trial
- Development of a novel Ara h 2 hypoallergen with no IgE binding or anaphylactogenic activity.The Journal of allergy and clinical immunology · 2020Trial
- Ara h 7 isoforms share many linear epitopes: Are 3D epitopes crucial to elucidate divergent abilities?Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2019Trial
- 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
- Immunization with Virus-Like Particles Displaying Ara h 2‑Derived Peptides to Mitigate Peanut Allergy.ACS nano medicine · 2026Article
- 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
- 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
- Proteomic characterization of peanut flour fermented byHeliyon · 2024Article
- Defining the cross-reactivity between peanut allergens Ara h 2 and Ara h 6 using monoclonal antibodies.Clinical and experimental immunology · 2024Article
- Self-Assembling Allergen Vaccine Platform Raises Therapeutic Allergen-Specific IgG Responses without Induction of Systemic Allergic Responses.ACS biomaterials science & engineering · 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
- 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
- Peanut Allergenicity: An Insight into Its Mitigation Using Thermomechanical Processing.Foods (Basel, Switzerland) · 2023Review
- 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
- IgE and IgG4 Epitope Mapping of Food Allergens with a Peptide Microarray Immunoassay.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Unique allergen-specific human IgE monoclonal antibodies derived from patients with allergic disease.Frontiers in allergy · 2023Article
- Immunodominant conformational and linear IgE epitopes lie in a single segment of Ara h 2.The Journal of allergy and clinical immunology · 2022Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundAra h 2 and Ara h 6 are moderately homologous and highly potent peanut allergens.
objectiveTo identify IgE-binding linear epitopes of Ara h 6, compare them to those of Ara h 2, and to stratify binding based on clinical histories.
methodsThirty highly peanut-allergic subjects were stratified by clinical history. Sera were diluted to contain the same amount of anti-peanut IgE. IgE binding to overlapping 20-mer peptides of Ara h 2 and Ara h 6 was assessed using microarrays.
resultsEach subject had a unique IgE-binding fingerprint to peptides; these data were coalesced into epitope binding. IgE from subjects with a history of more severe reactions (n = 19) had a smaller frequency of binding events (BEs) for both Ara h 2 (52 BEs of 152 (19X8epitopes) possible BEs and Ara h 6 (13 BEs of 133 (19X7 epitopes) possible BEs) compared to IgE from those with milder histories (n = 11) (Ara h 2: 47 BEs of 88 (11X8 epitopes) possible BEs, P < 0.01; Ara h 6: 25 BEs of 77 (11X7 epitopes) possible BEs, P < 0.001). Using an unsupervised hierarchal cluster analysis, subjects with similar histories tended to cluster. We have tentatively identified a high-risk pattern of binding to peptides of Ara h 2 and Ara h 6, predominantly in subjects with a history of more severe reactions (OR = 12.6; 95% CI: 2.0-79.5; P < 0.01). CONCLUSIONS AND CLINICAL RELEVANCE: IgE from patients with more severe clinical histories recognize fewer linear epitopes of Ara h 2 and Ara h 6 than do subjects with milder reactions and bind these epitopes in characteristic patterns. Close examination of IgE binding to epitopes of Ara h 2 and Ara h 6 may have prognostic value.
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