ArticleJournal of agricultural and food chemistry2014
Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut.
Article in Journal of agricultural and food chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- 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
- Impact of recombinant expression inFrontiers in immunology · 2025Article
- Evaluating clinical importance of sensitization to Ara h 6 quantitively in Japanese children.The World Allergy Organization journal · 2024Article
- Viral Vector Based Immunotherapy for Peanut Allergy.Viruses · 2024Review
- Defining the cross-reactivity between peanut allergens Ara h 2 and Ara h 6 using monoclonal antibodies.Clinical and experimental immunology · 2024Article
- Development of a mini pig model of peanut allergy.Frontiers in allergy · 2024Article
- 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
- Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies.Antioxidants (Basel, Switzerland) · 2023Review
- Changes in Serum Protein-Peptide Patterns in Atopic Children Allergic to Plant Storage Proteins.International journal of molecular sciences · 2023Article
- Immunodominant conformational and linear IgE epitopes lie in a single segment of Ara h 2.The Journal of allergy and clinical immunology · 2022Article
- 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
- Molecular evolution of genes encoding allergen proteins in the peanuts genus Arachis: Structural and functional implications.PloS one · 2019Article
- Determination of Crucial Immunogenic Epitopes in Major Peanut Allergy Protein, Ara h2, via Novel Nanoallergen Platform.Scientific reports · 2017Article
- Is peanut causing food allergy in Cuba? Preliminary assessment of allergic sensitization and IgE specificity profile to peanut allergens in Cuban allergic patients.The World Allergy Organization journal · 2017Article
- Heat processing of peanut seed enhances the sensitization potential of the major peanut allergen Ara h 6.Molecular nutrition & food research · 2016Article
- Mono-sensitisation to peanut component Ara h 6: a case series of five children and literature review.European journal of pediatrics · 2016Review
- Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity.Scientific reports · 2016Article
- Epitope analysis of Ara h 2 and Ara h 6: characteristic patterns of IgE-binding fingerprints among individuals with similar clinical histories.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2015Article
- Peanut sensitization pattern in Norwegian children and adults with specific IgE to peanut show age related differences.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2015Article
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Authors and funding
8 authors.
Funding
Abstract
The similarities of two major peanut allergens, Ara h 2 and Ara h 6, in molecular size, amino acid sequence, and structure have made it difficult to obtain natural Ara h 6 free of Ara h 2. The objectives of this study were to purify natural Ara h 6 that is essentially free of Ara h 2 and to compare its IgE reactivity and potency in histamine release assays to Ara h 2. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the highly purified allergen (<0.01% Ara h 2) revealed a single 14.5 kD band, and the identity of Ara h 6 was confirmed by liquid chromatography-tandem mass spectrometry. Ara h 6 showed a higher seroprevalence in chimeric IgE enzyme-linked immunosorbent assay (n = 54) but a weaker biological activity in basophil histamine release assays than Ara h 2. Purified Ara h 6 will be useful for diagnostic IgE antibody assays as well as molecular and cellular studies to investigate the immunological mechanisms of peanut allergy.
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