ArticleInternational archives of allergy and immunology2013
Ara h 2 and Ara h 6 have similar allergenic activity and are substantially redundant.
Article in International archives of allergy and immunology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 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
- Research Advancements in Peanut Proteins, Their Allergenic Potentials, and the Approaches to Mitigate Peanut Allergenicity.Nutrients · 2025Review
- 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
- Biological activity of human IgE monoclonal antibodies targeting Der p 2, Fel d 1, Ara h 2 in basophil mediator release assays.Frontiers in immunology · 2023Article
- The Effector Function of Allergens.Frontiers in allergy · 2022Review
- Ara h 2 is the dominant peanut allergen despite similarities with Ara h 6.The Journal of allergy and clinical immunology · 2020Article
- Could This Be IT? Epicutaneous, Sublingual, and Subcutaneous Immunotherapy for the Treatment of Food Allergies.Current allergy and asthma reports · 2019Review
- Human monoclonal antibodies to Ara h 2 inhibit allergen-induced, IgE-mediated cell activation.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2019Article
- A cashew specific monoclonal antibody recognizing the small subunit of Ana o 3.Toxicology reports · 2019Article
- 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 IgE epitopes of peanut allergens Ara h 2 and Ara h 6.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 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
- The molecular basis of peanut allergy.Current allergy and asthma reports · 2014Article
- Cross-reactivity of peanut allergens.Current allergy and asthma reports · 2014Review
- Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut.Journal of agricultural and food chemistry · 2014Article
- Developing therapies for peanut allergy.International archives of allergy and immunology · 2014Review
- Redefining the major peanut allergens.Immunologic research · 2013Review
- Peanut Allergy, Allergen Composition, and Methods of Reducing Allergenicity: A Review.International journal of food science · 2013Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
backgroundThe moderately homologous (approx. 60%) proteins Ara h 2 and Ara h 6 are the most potent peanut allergens. This study was designed to define the relative individual contributions of Ara h 2 and Ara h 6 to the overall allergenic activity of a crude peanut extract (CPE).
methodsAra h 2 and Ara h 6 were removed from CPE by gel filtration chromatography. Ara h 2.01, Ara h 2.02 and Ara h 6 were further purified (>99%). The potency of each allergen and the ability of these allergens to reconstitute the allergenic activity of CPE depleted of Ara h 2 and Ara h 6 was measured with RBL SX-38 cells sensitized with IgE from sensitized peanut allergic patients.
resultsThe potency of the native proteins were significantly different (p < 0.0001) although not dramatically so, with a rank order of Ara h 2.01 > Ara h 2.02 > Ara h 6. The addition of either purified Ara h 2 or Ara h 6 independently at their original concentration to CPE depleted of both Ara h 2 and Ara h 6 restored 80-100% of the original CPE allergenic activity. Addition of both Ara h 2 and Ara h 6 consistently completely restored the allergenic activity of CPE.
conclusionsThese studies indicate that either Ara h 2 or Ara h 6 independently can account for most of the allergenic activity in a CPE and demonstrate important redundancy in the allergenic activity of these related molecules.
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