ArticleClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology2020
Identification of the amino-terminal fragment of Ara h 1 as a major target of the IgE-binding activity in the basic peanut protein fraction.
Article in Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- Linear and conformational epitopes of vicilin-buried peptides as a model for improved nut allergy diagnostics.Frontiers in allergy · 2025Article
- Legume Allergens Pea, Chickpea, Lentil, Lupine and Beyond.Current allergy and asthma reports · 2024Review
- 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
- Structure and IgE Cross-Reactivity among Cashew, Pistachio, Walnut, and Peanut Vicilin-Buried Peptides.Journal of agricultural and food chemistry · 2023Article
- Structure, Immunogenicity, and IgE Cross-Reactivity among Walnut and Peanut Vicilin-Buried Peptides.Journal of agricultural and food chemistry · 2022Article
- Identification of vicilin, legumin and antimicrobial peptide 2a as macadamia nut allergens.Food chemistry · 2022Article
- Article
- Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens.Journal of visualized experiments : JoVE · 2021Article
- Abundance and Stability as Common Properties of Allergens.Frontiers in allergy · 2021Review
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 4 countries.
Funding
Abstract
backgroundSmall, basic peanut proteins are often poorly extracted in pH-neutral buffers that are optimal for the extraction of peanut storage proteins such as Ara h 1. As a result, such proteins are easily missed as potential allergens.
objectiveTo analyse the allergenic composition of the basic peanut protein (BPP) fraction.
methodsA peanut extract prepared at pH 4 was fractionated by physicochemical procedures. Chemical analysis was performed by SDS-PAGE and mass spectrometry. Because immunoblotting was found to be inefficient for most of these small basic proteins, IgE-binding activity was measured by coupling the fractions to CNBr-activated Sepharose, followed by incubation with sera from 55 Dutch peanut-allergic children and
resultsMost IgE reactivity of the BPP fraction was due to the 5-7 kDa amino-terminal fragment of Ara h 1. This finding was confirmed by the use of the fragment in recombinant form, to which 25/55 of the sera was IgE-positive.
conclusionThe amino-terminal fragment of Ara h 1, a member of a family of small anti-microbial proteins, is an allergen independent of the carboxy-terminal fragment of Ara h 1.
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