ArticleThe Biochemical journal2006
Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
65 citing papers in PubMed, 228 citations in OpenAlex.
- Development of a novel Ara h 2 hypoallergen with no IgE binding or anaphylactogenic activity.The Journal of allergy and clinical immunology · 2020Trial
- 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
- Food-specific sublingual immunotherapy is well tolerated and safe in healthy dogs: a blind, randomized, placebo-controlled study.BMC veterinary research · 2017Trial
- Quinoa and Peanut Extracts as Alternatives to Animal-Derived Extracellular Matrix Proteins in Cultured Meat Production.Journal of food science · 2026Article
- A Review of Allergen Characteristics from Major Plant Allergenic Foods.Foods (Basel, Switzerland) · 2026Review
- The "Survivor Peptide" Hypothesis: Structural Resilience and Immunological Persistence of Food Allergens in the Gut-Mammary Axis.Nutrients · 2026Review
- Microbial fermentation as a strategy for the abatement of peanut allergens.Applied and environmental microbiology · 2026Review
- Food Allergen Component Sensitization Patterns in Eosinophilic Esophagitis: Insights from a Retrospective Comparative Study.Foods (Basel, Switzerland) · 2026Article
- Gold Nanoparticle-Based Systems for Targeting the Ara h2 Allergen: A Molecular Modeling Approach.Computational and structural biotechnology journal · 2026Article
- Research Advancements in Peanut Proteins, Their Allergenic Potentials, and the Approaches to Mitigate Peanut Allergenicity.Nutrients · 2025Review
- Defining the cross-reactivity between peanut allergens Ara h 2 and Ara h 6 using monoclonal antibodies.Clinical and experimental immunology · 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
- Food Allergens of Plant Origin.Foods (Basel, Switzerland) · 2023Review
- Molecular cloning and characterization of an alpha-amylase inhibitor (TkAAI) gene from Trichosanthes kirilowii Maxim.Biotechnology letters · 2022Article
- Immunodominant conformational and linear IgE epitopes lie in a single segment of Ara h 2.The Journal of allergy and clinical immunology · 2022Article
- Molecular Interactions Associated with Coagulation of Organic Pollutants by 2S Albumin of Plant Proteins: A Computational Approach.Molecules (Basel, Switzerland) · 2022Article
- Tree Nuts and Peanuts as a Source of Beneficial Compounds and a Threat for Allergic Consumers: Overview on Methods for Their Detection in Complex Food Products.Foods (Basel, Switzerland) · 2022Review
- Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?Clinical reviews in allergy & immunology · 2022Review
- Introduction of Heated Cow's Milk Protein in Challenge-Proven Cow's Milk Allergic Children: The iAGE Study.Nutrients · 2022Article
- Characterization of Relevant Biomarkers for the Diagnosis of Food Allergies: An Overview of the 2S Albumin Family.Foods (Basel, Switzerland) · 2021Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resistance to proteolytic enzymes and heat is thought to be a prerequisite property of food allergens. Allergens from peanut (Arachis hypogaea) are the most frequent cause of fatal food allergic reactions. The allergenic 2S albumin Ara h 2 and the homologous minor allergen Ara h 6 were studied at the molecular level with regard to allergenic potency of native and protease-treated allergen. A high-resolution solution structure of the protease-resistant core of Ara h 6 was determined by NMR spectroscopy, and homology modelling was applied to generate an Ara h 2 structure. Ara h 2 appeared to be the more potent allergen, even though the two peanut allergens share substantial cross-reactivity. Both allergens contain cores that are highly resistant to proteolytic digestion and to temperatures of up to 100 degrees C. Even though IgE antibody-binding capacity was reduced by protease treatment, the mediator release from a functional equivalent of a mast cell or basophil, the humanized RBL (rat basophilic leukaemia) cell, demonstrated that this reduction in IgE antibody-binding capacity does not necessarily translate into reduced allergenic potency. Native Ara h 2 and Ara h 6 have virtually identical allergenic potency as compared with the allergens that were treated with digestive enzymes. The folds of the allergenic cores are virtually identical with each other and with the fold of the corresponding regions in the undigested proteins. The extreme immunological stability of the core structures of Ara h 2 and Ara h 6 provides an explanation for the persistence of the allergenic potency even after food processing.
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What OpenQuestion holds
Registered trials
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.