ArticleMolecules (Basel, Switzerland)2016
What Characteristics Confer Proteins the Ability to Induce Allergic Responses? IgE Epitope Mapping and Comparison of the Structure of Soybean 2S Albumins and Ara h 2.
Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Nutritional and Functional Potential of Rapeseed and Canola Proteins: Advances in Protein Extraction, Phenolic Removal, and Food Applications.Comprehensive reviews in food science and food safety · 2026Review
- Deciphering Allergen Peptides for Dermatological and Cosmetic Applications with Explainable Artificial Intelligence.Journal of proteome research · 2026Article
- Insights into Api m 10-Isoforms and Splice Variants: More Than One Major IgE-Binding Epitope.Clinical and translational allergy · 2026Article
- Molecular Profiling of Peanut under Raw, Roasting, and Autoclaving Conditions Using High-Resolution Magic Angle Spinning and SolutionMolecules (Basel, Switzerland) · 2023Article
- The Heterogeneity of Ovomucoid-Specific IgE Idiotype Is Associated With Egg Allergy Symptom Severity.Allergy, asthma & immunology research · 2023Article
- Soy Gly m 8 sIgE Has Limited Value in the Diagnosis of Soy Allergy in Peanut Ara h 2-Sensitized Adults.International archives of allergy and immunology · 2023Article
- Lentil allergens identification and quantification: An update from omics perspective.Food chemistry. Molecular sciences · 2022Review
- Characterization of Relevant Biomarkers for the Diagnosis of Food Allergies: An Overview of the 2S Albumin Family.Foods (Basel, Switzerland) · 2021Article
- 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
- Epitope-Resolved Detection of Peanut-Specific IgE Antibodies by Surface Plasmon Resonance Imaging.Chembiochem : a European journal of chemical biology · 2018Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ara h 2, a peanut 2S albumin, is associated with severe allergic reactions, but a homologous protein, soybean 2S albumin, is not recognized as an important allergen. Structural difference between these proteins might explain this clinical discrepancy. Therefore, we mapped sequential epitopes and compared the structure of Ara h 2, Soy Al 1, and Soy Al 3 (Gly m 8) to confirm whether structural differences account for the discrepancy in clinical responses to these two proteins. Commercially synthesized peptides covering the full length of Ara h 2 and two soybean 2S albumins were analyzed by peptide microarray. Sera from 10 patients with peanut and soybean allergies and seven non-atopic controls were examined. The majority of epitopes in Ara h 2 identified by microarray are consistent with those identified previously. Several regions in the 2S albumins are weakly recognized by individual sera from different patients. A comparison of allergenic epitopes on peanut and soybean proteins suggests that loop-helix type secondary structures and some amino acids with a large side chain including lone electron pair, such as arginine, glutamine, and tyrosine, makes the peptides highly recognizable by the immune system. By utilizing the peptide microarray assay, we mapped IgE epitopes of Ara h 2 and two soybean 2S albumins. The use of peptide microarray mapping and analysis of the epitope characteristics may provide critical information to access the allergenicity of food proteins.
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