ArticleNutrients2026
Heat Processing Reduces IgE Binding but Not Basophil Sensitivity to Pea Proteins in Pea-Allergic Children.
Article in Nutrients, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Allergenicity Assessment of Precision Fermentation-Derived Food Proteins.Foods (Basel, Switzerland) · 2026Review
- Emerging Biomarkers in Pediatric Food Allergy: From Mechanistic Endotyping to Precision Diagnosis and Therapeutic Monitoring.Biomedicines · 2026Review
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Authors and funding
6 authors.
Funding
Abstract
BACKGROUND/
objectivesThe increasing use of pea protein in plant-based foods raises concerns about IgE-mediated reactions, particularly in individuals sensitized to peanut. Knowledge on clinically relevant pea allergens and the impact of heat processing remains limited. This study investigated how thermal treatment affects the IgE binding and functional allergenicity of pea proteins in children with a confirmed pea allergy, with or without a concomitant peanut allergy.
methodsSerum from 11 patients was analyzed using SDS-PAGE, Western blotting, and an indirect basophil activation test (iBAT).
resultsAll patients showed IgE binding to Pis s 1 and PA2a/b in raw pea extract, with variable sensitization to Pis s 2 and mitogenic lectin. Heating (120 °C, 5 min) markedly reduced IgE binding and eliminated detectable IgE to Legumin S and ML. Despite this reduction, basophil sensitivity did not decrease; in several patients, EC50 values significantly decreased, indicating increased basophil responsiveness to heated pea. Patients with IgE profiles dominated by Pis s 1 and PA2a/b were most likely to show enhanced basophil activation after heating.
conclusionsThese findings demonstrate that heat-stable vicilin subunits and albumins can maintain functional allergenicity despite reduced IgE recognition, underscoring the need for diagnostic approaches that incorporate processed food allergens.
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