Sensitization pattern and IgE cross-reactivity to peanut allergen molecules in patients with allergic diseases

Peanuts are widely used to produce multi-component food products. Such meal may cause severe allergies in patients with sensitization to peanuts. The severity of symptoms depends on both individual characteristics of immune system and on distinct peanut allergen components causing the hypersensitivity. In addition, peanut contains protein components similar in structure and function to molecules of other plant species, thus leading to occurence of cross-allergic reactions. The aim of our study was to detect sensitization to peanut allergen components and evaluate their IgE cross-reactions with homologous proteins of other superfamilies in patients with allergic diseases. A total of 29 serum samples from patients with atopic diseases were tested. In these sera, sIgEs to 112 allergen components were determined using ImmunoCap ISAC panel (Phadia, Sweden). The detection frequency of sIgE to rAra h 8 was maximal (55.17%; 16 patients of 29), while the level of these antibodies was 0.92±0.39 ISU-E. The level of sIgE to rAra h 2, nAra h 6 and rAra h 9 was also increased (0.67±0.65 ISU-E; 0.48±0.29 ISU-E and 0.34±0.1 ISU-E, respectively). Sensitization to rAra h 1 and rAra h 3 was not detected. The study of correlation relationships showed the presence of significant direct correlation between sIgE to rAra h 8 and to allergens of other taxonomically different plants, i.e., celery (rApi g 1), apple (rMal d 1) and peach (rPru p 1). We have shown that determination of sIgE only to two allergens Ara h 2 and Ara h 6 allows us to determine primary peanut allergy, which is crucial in predicting severe complications. We have assessed the IgE cross-reactivity profile, thus allowing us to avoid hidden cross-reactions, which may also cause significant sensitization and trigger pathological processes in people with allergic diseases.