SENSITIZATION PATTERN AND IGE CROSS-REACTIVITY TO PEANUT ALLERGEN MOLECULES IN PATIENTS WITH ALLERGIC DISEASES

AbstractToday peanut is widely used to produce multi-component food products. Such food products can cause severe allergies in patients with sensitization to peanuts. The severity of symptoms depends on both individual characteristics of the immune system and on which peanut allergen components have caused hypersensitivity. In addition, peanut contains protein components similar in structure and function to molecules of other plant species, which leads to formation of cross-allergic reactions.The aim of the study was to identify 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, sIgE was determined to 112 allergen components using ImmunoCap ISAC method (Phadia, Sweden).The frequency of detection of sIgE to rAra h 8 was maximum (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 reliable direct correlation between sIgE to rAra h 8 and allergens of other taxonomically different plants - celery (rApi g 1); apple (rMal d 1) and peach (rPru p 1). We showed 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 identified the IgE cross-reactivity profile and it allows us to avoid hidden cross-reactions, which can also cause significant sensitization and trigger pathological processes in people with allergic diseases.