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Food allergen proteins are a diverse group of proteins derived from various food sources that trigger IgE-mediated hypersensitivity reactions in susceptible individuals [1, 9]. These proteins typically belong to specific structural families, such as cupins, prolamins, and profilins, and often exhibit high stability against heat and proteolytic digestion, allowing them to reach the intestinal immune system intact [16, 25]. In the context of disease, they act as the primary triggers for food allergies, ranging from mild symptoms like urticaria to life-threatening systemic anaphylaxis [18, 31]. From a therapeutic perspective, these proteins serve as the active components in allergen-specific immunotherapy (AIT), where controlled exposure aims to induce clinical desensitization and long-term immunological tolerance [3, 13]. Drugs like Palforzia utilize standardized peanut allergen proteins to modulate the immune system, shifting the response from a Th2-driven allergic profile to a more tolerant state characterized by increased regulatory T cells and IgG4 blocking antibodies [2, 30]. While effective for desensitization, the use of these proteins in therapy carries significant risks, including the potential for systemic reactions and the development of eosinophilic esophagitis [14, 18].
Immunological desensitization through gradual exposure, leading to a shift from Th2 to Th1/Treg immune responses, induction of allergen-specific IgG4 blocking antibodies, and reduced reactivity of mast cells and basophils [3, 5, 12].
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