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Tree nut allergen proteins are a heterogeneous group of proteins derived from various botanical families, including Juglandaceae (walnuts, pecans), Anacardiaceae (cashews, pistachios), and Betulaceae (hazelnuts), which are responsible for severe IgE-mediated food allergies. These proteins are typically classified into structural superfamilies such as cupins (7S vicilins and 11S legumins) and prolamins (2S albumins and lipid transfer proteins), which are often highly resistant to heat and proteolysis, contributing to their potent allergenicity (Costa et al., 2022, PMID: 35154170). In sensitized individuals, these proteins act as antigens that cross-link allergen-specific IgE on the surface of mast cells and basophils, triggering the release of inflammatory mediators like histamine (WHO-IUIS Allergen Nomenclature, 2024). This physiological response can lead to clinical manifestations ranging from localized oral symptoms to systemic anaphylaxis. Therapeutic interventions currently focus on oral immunotherapy (OIT) to induce clinical desensitization by gradually exposing the patient to the allergen. Additionally, biologics such as Omalizumab are used to sequester IgE, thereby increasing the threshold of reactivity to these proteins (Wood et al., 2024, NEJM, PMID: 38405950). Understanding the molecular structure of these allergens through component-resolved diagnostics is crucial for predicting the severity of reactions and tailoring patient-specific treatments. These proteins serve as the primary target for diagnostic assays and emerging immunomodulatory therapies aimed at mitigating life-threatening allergic responses.
IgE-mediated mast cell degranulation inhibition, Immune desensitization, IL-4/IL-13 signaling blockade, IgE sequestration
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