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Peanut allergen-specific B-cell receptors (BCRs) and immunoglobulin E (IgE) antibodies are the primary immunological mediators of peanut allergy, a potentially life-threatening type I hypersensitivity (Wood et al., 2024). These molecules are characterized by their high affinity for specific peanut proteins, primarily Ara h 1, Ara h 2, and Ara h 3 (Bublin & Breiteneder, 2014). In sensitized individuals, B cells express BCRs that, upon activation, differentiate into plasma cells secreting peanut-specific IgE. This IgE then coats mast cells and basophils via the high-affinity FcεRI receptor. Subsequent exposure to peanut allergens causes cross-linking of the IgE-FcεRI complexes, triggering the rapid release of vasoactive amines and cytokines that drive allergic inflammation and anaphylaxis (Croote et al., 2018). Modern therapeutic approaches target this pathway either by sequestering IgE to prevent effector cell activation or by employing oral immunotherapy to desensitize the immune system and promote the production of blocking IgG4 antibodies (Vickery et al., 2018). Understanding the repertoire of these BCRs is crucial for developing precision treatments and diagnostic tools for food allergies.
Therapeutic agents target this axis by binding to the Fc region of free IgE to prevent its interaction with high-affinity FcεRI receptors on mast cells and basophils (e.g., Omalizumab), or by utilizing allergen immunotherapy to induce immune tolerance and shift antibody production from pathogenic IgE to protective IgG4 (e.g., Palforzia).
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