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IgE-binding epitopes on house dust mite (HDM) and mixed pollen allergens are the specific molecular regions on allergenic proteins recognized and bound by allergen-specific Immunoglobulin E (IgE) antibodies. These epitopes are found on major allergens such as Der p 1 and Der p 2 from mites, and Bet v 1 or Phl p 1 from pollens [PMID: 25210972]. The binding and subsequent cross-linking of IgE on the surface of mast cells and basophils by these epitopes trigger the immediate release of inflammatory mediators like histamine, which drives the symptoms of allergic rhinitis, asthma, and atopic dermatitis [PMID: 30145924]. In therapeutic contexts, these epitopes are the primary focus of allergen-specific immunotherapy (AIT), which aims to desensitize the immune system through controlled exposure to the allergens. Modern strategies also involve the development of 'hypoallergens'—engineered proteins with modified epitopes that have reduced IgE-binding capacity but retain the ability to induce T-cell tolerance, thereby improving the safety profile of allergy treatments [PMID: 21930573].
Allergen-specific immunotherapy (AIT) induces immune tolerance by promoting the production of regulatory T cells (Tregs) and allergen-specific IgG4 antibodies. These IgG4 antibodies act as blocking antibodies that compete with IgE for the IgE-binding epitopes on the allergens, thereby preventing the cross-linking of IgE on mast cells and basophils and inhibiting the release of inflammatory mediators [PMID: 28024493, PMID: 30145924].
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