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Immunoglobulin E (IgE) antibodies specific for Pen c 13 epitopes are specialized immune proteins that mediate allergic reactions to the mold Penicillium citrinum. Pen c 13 is an alkaline serine protease and a major allergen of this fungal species (Shen et al., 1999, J Allergy Clin Immunol). In sensitized individuals, these specific IgE (sIgE) antibodies bind to the epitopes of Pen c 13, leading to the cross-linking of high-affinity IgE receptors (FcεRI) on the surface of mast cells and basophils (Gould & Sutton, 2008, Nature Reviews Immunology). This interaction triggers the degranulation of these cells, releasing potent inflammatory mediators such as histamine and leukotrienes, which cause the symptoms of allergic rhinitis and asthma. While these specific antibodies serve as critical diagnostic biomarkers for mold allergy, they are also indirectly targeted by broad anti-IgE therapies like Omalizumab, which neutralize the circulating IgE pool to prevent the allergic cascade (FDA, Xolair Label).
Anti-IgE monoclonal antibodies bind to the Cε3 domain of free IgE, preventing its interaction with the high-affinity IgE receptor (FcεRI) on mast cells and basophils, thereby inhibiting the allergic cascade.
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