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Cow's milk allergen epitopes are short peptide regions within cow's milk proteins that are specifically recognized by IgE or T cell receptors in individuals with cow's milk allergy[2][3][4]. The major milk protein allergens — casein, α-lactalbumin, and β-lactoglobulin — contain multiple epitopes that are responsible for triggering the immune response, leading to symptoms like rash, anaphylaxis, gastrointestinal distress, and asthma[2][5]. The configuration and presence of these epitopes can vary with processing (such as heating or fermentation), which may destroy or alter some epitopes and reduce allergenicity[2]. Diagnostic and therapeutic approaches increasingly target these epitopes, including the use of peptide-based immunotherapy and immune monitoring of T cell responses to specific cow's milk peptides[3][4]. Safety concerns include severe reactions and the technical challenge of identifying all relevant epitopes in a genetically diverse population[3][4].
Induction of immune tolerance: Peptides or altered proteins that lack or modify allergenic epitopes can retrain the immune system to reduce allergic responses[3]. Suppression of IgE binding: Hydrolyzed or processed proteins reduce exposure to or alter these epitopes, decreasing sensitization[2].
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