Peanut allergen proteins (Ara h allergens (collective))

Peanut allergen proteins are a group of structurally diverse proteins from Arachis hypogaea that elicit IgE-mediated hypersensitivity; at least 12 allergens (Ara h 1–Ara h 13 with gaps) are recognized by the IUIS Allergen Nomenclature Sub-Committee and fall mainly into the cupin superfamily (Ara h 1, Ara h 3), prolamin superfamily/2S albumins (Ara h 2, Ara h 6, Ara h 7, Ara h 9), profilin family (Ara h 5), Bet v 1-related/PR-10 proteins (Ara h 8), oleosins (Ara h 10, Ara h 11), and plant defensins (Ara h 12, Ara h 13)[1][3]. Among these, Ara h 2 is a major and highly potent allergen recognized by approximately 80–90% of peanut-allergic patients, with a five-helix bundle fold stabilized by four disulfide bonds typical of the prolamin superfamily, and its epitope diversity helps distinguish subpopulations of patients based on IgE binding patterns[2]. Collectively, these allergens’ biological roles include seed nutrient storage, plant defense, lipid body stabilization, and cytoskeletal regulation, but clinically they are relevant as triggers of peanut allergy and anaphylaxis and as components used in component-resolved diagnostics to stratify true peanut allergy (e.g., Ara h 2, Ara h 6) versus pollen-related cross-reactivity (e.g., Ara h 8, Ara h 5)[1][3].

Other names

Peanut allergensArachis hypogaea allergensAra h (family of peanut allergen proteins)Peanut seed storage proteins (allergen subset)Peanut defensins (allergen subset)Peanut oleosins (allergen subset)Peanut profilin (Ara h 5)Peanut Bet v 1-like protein (Ara h 8)

Not applicable for drugs directly targeting these allergens; current therapeutics (e.g., oral immunotherapy, epicutaneous immunotherapy, monoclonal anti-IgE) act on the immune system rather than directly on peanut proteins