title: Cross-reactivity of peanut allergens.
abstract: Peanut seeds are currently widely used as source of human food ingredients in the United States of America and in European countries due to their high quality protein and oil content. This article describes the classification and molecular biology of peanut seed allergens with particular reference to their cross-reactivities. Currently, the IUIS allergen nomenclature subcommittee accepts 12 peanut allergens. Two allergens belong to the cupin and four to the prolamin superfamily, and six are distributed among profilins, Bet v 1-like proteins, oleosins, and defensins. Clinical observations frequently report an association of peanut allergy with allergies to legumes, tree nuts, seeds, fruits and pollen. Molecular cross-reactivity has been described between members of the Bet v 1-like proteins, the non-specific lipid transfer proteins, and the profilins. This review also addresses the less well-studied cross-reactivity between cupin and prolamin allergens of peanuts and of other plant food sources and the recently discovered cross-reactivity between peanut allergens of unrelated protein families.
authors.affiliation: Department of Pathophysiology and Allergy Research, Medical University of Vienna, Währinger Gürtel 18-20, 1090, Vienna, Austria.
authors.forename: Merima
authors.initials: M
authors.lastname: Bublin
authors.forename: Heimo
authors.initials: H
authors.lastname: Breiteneder
mesh_terms: D000485:Allergens / Q000145:classification / Q000276:immunology*; D052179:Antigens, Plant / Q000276:immunology*; D010367:Arachis / Q000276:immunology*; D003429:Cross Reactions / Q000276:immunology; D006801:Humans; D021183:Peanut Hypersensitivity / Q000276:immunology*; D010940:Plant Proteins / Q000276:immunology*
chemical_list: D000485:Allergens; D052179:Antigens, Plant; D010940:Plant Proteins