Most of the protein content is made up by seed storage proteins of the cupin or prolamin superfamilies. The total protein content of three of the most commonly used peanut cultivars (Valencia, Virginia, and Spanish) was determined to be between 24 and 29 %. Peanuts contain 44–56 % oil and 22–30 % protein. Peanuts are very rich in nutrients and are one of the basic crops of India, China, the USA and West Africa. The typical peanut seed pod which usually contains two seeds matures buried underground. The peanut is botanically related to beans and peas but not to tree nuts. Peanuts are the seeds of the peanut plant ( Arachis hypogaea) which is a member of the legume family (Fabaceae). 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. Molecular cross-reactivity has been described between members of the Bet v 1-like proteins, the non-specific lipid transfer proteins, and the profilins. Clinical observations frequently report an association of peanut allergy with allergies to legumes, tree nuts, seeds, fruits and pollen. 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. Currently, the IUIS allergen nomenclature subcommittee accepts 12 peanut allergens. This article describes the classification and molecular biology of peanut seed allergens with particular reference to their cross-reactivities.
All rights reserved.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. Considerations for an approach to individual patient care are highlighted.Ĭopyright © 2020 American Academy of Allergy, Asthma & Immunology. The complicating factor of addressing co-allergy, for example, the risks of allergy to both peanut and tree nuts among atopic patients, is also discussed. This review discusses clinically relevant cross-reactivity related to the aforementioned food groups as well as seeds, legumes (including peanut, soy, chickpea, lentil, and others), tree nuts, meats, fruits and vegetables (including the lipid transfer protein syndrome), and latex. Low rates are noted for grains (wheat, barley, rye), and rates of cross-reactivity are variable for most other foods. Examples of food families with high rates of cross-reactivity include mammalian milks, eggs, fish, and shellfish. Although molecular diagnostics have improved our ability to identify clinically relevant cross-reactivity, the optimal approach to patients requires an understanding of the epidemiology of clinically relevant cross-reactivity, as well as the food-specific (degree of homology, protein stability, abundance) and patient-specific factors (immune response, augmentation factors) that determine clinical relevance.
However, many are sensitized to foods without exhibiting clinical reactivity. This results in patients having allergic sensitization (positive tests) to many biologically related foods. The diagnosis and management of food allergy is complicated by an abundance of homologous, cross-reactive proteins in edible foods and aeroallergens.
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