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Food-dependent exercise-induced anaphylaxis to pistachio has also been reported. Ingestion of roasted pistachio nuts ( Pistacia vera) has been reported to cause potentially harmful anaphylactic reactions, but pistachio is also currently incorporated in ice creams, bakery products and various exotic dishes. This is the case with pistachio allergens, which are responsible for sometimes severe allergic manifestations. However, except for peanut and hazelnut, seed allergens from other tree nuts are less well known.
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Although belonging to different botanical families, tree nuts share with peanut ( Arachis hypogaea) and other edible seeds from lentil ( Lens culinaris), pea ( Pisum sativum), kidney bean ( Phaseolus vulgaris), soybean ( Glycine max), sesame ( Sesamum indicum) and buckwheat ( Fagopyrum esculentum), three groups of 2S albumins, 7S globulins or vicilins, and 11S globulins or legumins that have been recognized for a long time as being the most frequent allergen sources in seeds. The IgE-mediated anaphylaxis to tree nuts, such as almond ( Prunus dulcis), Brazil nut ( Bertholletia excelsa), cashew nut ( Anacardium occidentale), hazelnut ( Corylus avellana), pecan nut ( Carya illinoinensis), pistachio nut ( Pistacia vera), walnut ( Juglans regia), has now become a public health concern, responsible for a major proportion of often severe anaphylactic shocks in both children and adults. Conversely, conformation of most of the epitopic regions of the pistachio allergens often differs from that of epitopes occurring on the molecular surface of the corresponding Ara h 1 (vicilin), Ara h 2 (2S albumin) and Ara h 3 (legumin) allergens from peanut ( Arachis hypogaea). Other conformational similarities were identified with the corresponding allergens Ses i 1 (2S albumin), Ses i 3 (vicilin) and Ses i 6 (legumin) from sesame ( Sesamum indicum), and Jug r 1 (2S albumin), Jug r 2 (vicilin) and Jug r 4 (legumin) from walnut ( Juglans regia). They support the recommendation for prescribing pistachio avoidance in cashew allergic patients. These results offer a molecular basis for the IgE-binding cross-reactivity often observed between pistachio and cashew nut. Surface analysis of these epitopic regions indicates a high degree of conformational similarity with the previously identified epitopic regions of the corresponding allergens Ana o 1 (vicilin), Ana o 2 (legumin) and Ana o 3 (2S albumin) from the cashew ( Anacardium occidentale) nut.
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Most of the epitopic regions identified on Pis v 1 and Pis v 3 do not coincide with the putative N-glycosylation sites and thus are not considered as glycotopes. They essentially consist of hydrophilic and electropositively charged residues well exposed on the surface of the allergens. Sequential IgE-binding epitopes were identified on the molecular surface of the Pis v 1 (2S albumin), Pis v 2 (11S globulin/legumin) and Pis v 3 (7S globulin/vicilin)-major allergens from pistachio ( Pistacia vera) seeds-using the Spot technique.