Abstract
The consumption of cashew as roasted nuts or as a hidden allergen in various foodstuffs, e.g. Asian meals, ice creams or cakes, is responsible for severe anaphylactic reactions in previously sensitized individuals. Like peanut allergy, allergy to Cashew nut has now become a worrying problem of public health due to the extreme severity of its clinical manifestations. The major cashew allergens consist of seed storage proteins embedded in the seed protein bodies, namely Ana o 1 (vicilin) and Ana o 2 (legumin) of the cupin family, and Ana o 3 (2S albumin). All of these cashew allergens strongly resist to heat denaturation (roasting) and hydrolysis by digestive proteases (pepsin, trypsin), and thus display a high allergenic potency. The IgE-binding epitopes have been identified on the molecular surface of both allergens. A high degree of IgE-binding cross-reactivity occurs between the cashew allergens and the corresponding allergens Pis v 1, Pis v 2 and Pis v 3, of the closely-related pistachio. Obviously, this cross-reactivity depends on the highly conserved character of both the sequence and three-dimensional fold among these allergens. Less frequent cross-reactions also occur with other tree nuts, like almond and hazelnut. Conversely, almost no cross-reaction was reported to occur between cashew and peanut. In most cases, however, this cross-reactivity is apparently devoid of any clinical significance and would simply reflect some phylogenetical relatedness among tree nuts. In this respect, it is noteworthy that cashew and pistachio belong to the same family of Anacardiaceae.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call