Identification of allergens in Artocarpus heterophyllus, Moringa oleifera, Trianthema portulacastrum and Syzygium samarangense

Abstract

Background It is clinically important to identify allergens in Artocarpus heterophyllus (jackfruit), Moringa oleifera (moringa), Trianthema portulacastrum (horse purslane) and Syzygium samarangense (rose apple). This study included 7 patients who developed anaphylaxis to jackfruit (1), moringa (2), horse purslane (3) and rose apple (1). We sought to determine allergens in the edible ripening stages of jackfruit (tender, mature, and ripened jackfruit) and seeds, edible parts of moringa (seeds, seedpod, flesh inside seedpod, and leaves), horse purslane leaves and ripened rose apple fruit. The persistence of the allergens after cooking was also investigated. Methods Allergens were identified by clinical history followed by a skin prick test. Protein profiles of plant/fruit crude protein extracts were determined by SDS-PAGE. Molecular weights of the allergens were determined by immunoblotting with patient sera. Results A heat-stable allergen of 114 kDa in A. heterophyllus which is shared among different ripening stages and seeds was identified. Additionally, 101 kDa allergen in boiled tender jackfruit, 86 kDa allergen in boiled seeds and 80 kDa allergen in boiled mature jackfruit were identified. Five heat-stable allergens of 14, 23, 35, 43, and 48 kDa in M. oleifera, 1 heat-stable allergen of 97 kDa in T. portulacastrum, and 4 allergens of 26, 31. 60, and 82 kDa in S. samarangense were identified. Conclusion Novel IgE-sensitive proteins of A. heterophyllus, M. oleifera, T. portulacastrum and S. samarangense were identified which would be especially useful in the diagnosis of food allergies. The identified allergens can be used in Component Resolved Diagnostics (CRD).

The Potential Role of Moringa oleifera Lam. Leaf Proteins in Moringa Allergy by Functionally Activating Murine Bone Marrow-Derived Dendritic Cells and Inducing Their Differentiation toward a Th2-Polarizing Phenotype

“…However, it should be noted that some individuals may be allergic to M. oleifera leaves. Previous studies have investigated M. oleifera leaf allergens [ 6 , 7 , 8 ], but the mechanism through which Mo-Pr or M. oleifera leaf allergen causes allergies as well as its effect on DCs remain unclear. Food allergy is a significant public health issue worldwide.…”

“…Giovanni D’Auria et al identified potential M. oleifera leaf allergens, including morintides and nsLTP, through proteomic analysis [ 7 ]. Janitha Iddagoda et al determined the molecular weights of the M. oleifera leaf allergens to be 14, 23, 35, 43, and 48 kDa using Western blotting with serum from patients with M. oleifera leaf allergy [ 8 ]. While the current evidence suggests the existence of potential allergens in M. oleifera leaf, the mechanism of allergy caused by M. oleifera leaf protein or M. oleifera leaf allergen remains unclear.…”