RESUMO
BACKGROUND: Hymenoptera stings are one of the most common causes of anaphylaxis. Vespa orientalis (red hornet) is a common and very aggressive hymenopteran endemic in central and southern areas of Iran. Allergy testing and venom immunotherapies are carried out with venom components which are expensive, have limited commercial availability, and often lack specificity. Although proteomic analysis of hymenopteran venom has been shown to be a powerful technique to identify allergens, data on the protein components of V. orientalis venom are lacking. AIM: This study was designed to characterize the allergenome profile (proteome of allergenic proteins) of this local hornet venom. METHODS: Venom was extracted from V. orientalis worker venom sacs. The venom constituents were separated by two-dimensional gel electrophoresis (2DE). Protein components were blotted and probed with serum from 10 allergic patients by immunoblotting. Reactive spots were isolated and characterized by liquid chromatography with tandem mass spectrometry. RESULTS: A total of 195 protein spots were detected on the 2DE gels. Fifteen distinct venom proteins showed reactivity to IgE in patients' sera. Four major allergens in order of allergenicity in patients were identified as hyaluronidase, arginine kinase, phospholipase A1 (PLA1) and PLA1 magnifin. CONCLUSIONS: Broadening our knowledge of V. orientalis venom constituents can contribute to improvements in diagnostic and immunotherapeutic techniques, both of which are dependent on the major allergens in venom extract. This information is also potentially helpful to develop medical uses of major allergens in this venom to improve the diagnostic specificity and the efficacy of immunotherapy.
