Vespa velutina nigrithorax (VVN), accidentally introduced in France in 2004 from South-East Asia and rapidly spread across Europe (1), may cause relevant health problems to humans due to its venom: indeed, the proteins contained in VVN's venom are able to act both as toxins and allergens, and deaths due to organ dysfunction induced by toxins in venom and to fatal allergic reactions were both reported (2-5). The two most dangerous groups of toxins identified are the hemostasis-impairing toxins, that participate in the blood coagulation cascade with a distinct hemolytic effect, probably representing the main lethal factor of the multiple organ failure produced by VVN stings, and neurotoxins, that can induce varying degrees of nerve degeneration and paralysis (2). About the allergenic components, according to the serum samples from patients who had experienced allergenic reactions, two most common allergens have been identified: Vesp v 5, corresponding to antigen 5, and Vesp v 1, corresponded to A1-phospholipase (one of whose most interesting features is its glycosylated nature) (4, 6, 7). Despite this, only Vesp v 5 may be considered a dominant allergen, with more than 85% of patients having IgE against it, while Vesp v 1 has been detected in less than 50% of patients (6-8) Additionally, IgE against Vesp v 5 also resulted higher than IgE against VVN whole venom (9, 10). Other two components purified in the venom of VVN specimen, Vesp v 2A and 2B (two hyaluronidase isoforms) have been characterized as potential allergens, but specific IgE against these isoforms has not yet been demonstrated (4,11,12).Since there is no specific available VIT for VVN yet, several studies focused on the importance of finding out if VVN stung patients with severe systemic reactions may be treated with actual Hymenoptera commercially available extracts. By studying the degree of similarity with respect to antigen 5 and A1-phospholipase from Vespula spp., Vespa crabro and Polistes dominula, it was found that both VVN antigen 5 and A1phospholipase show a very high homology with Vespa crabro and Vespula spp. Instead, a lower percentage of structural identity has been found with antigen 5 and A1-phospholipase present in Polistes dominula (12).