## 3 Discussion
Notably, the homologues of glucose dehydrogenase [FAD, quinone] have being identified in the venom proteome of the parasitic ant _E. tuberculatum_[42], although it was not described as a genuine insect antigen or venom component. The MRJPs sequence identified in the transcriptome and venom proteome of _D. quadriceps_ might represent a new member of the same family, but with distinct function from its counterparts in bee and fruit fly. The MRJPs is known to have anti-apoptotic activity and act in similar way that the nerve growth factor (NGF) does in hepatocyte culture, interacting with mitogen-activated protein kinase and protein kinase B, controlling the pattern of adult fly cuticle pigmentation and larval buccal parts [43]. It is important to note that the MRJP-like protein of _D. quadriceps_ shares only 27% of similarity with the _A. mellifera_ MRJP-1 and 40% with the _D. melanogaster_ yellow protein, which controls the pattern of pigmentation of the fly cuticle and larvae. The yellow proteins (MRJPs) are involved in the enzymatic conversion processes of the melanization pathways [44]. It is interesting note that the C-terminal end of the bee MRJP-1 can be cleaved in jellein-2, which is subsequently cleaved in jellein-1 and jellein-4, which in turn show antimicrobial activity [45]. The jellein-related peptides were not observed in the _D. quadriceps_ venom either because the _D. quadriceps_ MRJP-1 was not cleaved or because a molecular weight cut-off of 10 kDa was defined for polypeptide analysis in this study. Indeed, it would be necessary to verify if the C-terminus of the _D. quadriceps_ MRJP-1 could be cleaved into smaller peptides, similar to jellein antimicrobial peptides, since the _D. quadriceps_ MRJP-like venom protein displays a C-terminal segment that has alternating hydrophilic and hydrophobic residues and is rich in proline residues (see green box in Figure 5), close to the lysine residues, the likely site of proteolytic cleavage. The phospholipases A2 are the main components of bee venoms, while PLA1s are found as the main allergens in wasp venom (e.g., Sol i1, Api m1, Bom p1, Bom t1, Ves v1, Ves m2, Ves s1, Vez c1, Pol a1 and Pol e1). Based on the structural similarity and conservation, the _D. quadriceps_ venom PLA1 could cause hemorrhagic disorders and exacerbate envenoming response as a result of its expression in the venom and catalytic activity that generates pharmacologically active lipids. The wasp PLA1 catalyzes the hydrolysis of emulsified phospholipids exclusively at the sn-1 position, releasing free fatty acids and lysophospholipids. Lysophospholipids are multifunctional mediators and second messengers involved in diverse cellular processes, including platelet activity and blood coagulation, as well as in the physiopathology of a number of human diseases [46]. The phospholipase A1 from the black-bellied hornet wasp (_Vespa basalis_) was shown to display a potent hemolytic activity that is responsible for their lethal effects [47; 48]. The roles of wasp venom PLAs in platelet activation and allergic response have been reported [49; 50]. The roles of PLA1 and PLA2 in the envenomation and allergic response caused by wasps, as well as the involvement of venom PLA1 in allergy caused by ant stings, is reviewed elsewhere and further information can be taken [26; 51]. In this context, the PLA1 from giant ant venom is not only an enzymatic component (hydrolase), but also appears as a potential allergen that contributes to trigger a late immune response in the victim. In the venom of _D. quadriceps_, enzymes are one of the main components that apart from their role in catalytic destruction of tissues that can contribute to allergic responses. Among these venom-enzymes, the hyaluronidase-type found in the _D. quadriceps_ crude venom shares structural characteristics with the wasp hyaluronidase; for example, two intra-molecular disulfide bridges formed between four cysteine residues located in conserved positions in contrast to the mammalian hyaluronases that have four disulfide bonds.