Project description:A phylogenomic perspective on the Systematics of Mutillidae (Hymenoptera), with emphasis on Sphaeropthalminae (genome sequencing and assembly)
Project description:(1)Background: Dipeptidyl Peptidases IV (DPPIVs), present in many organisms, are minor components in the venoms of Hymenoptera, where they have been shown as cross-reactive allergenic molecules. Since the structure of homologous DPPIVs is well characterized, we explain which regions have higher similarity among these proteins and present a comparison including a new Vespa velutina DPPIV sequence. Moreover, two cases of sensitization to DPPIV in wasps- and honeybees-sensitized patients are presented. (2) Methods: Proteomic analyses have been performed on the venom of the Asian Hornet V.velutina, in order to demonstrate the sequence of its DPPIV (putative allergen Vesp v 3). Comparison by alignments and analysis of the three-dimensional structure allow to show a region with higher similarity among Hymenoptera DPPIVs. Besides, ImmunoCAP™ determinations (including specific inhibition experiments), as well as IgE-immunoblotting, demonstrate the presence of Api m 5 and Ves v 3. (3) Results and conclusions: The data presented explain that the similarities among Hymenoptera DPPIVs are most probably localized at the C-terminal region of these enzymes. The clinical cases analyzed demonstrate the presence of this minor component in the preparations used in venom immunotherapy. Moreover, a new DPPIV sequence is published (Accession Number P0DRB8).
Project description:This study aimed to investigate the venom sac extracts (VSE) of the European hornet (EH) Vespa crabro (Linnaeus, 1758) (Hymenoptera: Vespidae), focusing on the differences between stinging females, gynes (G) and workers (W), at the protein level. Using a quantitative “Sequential Window Acquisition of all Theoretical Fragment Ion Mass Spectra” (SWATH-MS) analysis, we identified and quantified a total of 240 proteins. Notably, within the group, 45.8 % (n = 110) showed significant differential expression between VSE-G and VSE-W. In this set, 57.3 % (n = 63) were upregulated and 42.7 % (n = 47) downregulated in the G. Additionally, the 200 quantified proteins from the class Insecta belong to 16 different species, six of them to he Hymenoptera/Apidae lineage, comprising seven proteins with known potential as allergens. Phospholipase A1 (Vesp v 1), phospholipase A1 verutoxin 2b (VT-2b), hyaluronidase A (Vesp v 2A), hyaluronidase B (Vesp v 2B), and venom allergen 5 (Vesp v 5) were significantly downregulated in the G, and vitellogenin (Ves v 6) was upregulated. Overall, 46 % of the VSE proteins showed differential expression, with a majority being upregulated in G. These findings shed light on the proteomic differences in VSE between EH castes, potentially contributing to our understanding of their behavior and offering insights for allergy research.
