Project description:Health risks caused by stings from Vespa velutina nigrithorax (VV), also known as the yellow-legged Asian hornet, have become a public concern, but little is known about its venom composition. This study presents the proteome profile of the VV’s venom sac based on Sequential Window Acquisition of all Theoretical Mass Spectra (SWATH-MS). The study also performed proteomic quantitative analysis and examined the biological pathways and molecular functions of the proteins in the VS of VV gynes (i.e., future queens [SQ]) and workers [SW]). The total protein content per VS was significantly higher in the SW than in the SQ (274 ± 54 µg/sac vs. 175 ± 22 µg/sac; p=0.02). We quantified a total of 228 proteins belonging to 7 different classes: Insecta (n=191); Amphibia and Reptilia (n=20); Bacilli, γ-Proteobacteria and Pisoniviricetes (n=12); and Arachnida (n=5). Phage proteins of Paenibacillus larvae, the etiological agent of American foulbrood, and genome polyprotein from deformed wing virus were quantified by SWATH-MS. Among the 228 identified proteins, 66 showed significant differential expression between SQ and SW. The well-known allergens hyaluronidase A, venom antigen 5 and phospholipase A1 were significantly downregulated in the SQ venom.
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).
