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.

2023-05-10 | PXD040764 | Pride

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).

2024-01-26 | PXD046030 | Pride

iVesVel2

Project description:Vespa velutina (Asian hornet) genome assembly, iVesVel2

| PRJEB46979 | ENA

Stings on wings: venom proteomics and tissue transcriptomics of the lesser banded hornet, Vespa affinis

Project description:The project aims at unraveling the venom repertoire of the lesser banded hornet (Vespa affinis) and investigate the regimes of natural selection underpinning their venom evolution. The study also sheds light on the clinical repercussions of the V. affinis venom.

2023-03-10 | PXD037171 | Pride

iVesVel2 alternate haplotype

Project description:Vespa velutina (Asian hornet) genome assembly, iVesVel2, alternate haplotype

| PRJEB46980 | ENA

Fraxinus velutina

Project description:Fraxinus velutina overview

| PRJNA791989 | ENA

Vespa mandarinia

Project description:Metagenome of the gut flora of Vespa mandarinia

| PRJNA751718 | ENA