Multi-Omics Analyses Elucidate the Venom Components of the Wasp Vespa mandarinia

The wasp Vespa mandarinia was widely reared in Yunnan province in China. It is characterized by notable toxicity, large body size, and strong invasiveness. Its extremely potent venom and high output lead to aggressive behavior. To elucidate the composition of V. mandarinia venom, proteome, peptidome, and metabolome analyses were conducted in this study. Proteome analysis identified 2189 proteins, among which 842 were proteases, and 20 were venom-related proteases. 1294 proteins were identified as nonenzymatic proteins, with 2 toxic proteins. Moreover, hyaluronidase, venom dipeptidyl peptidase 4, and phospholipase A1 were detected. Peptidome analysis detected 1263 peptides, 70 of which were proteolytic peptides, including one phospholipase A2 isozyme. Among the 223 nonenzymatic peptides, two were characterized as vespid chemotactic peptide and the mastoparan-like peptide. Metabolome analysis tentatively annotated 918 compounds in positive mode versus 499 in negative mode. Organic heterocyclic compounds, organic acids, and their derivatives were the most abundant superclasses of venom metabolites. γ-aminobutyric acid, N-acetylhistamine, tryptamine, and dopamine were also identified. These results uncovered key toxic components, including venom-related proteases, toxic peptides, and bioactive metabolites. It constituted a comprehensive molecular basis for understanding toxicity and biological functions of V. mandarinia venom.