Integrated Venomics Profiling of Apis dorsata and Vespa sp. Venoms Reveal Putative Bioactive Candidates

Apis dorsata and Vespa sp. venoms represent underexplored Hymenopteran bioresources with potential chemical and peptide diversity relevant to antimicrobial, cytoregulatory, and enzyme-target discovery. This exploratory venomics study generated a molecular profile comprising 510 metabolite features and 118 peptides/proteins, including 29 curated metabolite annotations and seven venom-associated peptide/protein classes supported by spectral evidence, database matching, and literature-supported curation. Major metabolite classes included lipids, hydrocarbons, heterocyclic compounds, fatty acids, phenols, terpenoids, esters, and amino acid/peptide-related metabolites. Proteomic profiling identified melittin, apamin, phospholipase A2, hyaluronidase, lysozyme, chymotrypsin inhibitor, and Kazal-like proteins in A. dorsata, while comparative Vespa sp. proteomics revealed homology-supported PLA1/PLA2-like proteins, DPP4-like proteins, serpins, PNGase, and QPCT. Exploratory co-abundance mapping suggested possible relationships among antioxidant triterpenoids, immune-regulating enzymes, neuropeptides, and lipid-associated venom components. Docking indicated preliminary interactions of vorinostat with Histone Deacetylase (HDAC) and adipostatin derivatives with Fatty Acid Synthase (FASN). Overall, this study prioritizes putative bioactive metabolites, venom-associated proteins, and predicted peptide candidates for future biochemical and functional validation.