Bottom-Up Proteomic Analysis of Polypeptide Venom Components of the Giant Ant Dinoponera Quadriceps.

摘要: Ant species have specialized venom systems developed to sting and inoculate a biological cocktail of organic compounds, including peptide polypeptide toxins, for the purpose predation defense. The genus Dinoponera comprises predatory giant ants that capable causing long-lasting local pain, involuntary shaking, lymphadenopathy, cardiac arrhythmias, among other symptoms. To deepen our knowledge about composition with regard protein toxins their roles in chemical-ecological relationship human health, we performed bottom-up proteomics analysis crude ant D. quadriceps, popularly known as "false" tocandiras. For this purpose, used two different analytical approaches: (i) gel-based approach, wherein was resolved by denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) all bands were excised analysis; (ii) solution-based components directly fragmented into tryptic peptides solution analysis. proteomic data resulted from these methodologies compared against previously annotated transcriptomic database subsequently, homology search identified transcript products. approach unequivocally nine high molecular mass venom, example, enzymes [hyaluronidase, phospholipase A1, dipeptidyl peptidase glucose dehydrogenase/flavin adenine dinucleotide (FAD) quinone] diverse allergens (homologous red fire Selenopsis invicta) venom-related proteins (major royal jelly-like). Moreover, revealed confirmed presence several hydrolases, oxidoreductases, proteases, Kunitz-like polypeptides, less abundant inhibitor cysteine knot (ICK)-like (knottin) neurotoxins insect defensin. Our results showed major quadriceps are highly likely damage cell membranes tissue, cause neurotoxicity, induce allergic reactions, thus, expanding its potential effects on prey victims.