Biological and Enzymatic Characterization of Proteases from Crude Venom of the Ant Odontomachus bauri

Abstract

Hymenoptera venoms constitute an interesting source of natural toxins that may lead to the development of novel therapeutic agents. The present study investigated the enzymatic and biological characteristics of the crude venom of the ant Odontomachus bauri. Its crude venom presents several protein bands, with higher staining for six proteins with gelatinolytic activity (17, 20, 26, 29, 43 and 48 kDa). The crude venom showed high proteolytic activity on azocasein at optimal pH 8.0 and 37 °C. In the presence of protease inhibitors as aprotinin, leupeptin and EDTA, the azocaseinolytic activity was reduced by 45%, 29% and 9%, respectively, suggesting that the enzymes present in the crude venom belong to the three classes of proteases, with the serine proteases in greater intensity. The crude venom degraded the fibrinogen α-chain faster than the β-chain, while the fibrinogen γ-chain remained unchanged. In biological assays, O. bauri venom showed hemolytic and coagulant activity in vitro, and defibrinating activity in vivo. In addition, the venom showed antimicrobial activity against Staphylococcus aureus and Escherichia coli as well as antiparasitic activity on Toxoplasma gondii infection in vitro. In that sense, this study sheds perspectives for pharmacological applications of O. bauri venom enzymes.

Shedding Lights on Crude Venom from Solitary Foraging Predatory Ant Ectatomma opaciventre: Initial Toxinological Investigation

“…Moreover, when we combined the results from the influence of different divalent cations on enzymatic activity, we can also suggest the presence of an ion-dependent enzyme, such as metalloproteinase. In agreement with our results, several proteases were identified and characterized in the crude venom of the ant Odontomachus bauri by collagen zymogram assay [45]. In addition, hyaluronidases from invertebrate and vertebrate venom animals were already described using polyacrylamide gel co-polymerized with hyaluronan [46], which corroborate with our data and conclusions.…”

Analysis of Protein Composition and Bioactivity of Neoponera villosa Venom (Hymenoptera: Formicidae)

“…Similarly, Lee et al [ 25 ] worked with Brachyponera chinensis venom and observed higher protein density between 12 and 85 kDa. Silva et al [ 31 ] analyzed Odontomachus bauri venom, and isolated proteins with molecular weight ranging from 18 to 160 kDa under nonreducing conditions, with more intense staining for bands above 29 kDa. Under reducing conditions, the electrophoretic profile changed, showing a wider range, from 24 to 160 kDa.…”

Composition and Acute Inflammatory Response from Tetraponera rufonigra Venom on RAW 264.7 Macrophage Cells

“…The Ectatomma brunneum ants collected from different environmental conditions, such as urban, intermediate, wood-land, and monoculture sites significantly showed different chemical profiles of the venoms [ 23 ]. Moreover, the dietary and nest site could alter the venom chemical profile [ 23 , 24 ]. The population ecology of T. rufonigra was observed in Penang Island, Malaysia, demonstrating a genetic divergence even through studies in nearby locations [ 25 ].…”