Assessing the Proteomic Activity of the Venom of the Ant<i>Ectatomma tuberculatum</i>(Hymenoptera: Formicidae: Ectatomminae)

Silva, Juliana Rocha da; Souza, Aline Zanotelli de; Pirovani, Carlos Priminho; Costa, Henrique Olival; Silva, Aline; Dias, João Carlos Teixeira; Delabie, Jacques Hubert Charles; Fontana, Renato

doi:10.1155/2018/7915464

Cited by 3 publications

(3 citation statements)

References 49 publications

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“…Another species of similar potential is that of the trap-jaw ant Daceton armigerum that is a common arboreal species in the tree canopy of the rain forests of northern South America. Other promising species include the common Latin American ant Ectatomma tuberculatum and many of the Australian bulldog ants in the genus Myrmecia that have been subject to a variety of studies [24,31]. The venoms of the social wasps in the enormous Old-World genus Ropalidia have been neglected and appear to have potential for new discoveries.…”

Section: Resultsmentioning

confidence: 99%

Pain and Lethality Induced by Insect Stings: An Exploratory and Correlational Study

Schmidt¹

2019

Toxins

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Pain is a natural bioassay for detecting and quantifying biological activities of venoms. The painfulness of stings delivered by ants, wasps, and bees can be easily measured in the field or lab using the stinging insect pain scale that rates the pain intensity from 1 to 4, with 1 being minor pain, and 4 being extreme, debilitating, excruciating pain. The painfulness of stings of 96 species of stinging insects and the lethalities of the venoms of 90 species was determined and utilized for pinpointing future directions for investigating venoms having pharmaceutically active principles that could benefit humanity. The findings suggest several under- or unexplored insect venoms worthy of future investigations, including: those that have exceedingly painful venoms, yet with extremely low lethality—tarantula hawk wasps (Pepsis) and velvet ants (Mutillidae); those that have extremely lethal venoms, yet induce very little pain—the ants, Daceton and Tetraponera; and those that have venomous stings and are both painful and lethal—the ants Pogonomyrmex, Paraponera, Myrmecia, Neoponera, and the social wasps Synoeca, Agelaia, and Brachygastra. Taken together, and separately, sting pain and venom lethality point to promising directions for mining of pharmaceutically active components derived from insect venoms.

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Section: Resultsmentioning

confidence: 99%

Pain and Lethality Induced by Insect Stings: An Exploratory and Correlational Study

Schmidt¹

2019

Toxins

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“…This is particularly true whether the concentrations required to kill or inhibit the microbial growth are closed to the concentrations that provoke (cyto-)toxicity. In fact, venom and venom-peptides from ants and insects commonly cause cell lysis, like hemolysis, and tissue damage that are intrinsic biological properties that contribute to the overall envenomation symptoms [48,49]. Indeed, a number of AMPs are active due to their membranolytic mechanism of action [50,51], therefore these peptides are invariably and potentially cytotoxic whether they are not selective to the pathogen targets.…”

Section: Discussionmentioning

confidence: 99%

Antifungal In Vitro Activity of Pilosulin- and Ponericin-Like Peptides from the Giant Ant Dinoponera quadriceps and Synergistic Effects with Antimycotic Drugs

2020

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Venoms from ants comprise a rich source of bioactive peptides, including antimicrobial peptides. From the proteome and peptidome of the giant ant Dinoponera quadriceps venom, members of five known classes of antimicrobial peptides were disclosed (e.g., dermaseptin-, defensin-, ICK-, pilosulin- and ponericin-like types). Based on comparative analysis, these family members have structural determinants that indicate they could display antimicrobial activities. In previous works, pilosulin- and ponericin-like peptides were demonstrated to be active against bacteria, fungi, and parasites. Herein, the antifungal activity of ponericin- and pilosulin-like peptides were assessed, aiming at the expansion of the knowledge about AMPs in predatory ants and the development of new microbicide strategies to deal with difficult-to-treat fungal infections. Synthetic pilosulin- (Dq-2562, Dq-1503, and Dq-1319) and ponericin-like (Dq-3162) peptides were evaluated for their fungicide and fungistatic activities against different species of Candida, including a drug-resistant clinical strain. The MICs and MLCs were determined for all peptides individually and in combination with general antifungal drugs by the microdilution method. The time-kill kinetic curves were set up by means of a luminescent reagent, of which the light signal is proportional to the number of viable cells. The candicidal synergism observed by the combination of subinhibitory concentrations of peptides and general antimycotic drugs were quantified by the checkerboard test and fluorescent dye permeation assay. The influence of ergosterol on the antifungal activity was verified by supplementation of culture medium. The pilosulin- (Dq-2562 and Dq-1503) and ponericin-like (Dq-3162) were the most active peptides, displaying a broad spectrum of antifungal activity in vitro, with MICs in the range of 0.625 to 10 µM. The combination of peptides and conventional antimycotic drugs displayed a synergistic reduction in the MIC values of individual peptides and drugs, while soluble ergosterol in the culture medium increased the MICs. The fungicide and fungistatic activity of the individual peptides and peptides in combination with antimycotics were time-dependent with a rapid onset of action and long-lasting effect, which involved membrane disruption as an underlying mechanism of their action. Altogether, pilosulin- and ponericin-like peptides from the giant ant D. quadriceps venom display a broad-spectrum of candicidal activity, what allows their inclusion in the row of the antifungal peptides and gives support for further studies on the development of strategies to fight candidiasis.

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“…In fruit fly D. melanogaster , similar enzyme, UniProtKB–P18173 (DHGL_DROME), is responsible for cuticular modification during morphogenesis. Notably, the homologues of glucose dehydrogenase [FAD, quinone] have being identified in the venom proteome of the parasitic ant E. tuberculatum [42], although it was not described as a genuine insect antigen or venom component.…”

Section: Discussionmentioning

confidence: 99%

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

Mariano

Oliveira

Zaharenko

et al. 2019

Toxins

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

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Assessing the Proteomic Activity of the Venom of the AntEctatomma tuberculatum(Hymenoptera: Formicidae: Ectatomminae)

Cited by 3 publications

References 49 publications

Pain and Lethality Induced by Insect Stings: An Exploratory and Correlational Study

Pain and Lethality Induced by Insect Stings: An Exploratory and Correlational Study

Antifungal In Vitro Activity of Pilosulin- and Ponericin-Like Peptides from the Giant Ant Dinoponera quadriceps and Synergistic Effects with Antimycotic Drugs

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

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