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Open AccessFeature PaperArticle

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

1
Laboratory of Biochemistry and Biophysics, Instituto Butantan, São Paulo SP 05503-900, Brazil
2
Laboratory of Applied Toxinology, CeTICS, Instituto Butantan, São Paulo SP 05503-900, Brazil
3
Laboratory of Genetics, Instituto Butantan, São Paulo SP 05503-900, Brazil
4
Laboratorio of Biochemistry and Biotechnology, Institute for Marine Sciences, Federal University of Ceara, Fortaleza CE 60165-081, Brazil
*
Authors to whom correspondence should be addressed.
Toxins 2019, 11(8), 448; https://doi.org/10.3390/toxins11080448
Received: 2 June 2019 / Revised: 10 July 2019 / Accepted: 26 July 2019 / Published: 29 July 2019
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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. View Full-Text
Keywords: Dinoponera quadriceps; Formicidae; Hymenoptera venom; proteomics; venom allergens; ICK-like toxins Dinoponera quadriceps; Formicidae; Hymenoptera venom; proteomics; venom allergens; ICK-like toxins
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MDPI and ACS Style

Ceolin Mariano, D.O.; de Oliveira, Ú.C.; Zaharenko, A.J.; Pimenta, D.C.; Rádis-Baptista, G.; Prieto-da-Silva, Á.R.B. Bottom-Up Proteomic Analysis of Polypeptide Venom Components of the Giant Ant Dinoponera Quadriceps. Toxins 2019, 11, 448.

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