Comprehensive analysis of peptides and low molecular weight components of the giant ant Dinoponera quadriceps venom

Author:

Rádis-Baptista Gandhi1,Dodou Hilania V.12,Prieto-da-Silva Álvaro R.B.3,Zaharenko André J.3,Kazuma Kohei45,Nihei Ken-ichi6,Inagaki Hidetoshi7,Mori-Yasumoto Kanami8,Konno Katsuhiro4

Affiliation:

1. Laboratory of Biochemistry and Biotechnology, Institute for Marine Sciences, Federal University of Ceara, Av da Abolição 3207, Fortaleza 60165-081, CE, Brazil

2. Post-Graduate Program in Pharmaceutical Sciences, Federal University of Ceara, Fortaleza 60020-181, CE, Brazil

3. Laboratory of Genetics, Butantan Institute, Sao Paulo 05503-900, SP, Brazil

4. Institute of Natural Medicine, University of Toyama, Toyama 930-0194, Japan

5. present address: Eco-Frontier Center of Medicinal Resources, School of Pharmacy, Kumamoto University, 5-1 Oe, Chuo-ku, Kumamoto 862-0973, Japan

6. Faculty of Agriculture, Utsunomiya University, Utsunomiya, Tochigi 321-8505, Japan

7. Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8565, Japan

8. Faculty of Pharmaceutical Sciences at Kagawa Campus, Tokushima Bunri University, Sanuki, Kagawa 769-2193, Japan

Abstract

AbstractAnts (Hymenoptera, Apocrita, Aculeata, Formicoidea) comprise a well-succeeded group of animals. Like bees and wasps, ants are mostly venomous, having a sting system to deliver a mixture of bioactive organic compounds and peptides. The predatory giant ant Dinoponera quadriceps belongs to the subfamily Ponerinae that includes one of the largest known ant species in the world. In the present study, low molecular weight compounds and peptides were identified by online peptide mass fingerprint. These include neuroactive biogenic amines (histamine, tyramine, and dopamine), monoamine alkaloid (phenethylamine), free amino acids (e.g. glutamic acid and proline), free thymidine, and cytosine. To the best of our knowledge, most of these components are described for the first time in an ant venom. Multifunctional dinoponeratoxin peptide variants (pilosulin- and ponericin-like peptides) were characterized that possess antimicrobial, hemolytic, and histamine-releasing properties. These venom components, particularly peptides, might synergistically contribute to the overall venom activity and toxicity, for immobilizing live prey, and for defending D. quadriceps against aggressors, predators, and potential microbial infection.

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Biology,Biochemistry

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