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

Ectatomma tuberculatum has one of the most toxic venoms known among ants but there is no detailed study on its characteristics. In light of this, knowing the venom’s chemical composition is of paramount importance in order to obtain information about the mechanisms of its components. Several bioacti...

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Main Authors: Juliana Rocha da Silva, Aline Zanotelli de Souza, Carlos Priminho Pirovani, Helena Costa, Aline Silva, João Carlos Teixeira Dias, Jacques Hubert Charles Delabie, Renato Fontana
Format: Article
Language:English
Published: Wiley 2018-01-01
Series:Psyche: A Journal of Entomology
Online Access:http://dx.doi.org/10.1155/2018/7915464
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author Juliana Rocha da Silva
Aline Zanotelli de Souza
Carlos Priminho Pirovani
Helena Costa
Aline Silva
João Carlos Teixeira Dias
Jacques Hubert Charles Delabie
Renato Fontana
author_facet Juliana Rocha da Silva
Aline Zanotelli de Souza
Carlos Priminho Pirovani
Helena Costa
Aline Silva
João Carlos Teixeira Dias
Jacques Hubert Charles Delabie
Renato Fontana
author_sort Juliana Rocha da Silva
collection DOAJ
description Ectatomma tuberculatum has one of the most toxic venoms known among ants but there is no detailed study on its characteristics. In light of this, knowing the venom’s chemical composition is of paramount importance in order to obtain information about the mechanisms of its components. Several bioactive molecules have already been identified in Hymenoptera venoms, i.e., proteins such as phospholipases, hyaluronidases, and proteinases, as well as peptides. Protein databases show that information on protein components of ant venoms has been recently growing exponentially. In this study, we have identified proteins from the venom of Ectatomma tuberculatum by means of 2D PAGE, followed by tandem nanochromatography with mass spectrometry. A total of 48 proteins were identified, of which 42 are involved in metabolic processes, transport, and structural support. Moreover, six of them show similarity with not yet characterized proteins. Nine proteins are related to the attack/defense or maintenance process of the colony (colony asepsis, conservation of venom constituents, venom diffusion on prey, paralysis of prey, alteration of homeostasis, and cellular toxicity). Our findings may contribute to the identification of new natural prototypes of molecules to be synthesized and used in several areas of pharmacology.
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publishDate 2018-01-01
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series Psyche: A Journal of Entomology
spelling doaj-art-8874fe60b0bf42aa9ba5995f9935a8bf2025-02-03T05:43:44ZengWileyPsyche: A Journal of Entomology0033-26151687-74382018-01-01201810.1155/2018/79154647915464Assessing the Proteomic Activity of the Venom of the Ant Ectatomma tuberculatum (Hymenoptera: Formicidae: Ectatomminae)Juliana Rocha da Silva0Aline Zanotelli de Souza1Carlos Priminho Pirovani2Helena Costa3Aline Silva4João Carlos Teixeira Dias5Jacques Hubert Charles Delabie6Renato Fontana7Universidade Estadual de Santa Cruz (UESC), Programa de Pós-Graduação em Biologia e Biotecnologia de Microrganismos (PPGBBM), 45.662-900 Ilhéus, BA, BrazilUniversidade Estadual de Santa Cruz (UESC), Ilhéus, BA, BrazilUniversidade Estadual de Santa Cruz (UESC), Ilhéus, BA, BrazilUniversidade Estadual de Santa Cruz (UESC), Ilhéus, BA, BrazilUniversidade Estadual de Santa Cruz (UESC), Ilhéus, BA, BrazilUniversidade Estadual de Santa Cruz (UESC), Ilhéus, BA, BrazilUniversidade Estadual de Santa Cruz (UESC), Ilhéus, BA, BrazilUniversidade Estadual de Santa Cruz (UESC), Ilhéus, BA, BrazilEctatomma tuberculatum has one of the most toxic venoms known among ants but there is no detailed study on its characteristics. In light of this, knowing the venom’s chemical composition is of paramount importance in order to obtain information about the mechanisms of its components. Several bioactive molecules have already been identified in Hymenoptera venoms, i.e., proteins such as phospholipases, hyaluronidases, and proteinases, as well as peptides. Protein databases show that information on protein components of ant venoms has been recently growing exponentially. In this study, we have identified proteins from the venom of Ectatomma tuberculatum by means of 2D PAGE, followed by tandem nanochromatography with mass spectrometry. A total of 48 proteins were identified, of which 42 are involved in metabolic processes, transport, and structural support. Moreover, six of them show similarity with not yet characterized proteins. Nine proteins are related to the attack/defense or maintenance process of the colony (colony asepsis, conservation of venom constituents, venom diffusion on prey, paralysis of prey, alteration of homeostasis, and cellular toxicity). Our findings may contribute to the identification of new natural prototypes of molecules to be synthesized and used in several areas of pharmacology.http://dx.doi.org/10.1155/2018/7915464
spellingShingle Juliana Rocha da Silva
Aline Zanotelli de Souza
Carlos Priminho Pirovani
Helena Costa
Aline Silva
João Carlos Teixeira Dias
Jacques Hubert Charles Delabie
Renato Fontana
Assessing the Proteomic Activity of the Venom of the Ant Ectatomma tuberculatum (Hymenoptera: Formicidae: Ectatomminae)
Psyche: A Journal of Entomology
title Assessing the Proteomic Activity of the Venom of the Ant Ectatomma tuberculatum (Hymenoptera: Formicidae: Ectatomminae)
title_full Assessing the Proteomic Activity of the Venom of the Ant Ectatomma tuberculatum (Hymenoptera: Formicidae: Ectatomminae)
title_fullStr Assessing the Proteomic Activity of the Venom of the Ant Ectatomma tuberculatum (Hymenoptera: Formicidae: Ectatomminae)
title_full_unstemmed Assessing the Proteomic Activity of the Venom of the Ant Ectatomma tuberculatum (Hymenoptera: Formicidae: Ectatomminae)
title_short Assessing the Proteomic Activity of the Venom of the Ant Ectatomma tuberculatum (Hymenoptera: Formicidae: Ectatomminae)
title_sort assessing the proteomic activity of the venom of the ant ectatomma tuberculatum hymenoptera formicidae ectatomminae
url http://dx.doi.org/10.1155/2018/7915464
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