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Proteome of fraction from Tityus serrulatus venom reveals new enzymes and toxins
Amorim, Fernanda Gobbi; Longhim, Heloisa Tavoni; Cologna, Camila Takeno; Degueldre, Michel; Pauw, Edwin De; Quinton, Loïc; Arantes, Eliane Candiani.
Afiliação
  • Amorim, Fernanda Gobbi; University of São Paulo. School of Pharmaceutical Sciences of Ribeirão Preto. Department of Physics and Chemistry. Ribeirão Preto. Brasil
  • Longhim, Heloisa Tavoni; University of São Paulo. School of Pharmaceutical Sciences of Ribeirão Preto. Department of Physics and Chemistry. Ribeirão Preto. Brasil
  • Cologna, Camila Takeno; University of São Paulo. School of Pharmaceutical Sciences of Ribeirão Preto. Department of Physics and Chemistry. Ribeirão Preto. Brasil
  • Degueldre, Michel; Liège Université. MolSys Research Unit. Laboratory of mass spectrometry. Liège. Belgium
  • Pauw, Edwin De; Liège Université. MolSys Research Unit. Laboratory of mass spectrometry. Liège. Belgium
  • Quinton, Loïc; Liège Université. MolSys Research Unit. Laboratory of mass spectrometry. Liège. Belgium
  • Arantes, Eliane Candiani; University of São Paulo. School of Pharmaceutical Sciences of Ribeirão Preto. Department of Physics and Chemistry. Ribeirão Preto. Brasil
J. Venom. Anim. Toxins incl. Trop. Dis. ; 25: e148218, Apr. 18, 2019. graf
Article em En | VETINDEX | ID: vti-19272
Biblioteca responsável: BR68.1
ABSTRACT

Background:

Tityus serrulatus venom (Ts venom) is a complex mixture of several compounds with biotechnological and therapeutical potentials, which highlights the importance of the identification and characterization of these components. Although a considerable number of studies have been dedicated to the characterization of this complex cocktail, there is still a limitation of knowledge concerning its venom composition. Most of Ts venom studies aim to isolate and characterize their neurotoxins, which are small, basic proteins and are eluted with high buffer concentrations on cation exchange chromatography. The first and largest fraction from carboxymethyl cellulose-52 (CMC-52) chromatography of Ts venom, named fraction I (Fr I), is a mixture of proteins of high and low molecular masses, which do not interact with the cation exchange resin, being therefore a probable source of components still unknown of this venom. Thus, the present study aimed to perform the proteome study of Fraction I from Ts venom, by high resolution mass spectrometry, and its biochemical characterization, by the determination of several enzymatic activities.

Methods:

Fraction I was obtained by a cation exchange chromatography using 50 mg of crude venom. This fraction was subjected to a biochemical characterization, including determination of L-amino acid oxidase, phospholipase, hyaluronidase, proteases activities and inhibition of angiotensin converting enzyme (ACE) activity. Fraction I was submitted to reduction, alkylation and digestion processes, and the tryptic digested peptides obtained were analyzed in a Q-Exactive Orbitrap mass spectrometer. Data analysis was performed by PEAKS 8.5 software against NCBI database.

Results:

Fraction I exhibits proteolytic activity and it was able to inhibit ACE activity. Its proteome analysis identified 8 different classes of venom components, among them neurotoxins (48%), metalloproteinases (21%), hypotensive peptides...(AU)
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Texto completo: 1 Base de dados: VETINDEX Idioma: En Revista: J. Venom. Anim. Toxins incl. Trop. Dis. Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Base de dados: VETINDEX Idioma: En Revista: J. Venom. Anim. Toxins incl. Trop. Dis. Ano de publicação: 2019 Tipo de documento: Article