Analysis of post-translational modifications of native and recombinant toxins from Tityus serrulatus venom by mass spectrometry

• Grant number: 13/26083-0
• Support Opportunities: Scholarships abroad - Research Internship - Doctorate
• Start date: September 01, 2014
• End date: February 28, 2015
• Field of knowledge: Health Sciences - Pharmacy - Toxicological Analysis
• Principal Investigator: Eliane Candiani Arantes Braga
• Grantee: Fernanda Gobbi Amorim
• Supervisor: Edwin De Pauw
• Host Institution: Faculdade de Ciências Farmacêuticas de Ribeirão Preto (FCFRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
• Institution abroad: Université de Liège (ULg), Belgium
• Associated to the scholarship: 11/12317-3 - Cloning and heterologous expression of hyaluronidase and/or novel toxins obtained from the transcriptome of Tityus serrulatus' venom gland, BP.DR

Abstract

The Tityus serrulatus venom is constituted by a complex mixture of enzymes, nucleotides, biogenic amines, insoluble mucus, oligopeptides, low molecular weight molecules, protease inhibitors, histamine releasers, aminoacids and other organic components, particularly, many low molar mass peptides with neurotoxic activity. Many of the abundant and toxic components have been isolated and well characterized, however, despite their biotechnological potentials, it is known that several venom components were not yet studied, primarily due to difficulties in obtaining it. Recent development of techniques for the production of biomolecules on a large scale, such as the heterologous expression system, is of great importance, since they enable the provision of new therapeutic agents for the pharmaceutical industry. The monitoring of post-translational modifications is pivotal in heterologous protein expression, once these modifications interfere with their physicochemical, structural and pharmacological properties of the proteins. During the last two decades, mass spectrometry has become a promising analytical tool for quality control of clinically-used protein production, and it allows the highly accurate quantitative and qualitative determination of molecular changes and conformational features. Therefore, this project aims to apply techniques of mass spectrometry in the assessment of post-translational modifications in native and recombinant toxins from T. serrulatus, in order to validate their heterologous expression aiming their potential biotechnological applications. (AU)

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

AMORIM, FERNANDA GOBBI; BOLDRINI-FRANCA, JOHARA; FIGUEIREDO BORDON, KARLA DE CASTRO; CARDOSO, IARA AIME; DE PAUW, EDWIN; QUINTON, LOUC; KASHIMA, SIMONE; ARANTES, ELIANE CANDIANI. Heterologous expression of rTsHyal-1: the first recombinant hyaluronidase of scorpion venom produced in Pichia pastoris system. Applied Microbiology and Biotechnology, v. 102, n. 7, p. 3145-3158, APR 2018. (11/12317-3, 13/26083-0, 12/14996-8)

AMORIM, FERNANDA GOBBI; LONGHIM, HELOISA TAVONI; COLOGNA, CAMILA TAKENO; DEGUELDRE, MICHEL; DE PAUW, EDWIN; QUINTON, LOIC; ARANTES, ELIANE CANDIANI. Proteome of fraction from Tityus serrulatus venom reveals new enzymes and toxins. Journal of Venomous Animals and Toxins including Tropical Diseases, v. 25, APR 18 2019. (14/07824-1, 15/17466-8, 12/14996-8, 13/26083-0, 11/23236-4, 14/22959-0, 13/26200-6)

CERNI, FELIPE AUGUSTO; PUCCA, MANUELA BERTO; AMORIM, FERNANDA GOBBI; FIGUEIREDO BORDON, KARLA DE CASTRO; ECHTERBILLE, JULIEN; QUINTON, LOIC; DE PAUW, EDWIN; PEIGNEUR, STEVE; TYTGAT, JAN; ARANTES, ELIANE CANDIANI. Isolation and characterization of Ts19 Fragment II, a new long-chain potassium channel toxin from Tityus serrulatus venom. Peptides, v. 80, p. 9-17, JUN 2016. (13/21342-7, 12/13590-8, 13/21329-0, 13/26083-0, 11/12317-3)