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Comparative proteomic study of Crotalus durissus terrificus white and yellow venoms, with emphasis on hyaluronidase and L-amino acid oxidase enzymes

Grant number: 13/26619-7
Support type:Scholarships abroad - Research
Effective date (Start): May 05, 2014
Effective date (End): July 04, 2014
Field of knowledge:Health Sciences - Pharmacy - Toxicological Analysis
Principal Investigator:Karla de Castro Figueiredo Bordon
Grantee:Karla de Castro Figueiredo Bordon
Host: Juan J. Calvete
Home Institution: Faculdade de Ciências Farmacêuticas de Ribeirão Preto (FCFRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
Local de pesquisa : Consejo Superior de Investigaciones Científicas (CSIC), Spain  

Abstract

Several studies show that the venom of Crotalus durissus terrificus (Cdt) vary significantly in terms of color, amount of protein and biological activity, even among snakes from the same region. This variability and complexity of the venom may be due to ontogenetic and geographical variations and has various implications in therapeutic accidents by snakes. This complicates the selection of antiophidic sera and specimens for the production of them, as well as understanding the nature of the components of the venom and the local and systemic pathological effects of the envenoming. CdtHya1 is the first reported crotalic venom hyaluronidase crotálicas recently isolated by our research group. This enzyme shows high antiedematogenic activity, increases the diffusion of crotoxin and phospholipase A2 and enhances the action of crotoxin. Although the relevance of hyaluronidase in crotalic envenoming, the enzyme is low expressed in the venoms, which has hindered its detection in proteomic transcriptomic studies of snakes of the genus Crotalus. This work aims to analyze the complexity and extent of post-translational modifications of hyaluronidase from Cdt white and yellow venoms using proteomic approaches. This project will be a pioneer in conducting comparative proteomic analysis of Cdt white and yellow venoms after fractionation by ion exchange in an attempt to identify minority proteins unprecedented in databases, contributing to the understanding of the heterogeneity of venoms and the development of more effective antivenoms. Additionally, it is intended to perform a comparative proteomics analysis of L-amino acid oxidase enzyme (LAAO) in the white and yellow venoms, sincethe color of the venom is usually related to the presence of LAAO. These enzymes are present in small amounts in the venom, which restricts their studies. However, the increased sensitivity of proteomic techniques, especially mass spectrometry, provides quick and efficient study of minimal amounts of sample and makes this project viable. (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)
FIGUEIREDO BORDON, KARLA DE CASTRO; COLOGNA, CAMILA TAKENO; FORNARI-BALDO, ELISA CORREA; PINHEIRO-JUNIOR, ERNESTO LOPES; CERNI, FELIPE AUGUSTO; AMORIM, FERNANDA GOBBI; PINO ANJOLETTE, FERNANDO ANTONIO; CORDEIRO, FRANCIELLE ALMEIDA; WIEZEL, GISELE ADRIANO; CARDOSO, IARA AIME; FERREIRA, ISABELA GOBBO; DE OLIVEIRA, ISADORA SOUSA; BOLDRINI-FRANCA, JOHARA; PUCCA, MANUELA BERTO; BALDO, MATEUS AMARAL; ARANTES, ELIANE CANDIANI. From Animal Poisons and Venoms to Medicines: Achievements, Challenges and Perspectives in Drug Discovery. FRONTIERS IN PHARMACOLOGY, v. 11, JUL 24 2020. Web of Science Citations: 0.
BOLDRINI-FRANCA, JOHARA; COLOGNA, CAMILA TAKENO; PUCCA, MANUELA BERTO; FIGUEIREDO BORDON, KARLA DE CASTRO; AMORIM, FERNANDO GOBBI; PINO ANJOLETTE, FERNANDO ANTONIO; CORDEIRO, FRANCIELLE ALMEIDA; WIEZEL, GISELE ADRIANO; CERNI, FELIPE AUGUSTO; PINHEIRO-JUNIOR, ERNESTO LOPES; TANAKA SHIBAO, PRISCILA YUMI; FERREIRA, ISABELA GOBBO; DE OLIVEIRA, ISADORA SOUSA; CARDOSO, LARA AIME; ARANTES, ELIANE CANDIANI. Minor snake venom proteins: Structure, function and potential applications. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, v. 1861, n. 4, p. 824-838, APR 2017. Web of Science Citations: 18.

Please report errors in scientific publications list by writing to: cdi@fapesp.br.