Characterization of post-translation modifications of an L-amino acid oxidase isolated from Crotalus durissus terrificus snake venom

• Grant number: 14/23285-3
• Support Opportunities: Scholarships abroad - Research Internship - Master's degree
• Start date: March 01, 2015
• End date: August 31, 2015
• Field of knowledge: Health Sciences - Pharmacy - Toxicological Analysis
• Principal Investigator: Eliane Candiani Arantes Braga
• Grantee: Gisele Adriano Wiezel
• Supervisor: Beatrix Ueberheide
• Host Institution: Faculdade de Ciências Farmacêuticas de Ribeirão Preto (FCFRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
• Institution abroad: NYU Langone Medical Center, United States
• Associated to the scholarship: 14/06170-8 - Biochemical and in vitro evaluation of fibroblast activation and leishmanicidal potential of an L-amino acid oxidase (LAAO) from Crotalus durissus terrificus venom, BP.MS

Abstract

Ophidian accidents are considered a serious public health problem in tropical countries and snake venoms from Crotalus genus is the most lethal one in Brazil. Among this genus, Crotalus durissus terrificus is the most abundant subspecies. Venom is the result of an evolutionary process of some snakes and presents multiple functions including immobilization, death and digestion of the prey. Snakes venoms are composed by mixtures of proteins, peptides and mineral and organic compounds that affect a huge variety of biological process. Many of these components are bioactive molecules of high scientific interest due to their important roles in envenoming and their high therapeutic potential. The study of these toxins can contribute to the development of new drugs and more specific antivenoms. L-amino acid oxidases (LAAOs) are flavoenzymes which catalyse the oxidation of L-amino acids concomitantly producing hydrogen peroxide and ammonia. Many biological activities have been reported for LAAOs, including apoptosis induction, changes in platelet aggregation, antitumor, antibacterial, antiviral and antiparasitic activities and activation of immune cells. However, snake venom LAAOs usually show some instability after freezing and freeze-drying, causing a reduction in catalytic activity, which hinders their biotechnological application. Thereby, the aim of this study is to characterize post-translational modifications (glycosylation and pattern of disulfide bonds) of an L-amino acid oxidase isolated from C. d. terrificus snake venom through modern tools of mass spectrometry. Studies of structural and functional characterization are required to broaden the understanding of structure-function relationship of this enzyme, which may lead to the development of strategies to increase its stability, enabling its biotechnological use. (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)

CORDEIRO, FRANCIELLE ALMEIDA; COUTINHO, BARBARA MARQUES; WIEZEL, GISELE ADRIANO; FIGUEIREDO BORDON, KARLA DE CASTRO; BREGGE-SILVA, CRISTIANE; ROSA-GARZON, NATHALIA GONSALES; CABRAL, HAMILTON; UEBERHEIDE, BEATRIX; ARANTES, ELIANE CANDIANI. Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata snake venom. Journal of Venomous Animals and Toxins including Tropical Diseases, v. 24, NOV 22 2018. (14/23285-3, 11/23236-4)

WIEZEL, GISELE A.; RUSTIGUEL, JOANE K.; MORGENSTERN, DAVID; ZOCCAL, KARINA E.; FACCIOLI, LUCIA H.; CRISTINA NONATO, M.; UEBERHEIDE, BEATRIX; ARANTES, ELIANE C.. Insights into the structure, function and stability of bordonein-L, the first L-amino acid oxidase from Crotalus durissus terrificus snake venom. Biochimie, v. 163, p. 33-49, AUG 2019. (14/03332-7, 11/23236-4, 15/24010-0, 14/23285-3, 14/06170-8, 14/07125-6)

WIEZEL, GISELE A.; BORDON, KARLA C. F.; SILVA, RONIVALDO R.; GOMES, MARIO S. R.; CABRAL, HAMILTON; RODRIGUES, VERIDIANA M.; UEBERHEIDE, BEATRIX; ARANTES, ELIANE C.. Subproteome of Lachesis muta rhombeata venom and preliminary studies on LmrSP-4, a novel snake venom serine proteinase. Journal of Venomous Animals and Toxins including Tropical Diseases, v. 25, APR 15 2019. (10/06199-5, 14/23285-3, 15/18432-0, 11/23236-4)