Effects of a metalloprotease and an acidic Phospholipase A2 from Bothrops atrox snake venom on the complement system and the inflammatory process

• Grant number: 12/11963-1
• Support type: Scholarships in Brazil - Post-Doctorate
• Effective date (Start): March 01, 2013
• Effective date (End): November 30, 2015
• Field of knowledge: Health Sciences - Pharmacy
• Principal Investigator: Suely Vilela
• Grantee: Danilo Luccas Menaldo
• Home Institution: Faculdade de Ciências Farmacêuticas de Ribeirão Preto (FCFRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
• Associated research grant: 11/23236-4 - Native and recombinant animal toxins: functional, structural and molecular analysis, AP.TEM

Abstract

Snake venoms are complex mixtures of inorganic and organic compounds constituted mainly of proteins and peptides. Among their toxic components are the metalloproteases, enzymes responsible for various local and systemic effects such as hemorrhage, myonecrosis, skin lesions, inflammation and activation of the complement system. Other toxic components are the phospholipases A2 (PLA2s), which act hydrolytically on membrane phospholipids and may present myotoxic, cardiotoxic, neurotoxic, hemolytic and inflammatory effects. This project aims at assessing the individual and synergistic effects of two enzymes previously isolated and partially characterized from the venom of Bothrops atrox (a PI class metalloprotease called Batroxase, and an acidic phospholipase A2 called BaPLA2-IV) on the complement system and the inflammatory process. The results obtained in this work should bring scientific advancements for understanding the still poorly studied effects of these classes of enzymes on the inflammatory processes induced after Bothrops envenomation. According to these data, possible actions of these toxins regarding epigenetic changes that culminate in alterations in the protein profile of the studied cells could be suggested, allowing a possible renewal of the scholarship for the determination of how these changes could be related to the immune response induced after the ophidian accident.

Scientific publications

(5)

(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)

MENALDO, DANILO L.; BERNARDES, CAROLINA P.; ZOCCAL, KARINA F.; JACOB-FERREIRA, ANNA L.; COSTA, TASSIA R.; DEL LAMA, MARIA P. F. M.; NAAL, ROSE M. Z. G.; FRANTZ, FABIANI G.; FACCIOLI, LUCIA H.; SAMPAIO, SUELY V. Immune cells and mediators involved in the inflammatory responses induced by a P-I metalloprotease and a phospholipase A(2) from Bothrops atrox venom. Molecular Immunology, v. 85, p. 238-247, MAY 2017. Web of Science Citations: 7.

MENALDO, DANILO L.; BERNARDES, CAROLINA P.; JACOB-FERREIRA, ANNA L.; NOGUEIRA-SANTOS, CINTIA G.; CASARE-OGASAWARA, TANIA M.; PEREIRA-CROTT, LUCIANA S.; SAMPAIO, SUELY V. Effects of Bothrops atrox venom and two isolated toxins on the human complement system: Modulation of pathways and generation of anaphylatoxins. Molecular Immunology, v. 80, p. 91-100, DEC 2016. Web of Science Citations: 5.

MENALDO, DANILO L.; JACOB-FERREIRA, ANNA L.; BERNARDES, CAROLINA P.; CINTRA, ADELIA C. O.; SAMPAIO, SUELY V. Purification procedure for the isolation of a P-I metalloprotease and an acidic phospholipase A(2) from Bothrops atrox snake venom. Journal of Venomous Animals and Toxins including Tropical Diseases, v. 21, AUG 13 2015. Web of Science Citations: 9.

DANILO L. MENALDO; ANNA L. JACOB-FERREIRA; CAROLINA P. BERNARDES; ADÉLIA C. O. CINTRA; SUELY V. SAMPAIO. Purification procedure for the isolation of a P-I metalloprotease and an acidic phospholipase A 2 fromBothrops atrox snake venom. Journal of Venomous Animals and Toxins including Tropical Diseases, v. 21, p. 0-0, 2015.

COSTA, TASSIA R.; BURIN, SANDRA M.; MENALDO, DANILO L.; DE CASTRO, FABIOLA A.; SAMPAIO, SUELY V. Snake venom L-amino acid oxidases: an overview on their antitumor effects. Journal of Venomous Animals and Toxins including Tropical Diseases, v. 20, JUN 2 2014. Web of Science Citations: 39.