Banca de DEFESA: MARLEI NOVAES DE SOUSA

Uma banca de DEFESA de MESTRADO foi cadastrada pelo programa.
STUDENT : MARLEI NOVAES DE SOUSA
DATE: 27/06/2022
TIME: 14:30
LOCAL: Sala Virtual Remota
TITLE:

KEY WORDS:

Snake venom, Bothrops jararacussu, metalloprotease, bacteria multidrug resistant, antimicrobial action.

PAGES: 61
BIG AREA: Ciências Biológicas
AREA: Biologia Geral
SUMMARY:

Snake venoms contain a mixture of molecules capable of mediating directly or indirectly inflammatory, hemorrhagic, neurotoxic, myotoxic and other cellular changes. In this context the metalloproteases, which are enzymes highly toxic profile, zinc dependent and of variable molecular mass, playing a relevant role in the complex and multifactorial response characteristic of the snake poisoning. In this pointing of view, several studies with snake venoms seek to find substances with possible potential therapeutic application for the development and drug improvement, demonstrating a beneficial characteristic for these biological molecules. Therefore, this work aims to evaluate in vitro the antimicrobial action from the Bothrops jararacussu snake venom, as well as from an isolated metalloprotease. To obtain the metalloprotease, it was necessary to fractionate the venom by liquid chromatography, using a CM-Sepharose-type ion-exchange column and the choice of fraction corresponding to the protein of interest was based on its electrophoretic characteristics (SDS-PAGE), molecular mass (mass spectrometry) and enzyme activity (fibrinogenolytic and caseinolytic). The results showed that the metalloprotease was purified with a satisfactory yield and adequate purity, representing about 5.4% of the total venom and presenting a single polypeptide chain with a molecular mass between 23 and 24 kDa, classifying it as a P1 class metalloprotease. This enzyme showed metal ion-dependent proteolytic activity, confirming that it belongs to the class of metalloproteases from snake venoms. It was also observed that this metalloprotease was capable of inducing hemorrhage in vivo in the cremaster muscle of mice analyzed by intravital microscopy. In antimicrobial activities, Bothrops jararacussu venom, showed inhibition at some concentrations tested in two ATCCs strains (100, 50, 25, 12.5 μL/mL for Klebsiella pneumoniae and 100 and 50 μL/mL for Stapylococcus aureus), however, the different concentrations of metalloprotease tested were not able to inhibit the bacterial growth. Finally, the data presented in this study support the biochemical and functional characterization of the protein under study, but they differ from other published studies regarding antimicrobial activity. Other work must be carried out to verify the pharmacological potential of metalloproteases, as well as other components of snake venom, which have a significant contribution to scientific knowledge with important biotechnological applications for human health.

BANKING MEMBERS:
Presidente - 004.161.386-40 - ANDREIMAR MARTINS SOARES - FIOCRUZ
Interna - 582.482.422-34 - NAJLA BENEVIDES MATOS - UNIR
Externo à Instituição - STELLA REGINA ZAMUNER - USP