Diversidade funcional das metaloproteinases do veneno de Bothrops neuwied

Abstract

The snake venom metalloproteinases (SVMPs) are abundant enzymes in the venoms of viper snakes and responsible for most of the symptoms of envenoming. Their actions are related to the hydrolysis of extracellular matrix components, plasma proteins and hydrolysis or binding to cell surface proteins resulting in the activation or inhibition of their activity. In this work, the main objective was to analyze the implications of the structural and functional diversity of B. neuwiedi venom SVMPs, evaluating their effects on mammal’s hemostatic disorders and against prey or predator of snakes. Initially, we elucidated the partial amino acid sequence of class P-I SVMPs (which presented only 78% similarity to each other), in addition to obtaining the crystal of one. Subsequently we identified different degrees of hemorrhage induced by class P-III SVMPs (with hemorrhagic minimum doses of: 3.08 μg for Ic, 5.67 μg for IIb and 7.55 μg for IIc). In addition, different actions of the SVMPs tested (both P-I and P-III) were observed against extracellular matrix components (adhesion and cleavage) and against endothelial cells (adhesion and viability). It was also observed in the coagulation experiment, the presence of SVMPs that specifically acted on mammalian blood, as well as others that acted only on bird blood, demonstrating a selective action of SVMPs. With this we conclude that there must be the contribution of other factors, besides the structural domains, to the functional diversity of SVMPs. Therefore, the functional diversity of SVMPs contributed to the adaptive role of snake venoms. Key words: Bothrops, metalloproteinases, hemostasis, proteolytic e