Adaptative advantages of the presence of different metalloproteinases in the composition of Bothrops venoms and implications of this variability in snakebites

• Grant number: 12/23018-0
• Support Opportunities: Scholarships in Brazil - Doctorate
• Start date: March 01, 2013
• End date: July 31, 2016
• Field of knowledge: Biological Sciences - Pharmacology - Biochemical and Molecular Pharmacology
• Principal Investigator: Ana Maria Moura da Silva
• Grantee: Juliana Lech Bernardoni
• Host Institution: Instituto Butantan. Secretaria da Saúde (São Paulo - Estado). São Paulo , SP, Brazil
• Associated scholarship(s): 14/13592-6 - Structural differences between two Bothrops neuwiedi SVMPs class P-I, BE.EP.DR

Abstract

Stand out as key components of the venom of Bothrops snakes proteases such as metalloproteinases and serine proteinases, phospholipases A2 and lectins. Among these components, metalloproteinases (SVMPs) are the most abundant in majority bothropic venoms reaching 38% of the components of B. pauloensis venom. Their action is related to the proteolysis of extracellular matrix components, plasma proteins and cell surface proteins. However, phylogeny, ontogeny, sex, environment or diet can change the composition of the venoms, mainly as the type and abundance of SVMPs. This variability in venom composition has been attributed to a snake adaptative advantage to capture preys and evade predators. However, though plausible, this hypothesis has little experimental evidence. In our Master's project, we identified the presence of several SVMPs in the venom of B. neuwiedi that, in addition to structural differences, showed activity in different targets of the coagulation system of mammals. In this project, our aim is to verify if the variability of SVMPs occurs in the venoms of other species of the genus Bothrops; to isolate the distinct SVMPs from B. neuwiedi venom and test whether there are significant differences in the action of such proteases against different mammalian physiological systems or coagulation systems of different prey/ predators as birds, amphibians and rodents. With this, we aim to understand the implications of variability of venom components in the pathophysiology of envenoming and also generate experimental data to prove the hypothesis that the variability in the composition of venoms result in an adaptive advantage to the species as prey capture and predator avoidance.

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)

SOUSA, LEIJIANE F.; BERNARDONI, JULIANA L.; ZDENEK, CHRISTINA N.; DOBSON, JAMES; COIMBRA, FRANCISCO; GILLETT, AMBER; LOPES-FERREIRA, MONICA; MOURA-DA-SILVA, A. M.; FRY, BRYAN G.. Differential coagulotoxicity of metalloprotease isoforms from Bothrops neuwiedi snake venom and consequent variations in antivenom efficacy. Toxicology Letters, v. 333, p. 211-221, OCT 15 2020. (12/23018-0, 17/15170-0, 14/13124-2)

BERNARDONI, JULIANA L.; SOUSA, LEIJIANE F.; WERMELINGER, LUCIANA S.; LOPES, ALINE S.; PREZOTO, BENEDITO C.; SERRANO, SOLANGE M. T.; ZINGALI, RUSSOLINA B.; MOURA-DA-SILVA, ANA M.. Functional Variability of Snake Venom Metalloproteinases: Adaptive Advantages in Targeting Different Prey and Implications for Human Envenomation. PLoS One, v. 9, n. 10, OCT 14 2014. (12/16277-9, 12/23018-0)