Exploring the venom of the largest Brazilian venomous snake (Lachesis muta): characterization and bioprospecting.

• Grant number: 23/16574-8
• Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
• Start date: August 01, 2024
• End date: July 31, 2028
• Field of knowledge: Biological Sciences - Physiology - Compared Physiology
• Principal Investigator: Anita Mitico Tanaka-Azevedo
• Grantee: Mariana Silva Tavares
• Host Institution: Instituto Butantan. Secretaria da Saúde (São Paulo - Estado). São Paulo , SP, Brazil

Abstract

Snake bite envenomination is considered a tropical disease neglected according to the World Health Organization (WHO). In Brazil, snakebites accidents is caused mainly by the genus Bothrops, Crotalus and Lachesis. Lachesis spp. represents one of the largest venomous snakes in the world. In Brazil, there is only the species L. muta, with the subspecies L. muta muta being a snake from the amazon region and L. muta rhombeata it is endemic to the Brazilian Atlantic Forest. The venom of Lachesis is composed mainly of metalloproteases, serine proteases, bradykinin potential peptide, phospholipase A2 and C-type lectins. L. muta venom presents several activities, such as coagulation, hemorrhage, proteolytic and neurotoxic activities. It is a clinically important animal in the Amazon region and with great potential for bioprospecting new compounds. However, the venom of Lachesis is not as studied as other genus of the Viperidae family and suffers with the underreporting of cases of snakebite accidents. Therefore, knowing thetoxins is essential to better understand the biology of the animal and how the poison acts on the body, resulting in improvements in treatment and enabling the discovery of new molecules with biotechnological applications. The aim of this work is to biochemically and biologically characterize the venom of the L. muta snake, as well as analyzing possible differences between the subspecies L. muta muta and L. muta rhombeata regarding the composition and activities of the venom. Furthermore, a bioprospective analysis regarding proteins present in L. muta venom will be conducted.