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Envenomation by Bothrops leucurus

ABSTRACT: Bothrops spp. is responsible for about 70% of snakebites, causing a diverse and complex pathophysiology, ranging from local to systemic effects in Brazil. Bothrops leucurus is the most common species in the Atlantic range of the Northeast and the main species of medical relevance in the region. Although the influence of the variability of Bothrops venom on the pathology, and the importance of B. leucurus is recognized, the pathophysiological effects involved in snakebite by this species, as well as the reaction of organisms in response to the envenoming have not been explored. We identify the plasma proteins that are affected in terms of abundance during envenoming, and their reflection in the face of biological and pathophysiological processes associated with the local tissue damage caused by snake venom B. leucurus.

INSTRUMENT(S): Q-Exactive (Thermo Fisher)

ORGANISM(S): Bothrops Leucurus

SUBMITTER: Joeliton dos Santos Cavalcante Lucilene Delazari dos Santos

PROVIDER: MSV000087544 | MassIVE | Sun May 30 13:17:00 BST 2021

REPOSITORIES: MassIVE

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Project description:Snake venoms are complex protein mixtures with different biological activities that can act in both their preys and human victims. Many of these proteins play a role in prey capture and in the digestive process of these animals. It is known that some snakes are resistant to the toxicity of their own venom by mechanisms not yet fully elucidated. However, it was observed in the Laboratory of Herpetology of Instituto Butantan that some Bothrops moojeni individuals injured by the same snake species showed mortalities caused by envenoming effects. This study analyzed the biochemical composition of 13 venom and plasma samples from Bothrops moojeni specimens to assess differences in their protein composition. Application of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed distinct venom protein profiles, but very homogeneous plasma profiles. Western Blotting (WB) was performed with plasma samples, which were submitted to incubation with the respective venom. Some individuals showed an immunorecognized band zone around 25 kDa, indicating interaction between the same individual plasma and venom proteins. Crossed-WB assay using non-self-plasma and venom showed that this variability is due to venom protein composition instead of plasma composition. These venoms presented higher caseinolytic, collagenolytic and coagulant activities than the venoms without these regions recognized by WB. Mass spectrometry analysis revealed that these individuals present, in addition to higher protein concentrations, other exclusive proteins in their composition. When these samples were tested in vivo, the results also showed higher lethality in these venoms, but lower hemorrhagic activity than in the venoms without these regions recognized by WB. In conclusion, some Bothrops moojeni specimens differ in venom composition, which may have implications in envenomation. Moreover, the high individual venom variability found in this species demonstrates the importance to work with individual analysis in studies involving intraspecific venom variability and venom evolution.

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Envenomation by Bothrops leucurus

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