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Bothrops jararaca and Crotalus durissus terrificus: plasma proteins responsible for protection against his own accidental poisoning and by crossed envenomation.

Sanches F, Grego KF, Morais-Zani K, Sant´Anna SS, Tanaka-Azevedo AM

Laboratório de Herpetologia, Instituto Butantan, Brasil

Introduction: Snakes are animals that use venom as an effective method not only to capture, but also to help prey digestion. It is know that most venomous snakes are resistant to toxicity of their own venom by different mechanisms of neutralization, such as anti-venom proteins in the plasma of these animals. In addition, some snakes also present protection against venom from others species.  Objectives: This study aims to characterize plasma proteins of Bothrops jararaca and Crotalus durissus terrificus snakes responsible for protection against his own accidental and crossed envenomation. Methods: Venom and plasma samples were provided by the Herpetology Laboratory of the Butantan Institute. These samples were kept at -20°C until analysis. Determination of protein concentration was performed by absorbance at 280 nm on a plate reader (Biotek-Epoch). Plasma samples were subjected to electrophoresis on SDS-PAGE, followed by Western Blotting method. For these experiments, snake plasma was incubated with its own venom and with the other species venom (for example: B. jararaca plasma x C. d. terrificus venom). Results and Discussion: Western blotting showed plasma proteins recognized by both, its own venom and the other species venom proteins. It is important to emphasize that, for crossed recognition, there are some bands around 50 kDa in C. d. terrificus plasma that were strongly recognized by B. jararaca venom proteins, suggesting some defensive mechanism of these animals against other species envenomation. Conclusion: This work showed immunological reaction of B. jararaca and C. d. terrificus to their own and crossed plasma and venom proteins. The next steps are to perform chromatographic experiments in order to purify these proteins and their identification by mass spectrometry.

Supported by Capes, CNPq, FAPESP



10 - BIODIVERSITY 21th Annual Scientific Meeting of Instituto Butantan.