Characterization of extracellular vesicles from Bothrops jararaca snake venom

Venoms are important evolutionary keys and innovation for several animal taxons., including snakes. Their use is specially related to feed, predation and defense. Snake venoms are composed mainly by free secreted proteins, about 98%, and stored in the lumen of the venom gland, where they are processed through poorly understood mechanisms. In the perspective of protein-diversity, venoms undergo evolutionary pressure which generate a rapid evolutionary response, causing a great diversity in their toxin-components. We know now that extracellular vesicles exist in snake venom, although their biological role are still unknown. We believe that understanding EV-mediated effects could change our way of seeing envenoming, especially long-term sequelae. From what we know about EVs and snake venoms, there is a lot of potential of cross-organism communication occurrence between snakes and human victims. To advance in the comprehension of venom EVs function, we used fresh B. jararaca venom as our model. Fresh venom was fractionated by sequential centrifugation, resulting in two populations of vesicles (Bj-EVs). Purified Bj-EVs were analyzed by electron microscopy, NTA and proteomics. The interaction of Bj-EVs with mammalian cells was accessed by fluorescence and electron microscopy.