Dataset Information

Characterization of extracellular vesicles from Bothrops jararaca snake venom

ABSTRACT: 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.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Bothrops Jararaca (jararaca) (bothrops Jajaraca)

TISSUE(S): Venom

SUBMITTER: Larissa Gonçalves Machado

LAB HEAD: Russolina Benedeta Zingali

PROVIDER: PXD037375 | Pride | 2023-03-10

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	NSAF_allpep_MaxPars.csv	Csv
	VL_0002510_RM_Bj_P100k_a.raw	Raw
	VL_0002510_RM_Bj_P100k_a.sqt	Other
	VL_0002510_RM_Bj_P100k_b.raw	Raw
	VL_0002510_RM_Bj_P100k_b.sqt	Other

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Publications

Extracellular Vesicles from <i>Bothrops jararaca</i> Venom Are Diverse in Structure and Protein Composition and Interact with Mammalian Cells.

Gonçalves-Machado Larissa L Verçoza Brunno Renato Farias BRF Nogueira Fábio César Sousa FCS Melani Rafael Donadélli RD Domont Gilberto Barbosa GB Rodrigues Silas Pessini SP Rodrigues Juliany Cola Fernandes JCF Zingali Russolina Benedeta RB

Toxins 20221119 11

Snake venoms are complex cocktails of non-toxic and toxic molecules that work synergistically for the envenoming outcome. Alongside the immediate consequences, chronic manifestations and long-term sequelae can occur. Recently, extracellular vesicles (EVs) were found in snake venom. EVs mediate cellular communication through long distances, delivering proteins and nucleic acids that modulate the recipient cell's function. However, the biological roles of snake venom EVs, including possible cross- ...[more]

PMID: 36422980

Similar Datasets

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.

Project description:Snake venoms have evolved in a few families of Caenophidae, and their toxins have been fine-tuned over the evolutive process into highly effective biochemical weapons with a particular role as a trophic adaptation. However, there are many outstanding questions on how venom contributes to the success of venomous species and their adaptation to different environments. Here we analyze the venoms from sympatric and generalist specimens of B. hyoprora, B. taeniatus, B. b. smaragdinus, B. brazili, and B. atrox collected in the wild of Alto Juruá region at the Amazon Forest aiming to understand whether the venom composition could be a driver or influence the arboreal habitats of B. taeniatus and B. b. smaragdinus, or the successful dispersion of B. atrox across the Amazon Forest. Venom composition and the primary sequences of toxin isoforms were characterized by venom gland transcriptomics followed by proteomics. The venom composition of the five species conserved the same protein families present in venoms of Bothropoid snakes but with remarkable differences in the chromatographic profiles and in the relative amount of each toxin group: CTLs were the most abundant in the venoms of B. taeniatus (31.6%), B. b. smaragdinus (33.0%), and B. atrox (32.0%) and SVMPs and PLA2s dominated in venoms of B. hyoprora (23.7% and 20.2%) and B. brazili (20.2% and 20.4%). Some peculiarities were also observed: B. hyoprora venom was the least complex, conserving important isoforms shared with B. atrox venom; the presence of one cluster of SVSPs exclusive to B. brazili venom isoforms; and the presence of the K49-PLA2 homologs only in B. b. smaragdinus and particularly in B. brazili venoms. The SVMP, SVSP, and PLA2 enzyme activities were consistent with the abundance and type of isoforms present in the venoms. B. hyoprora, B. taeniatus, B. b. smaragdinus, and B. atrox venoms presented low lethality to small rodents, while B. brazili venom was the most lethal. Concluding, differences were evidenced between the venoms of B. taeniatus and B. b. smaragdinus arboreal species, while B. b. smaragdinus shared a venom with a similar composition to B. atrox venom, mostly terrestrial. Considering the role of venom toxicity in species' success for adaptation in different areas, B. atrox is the most adapted in the whole Amazonian territory and presented the least lethal venom, while the venom of B. brazili was the most lethal despite its small distribution in the same area. Therefore, our data suggest that the selection of venom composition may not influence the success or behavior of snake species. In this way, other biotic or abiotic factors influence their foraging status or their dispersal in different ecological niches.