Origin and characterization of small membranous vesicles present in the venom of Crotalus durissus terrificus

Souza-Imberg, Andréia; Carneiro, Sylvia Mendes; Giannotti, Karina Cristina; Sant’Anna, Sávio Stefanini; Yamanouye, Norma

doi:10.1016/j.toxicon.2017.06.013

Cited by 10 publications

(14 citation statements)

References 45 publications

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“…Andréia Souza-Imberg et al . reported that the concentration of proteins in the microvesicles extract was 46.00 µg/mL of fresh venom, indicating a 0.1–0.2% of encapsulated versus total proteins 104 . In our study, we obtained 100 µg of proteins encapsulated in snake venom extracellular vesicles starting from 92 mg of total venom proteins loaded on the SEC column, indicating a 0.1% fraction.…”

Section: Resultsmentioning

confidence: 99%

Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity

Carregari

Rosa-Fernandes

Baldasso

et al. 2018

Sci Rep

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Proteins constitute almost 95% of snake venom’s dry weight and are produced and released by venom glands in a solubilized form during a snake bite. These proteins are responsible for inducing several pharmacological effects aiming to immobilize and initiate the pre-digestion of the prey. This study shows that proteins can be secreted and confined in snake venom extracellular vesicles (SVEVs) presenting a size distribution between 50 nm and 500 nm. SVEVs isolated from lyophilized venoms collected from four different species of snakes (Agkistrodon contortrix contortrix, Crotalus atrox, Crotalus viridis and Crotalus cerberus oreganus) were analyzed by mass spectrometry-based proteomic, which allowed the identification of proteins belonging to eight main functional protein classes such as SVMPs, serine proteinases, PLA2, LAAO, 5′nucleotidase, C-type lectin, CRISP and Disintegrin. Biochemical assays indicated that SVEVs are functionally active, showing high metalloproteinase and fibrinogenolytic activity besides being cytotoxic against HUVEC cells. Overall, this study comprehensively depicts the protein composition of SVEVs for the first time. In addition, the molecular function of some of the described proteins suggests a central role for SVEVs in the cytotoxicity of the snake venom and sheds new light in the envenomation process.

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Section: Resultsmentioning

confidence: 99%

Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity

Carregari

Rosa-Fernandes

Baldasso

et al. 2018

Sci Rep

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“…The 5′-NTs and PDEs found here contain a transmembrane region in their primary structure. It was found that some transmembrane proteins, including dipeptidyl peptidase IV, APA, and ecto-5′-nucleotidase, are released by exosomes into the venom gland lumen during venom secretion. , In fact, microvesicles that originated from microvilli fragmentation or budding have been detected in the venom of C. d. terrificus containing ecto-5′-nucleotidase and APN in addition to some cellular proteins. , The proteomic approach showed peptides matched to the same region in all three PDEs identified in the transcriptome, not allowing isoforms identification. On the other hand, regarding the 5′-NTs, only Cdt5′-NT1 was present in this venom.…”

Section: Discussionmentioning

confidence: 99%

In-Depth Venome of the Brazilian Rattlesnake Crotalus durissus terrificus: An Integrative Approach Combining Its Venom Gland Transcriptome and Venom Proteome

et al. 2018

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Snake venoms are complex mixtures mainly composed of proteins and small peptides. Crotoxin is one of the most studied components from Crotalus venoms, but many other components are less known due to their low abundance. The venome of Crotalus durissus terrificus, the most lethal Brazilian snake, was investigated by combining its venom gland transcriptome and proteome to create a holistic database of venom compounds unraveling novel toxins. We constructed a cDNA library from C. d. terrificus venom gland using the Illumina platform and investigated its venom proteome through high resolution liquid chromotography–tandem mass spectrometry. After integrating data from both data sets, more than 30 venom components classes were identified by the transcriptomic analysis and 15 of them were detected in the venom proteome. However, few of them (PLA2, SVMP, SVSP, and VEGF) were relatively abundant. Furthermore, only seven expressed transcripts contributed to ∼82% and ∼73% of the abundance in the transcriptome and proteome, respectively. Additionally, novel venom proteins are reported, and we highlight the importance of using different databases to perform the data integration and discuss the structure of the venom components-related transcripts identified. Concluding, this research paves the way for novel investigations and discovery of future pharmacological agents or targets in the antivenom therapy.

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“…Though svEVs were first observed in 1973 [ 24 ], only four recent studies have shown evidence for snake venom extracellular vesicles and partial characterization [ 25 , 26 , 27 , 28 ]; however, their precise protein content, function, and mechanism/role in snake envenomation remain unknown. In our study, we examined C. atrox and C. o. helleri snake venom-derived extracellular vesicles.…”

Section: Introductionmentioning

confidence: 99%

Proteomic Identification and Quantification of Snake Venom Biomarkers in Venom and Plasma Extracellular Vesicles

Willard

Salazar

Oyervides

et al. 2021

Toxins

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The global exploration of snakebites requires the use of quantitative omics approaches to characterize snake venom as it enters into the systemic circulation. These omics approaches give insights into the venom proteome, but a further exploration is warranted to analyze the venom-reactome for the identification of snake venom biomarkers. The recent discovery of extracellular vesicles (EVs), and their critical cellular functions, has presented them as intriguing sources for biomarker discovery and disease diagnosis. Herein, we purified EV’s from the snake venom (svEVs) of Crotalus atrox and C. oreganus helleri, and from plasma of BALB/c mice injected with venom from each snake using EVtrap in conjunction with quantitative mass spectrometry for the proteomic identification and quantification of svEVs and plasma biomarkers. Snake venom EVs from C. atrox and C. o. helleri were highly enriched in 5′ nucleosidase, L-amino acid oxidase, and metalloproteinases. In mouse plasma EVs, a bioinformatic analysis for revealed upregulated responses involved with cytochrome P450, lipid metabolism, acute phase inflammation immune, and heat shock responses, while downregulated proteins were associated with mitochondrial electron transport, NADH, TCA, cortical cytoskeleton, reticulum stress, and oxidative reduction. Altogether, this analysis will provide direct evidence for svEVs composition and observation of the physiological changes of an envenomated organism.

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Origin and characterization of small membranous vesicles present in the venom of Crotalus durissus terrificus

Cited by 10 publications

References 45 publications

Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity

Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity

In-Depth Venome of the Brazilian Rattlesnake Crotalus durissus terrificus: An Integrative Approach Combining Its Venom Gland Transcriptome and Venom Proteome

Proteomic Identification and Quantification of Snake Venom Biomarkers in Venom and Plasma Extracellular Vesicles

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