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

Victor Corassolla Carregari, Livia Rosa-Fernandes, Paulo Baldasso, Sergio Paulo Bydlowski, Sergio Marangoni, Martin R. Larsen, Giuseppe Palmisano*

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Resumé

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.

OriginalsprogEngelsk
Artikelnummer12067
TidsskriftScientific Reports
Vol/bind8
Udgave nummer1
Sider (fra-til)1-16
ISSN2045-2322
DOI
StatusUdgivet - 2018

Fingeraftryk

Proteome
Crotalus
Proteins
Agkistrodon
Disintegrins
Snake Bites
Snakes
Human Umbilical Vein Endothelial Cells
Metalloproteases
Weights and Measures

Citer dette

Carregari, V. C., Rosa-Fernandes, L., Baldasso, P., Bydlowski, S. P., Marangoni, S., Larsen, M. R., & Palmisano, G. (2018). Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity. Scientific Reports, 8(1), 1-16. [12067]. https://doi.org/10.1038/s41598-018-30578-4
Carregari, Victor Corassolla ; Rosa-Fernandes, Livia ; Baldasso, Paulo ; Bydlowski, Sergio Paulo ; Marangoni, Sergio ; Larsen, Martin R. ; Palmisano, Giuseppe. / Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity. I: Scientific Reports. 2018 ; Bind 8, Nr. 1. s. 1-16.
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abstract = "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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Carregari, VC, Rosa-Fernandes, L, Baldasso, P, Bydlowski, SP, Marangoni, S, Larsen, MR & Palmisano, G 2018, 'Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity', Scientific Reports, bind 8, nr. 1, 12067, s. 1-16. https://doi.org/10.1038/s41598-018-30578-4

Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity. / Carregari, Victor Corassolla; Rosa-Fernandes, Livia; Baldasso, Paulo; Bydlowski, Sergio Paulo; Marangoni, Sergio; Larsen, Martin R.; Palmisano, Giuseppe.

I: Scientific Reports, Bind 8, Nr. 1, 12067, 2018, s. 1-16.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity

AU - Carregari, Victor Corassolla

AU - Rosa-Fernandes, Livia

AU - Baldasso, Paulo

AU - Bydlowski, Sergio Paulo

AU - Marangoni, Sergio

AU - Larsen, Martin R.

AU - Palmisano, Giuseppe

PY - 2018

Y1 - 2018

N2 - 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.

AB - 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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DO - 10.1038/s41598-018-30578-4

M3 - Journal article

C2 - 30104604

AN - SCOPUS:85051656675

VL - 8

SP - 1

EP - 16

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

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