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

doi:10.1038/s41598-018-30578-4

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

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

27 Downloads (Pure)

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.

Original language	English
Article number	12067
Pages (from-to)	1-16
Number of pages	16
Journal	Scientific Reports
Volume	8
DOIs	https://doi.org/10.1038/s41598-018-30578-4
Publication status	Published - 2018
Externally published	Yes

Bibliographical note

Copyright the Author(s) 2018. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

A correction exists for this article, and can be found in Scientific Reports 8, art:15908 (2018) at doi: 10.1038/s41598-018-33284-3

Access to Document

10.1038/s41598-018-30578-4Licence: CC BY

Publisher version (open access)Final published version, 1.98 MBLicence: CC BY

Cite this

@article{f2e89c746fb94995bc7fc2c4511aabaa,

title = "Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity",

abstract = "Proteins constitute almost 95% of snake venom{\textquoteright}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.",

author = "Carregari, {Victor Corassolla} and Livia Rosa-Fernandes and Paulo Baldasso and Bydlowski, {Sergio Paulo} and Sergio Marangoni and Larsen, {Martin R.} and Giuseppe Palmisano",

note = "Copyright the Author(s) 2018. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher. A correction exists for this article, and can be found in Scientific Reports 8, art:15908 (2018) at doi: 10.1038/s41598-018-33284-3",

year = "2018",

doi = "10.1038/s41598-018-30578-4",

language = "English",

volume = "8",

pages = "1--16",

journal = "Scientific Reports",

issn = "2045-2322",

publisher = "Springer, Springer Nature",

}

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

N1 - Copyright the Author(s) 2018. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher. A correction exists for this article, and can be found in Scientific Reports 8, art:15908 (2018) at doi: 10.1038/s41598-018-33284-3

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.

UR - http://www.scopus.com/inward/record.url?scp=85055184628&partnerID=8YFLogxK

UR - https://doi.org/10.1038/s41598-018-33284-3

U2 - 10.1038/s41598-018-30578-4

DO - 10.1038/s41598-018-30578-4

M3 - Article

C2 - 30104604

SN - 2045-2322

VL - 8

SP - 1

EP - 16

JO - Scientific Reports

JF - Scientific Reports

M1 - 12067

ER -

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

Abstract

Bibliographical note

Access to Document

Other files and links

Fingerprint

Cite this