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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Carregari, Victor Corassolla [1, 2] ; Rosa-Fernandes, Livia [3, 2] ; Baldasso, Paulo [1] ; Bydlowski, Sergio Paulo [4] ; Marangoni, Sergio [1] ; Larsen, Martin R. [3] ; Palmisano, Giuseppe [2]
Total Authors: 7
Affiliation:
[1] State Univ Campinas UNICAMP, Inst Biol IB, Dept Biochem, Fac Med Sci, Campinas, SP - Brazil
[2] Univ Sao Paulo, Dept Parasitol, GlycoProte Lab, ICB, Sao Paulo - Brazil
[3] Univ Southern Denmark, Dept Biochem & Mol Biol, Odense - Denmark
[4] Univ Sao Paulo, Lab Genet & Mol Hematol LIM31, Med Sch FMUSP, Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: SCIENTIFIC REPORTS; v. 8, AUG 13 2018.
Web of Science Citations: 2
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, PLA(2), 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. (AU)

FAPESP's process: 14/06863-3 - Post-translational modifications in cancer and parasite infection diagnosis: methodological approaches and biological implications
Grantee:Giuseppe Palmisano
Support type: Research Grants - Young Investigators Grants