Busca avançada
Ano de início
Entree
(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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

Texto completo
Autor(es):
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]
Número total de Autores: 7
Afiliação do(s) autor(es):
[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
Número total de Afiliações: 4
Tipo de documento: Artigo Científico
Fonte: SCIENTIFIC REPORTS; v. 8, AUG 13 2018.
Citações Web of Science: 2
Resumo

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)

Processo FAPESP: 14/06863-3 - Modificações pós-traducionais para o diagnóstico de câncer e doenças parasitárias: abordagens metodológicas e implicações biológicas
Beneficiário:Giuseppe Palmisano
Linha de fomento: Auxílio à Pesquisa - Apoio a Jovens Pesquisadores