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(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.)

Characterising the enzymatic profile of crude tentacle extracts from the South Atlantic jellyfish Olindias sambaquiensis (Cnidaria: Hydrozoa)

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Autor(es):
Knittel, Paloma S. ; Long, Paul F. ; Brammall, Lucas ; Marques, Antonio C. ; Almeida, Michelle T. ; Padilla, Gabriel ; Moura-da-Silva, Ana M.
Número total de Autores: 7
Tipo de documento: Artigo Científico
Fonte: Toxicon; v. 119, p. 1-7, SEP 1 2016.
Citações Web of Science: 10
Resumo

Jellyfish venoms are of medical and biotechnological importance, with toxins displaying antimicrobial, analgesic and anti-tumor activities. Although proteolytic enzymes have also been described, detailed characterisation of these proteins is scant in Olindias spp. High throughput mass spectrometry profiling of cnidarian venoms has become increasingly popular since the first description of the proteomic profile of putative toxins isolated from nematocysts of the hydrozoan jellyfish Olindias sambaquiensis describing the presence of orthologous enzymes as presented in venoms of advanced species as snakes. Rigorous bioinformatics analyses can aid functional annotation, but biochemical assays are prerequisite to unambiguously assign toxic function to a peptide or protein. Here we present results that experimentally confirm previously predicted proteomic analysis that crude venom extracts from tentacles of O. sambaquiensis are composed of polypeptides with metalloproteinase, serine proteinase and phospholipases A(2) activities. Surprisingly, levels of serine proteinase and phospholipase A(2) activities were comparable to those observed in venoms of Bothrops snakes which were used as positive controls in this study. Hence, these data offer new opportunities to explore serine proteinase and phospholipase A2 activities in the clinical sequelae following O. sambaquiensis envenomation, with future possible biopharmaceutical applications. (C) 2016 Elsevier Ltd. All rights reserved. (AU)

Processo FAPESP: 14/26058-8 - Inibição de metaloproteinases de mamíferos e de venenos de serpentes pelo pró-domínio recombinante da jararagina e seus fragmentos peptídicos
Beneficiário:Ana Maria Moura da Silva
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 13/25593-4 - Explorando o potencial enzimático e citotóxico em extratos de nematocistos de água-viva
Beneficiário:Paloma Sirigatti Knittel
Linha de fomento: Bolsas no Brasil - Mestrado
Processo FAPESP: 11/50242-5 - Dimensões da vida marinha: padrões e processos de diversificação em cnidários planctônicos e bentônicos
Beneficiário:Antonio Carlos Marques
Linha de fomento: Auxílio à Pesquisa - Programa BIOTA - Temático