Proteomic characterisation of toxins isolated from nematocysts of the South Atlantic jellyfish Olindias sambaquiensis

Autor(es):Mostrar menos -

Weston, Andrew J. ^[1] ; Chung, Ray ^[1] ; Dunlap, Walter C. ^[2] ; Morandini, Andre C. ^[3] ; Marques, Antonio C. ^[3] ; Moura-da-Silva, Ana M. ^[4] ; Ward, Malcolm ^[1] ; Padilla, Gabriel ^[5] ; da Silva, Luiziana Ferreira ^[5] ; Andreakis, Nikos ^[6] ; Long, Paul F. ^{[2, 7]}

Afiliação do(s) autor(es)

^[1] Kings Coll London, Prote Facil, Inst Psychiat, London SE5 8AF - England

^[2] Kings Coll London, Inst Pharmaceut Sci, London SE1 9NH - England

^[3] Univ Sao Paulo, Inst Biociencias, Dept Zool, BR-05508090 Sao Paulo - Brazil

^[4] Inst Butantan, Lab Imunopatol, BR-05503900 Sao Paulo - Brazil

^[5] Univ Sao Paulo, Inst Ciencias Biomed, Dept Microbiol, BR-05508090 Sao Paulo - Brazil

^[6] Australian Inst Marine Sci, Ctr Marine Microbiol & Genet, Townsville, Qld 4810 - Australia

^[7] Kings Coll London, Dept Chem, London SE1 9NH - England

• Tipo de documento: Artigo Científico
• Fonte: Toxicon; v. 71, p. 11-17, SEP 1 2013.
• Citações Web of Science: 37

Resumo

Surprisingly little is known of the toxic arsenal of cnidarian nematocysts compared to other venomous animals. Here we investigate the toxins of nematocysts isolated from the jellyfish Olindias sambaquiensis. A total of 29 unique ms/ms events were annotated as potential toxins homologous to the toxic proteins from diverse animal phyla, including cone-snails, snakes, spiders, scorpions, wasp, bee, parasitic worm and other Cnidaria. Biological activities of these potential toxins include cytolysins, neurotoxins, phospholipases and toxic peptidases. The presence of several toxic enzymes is intriguing, such as sphingomyelin phosphodiesterase B (SMase B) that has only been described in certain spider venoms, and a prepro-haystatin P-IlId snake venom metalloproteinase (SVMP) that activates coagulation factor X, which is very rare even in snake venoms. Our annotation reveals sequence orthologs to many representatives of the most important superfamilies of peptide venoms suggesting that their origins in higher organisms arise from deep eumetazoan innovations. Accordingly, cnidarian venoms may possess unique biological properties that might generate new leads in the discovery of novel pharmacologically active drugs. Crown Copyright (C) 2013 Published by Elsevier Ltd. All rights reserved. (AU)

• Processo FAPESP: 10/50174-7 - Sistemática, ciclo de vida e padrões reprodutivos de medusas (Cnidaria: Medusozoa: Cubozoa e Scyphozoa) na Baixada Santista (São Paulo, Brasil): biodiversidade marinha
• Beneficiário: André Carrara Morandini
• Modalidade de apoio: Auxílio à Pesquisa - Programa BIOTA - Regular