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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.)

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

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Author(s):
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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]
Total Authors: 11
Affiliation:
[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
Total Affiliations: 7
Document type: Journal article
Source: Toxicon; v. 71, p. 11-17, SEP 1 2013.
Web of Science Citations: 37
Abstract

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)

FAPESP's process: 10/50174-7 - Systematics, life cycle and reproductive patterns of jellyfishes (Cnidaria: Medusozoa: Cubozoa and Scyphozoa) in the Baixada Santista (São Paulo, Brazil)
Grantee:André Carrara Morandini
Support Opportunities: BIOTA-FAPESP Program - Regular Research Grants