Journal
TOXICON
Volume 56, Issue 4, Pages 487-496Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.toxicon.2010.05.003
Keywords
Scorpionfish venom; Scorpaena plumieri; Cytolysin; Vasoactive protein
Categories
Funding
- CNPq [477514/06-5]
- FAPEMIG, CAPES [250/06]
- FINEP (Rede Proteoma Nacional)
- INCTTOX (Instituto Nacional de Ciencia e Tecnologia em Toxinas)
- FACITEC (Fundo de Apoio a Ciencia e Tecnologia do Municipio de Vitoria)
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A new vasoactive cytolytic toxin, referred to as Sp-CTx, has been purified from the venom of the scorpionfish Scorpaena plumieri by a combination of gel filtration and anion exchange chromatographies. An estimation of Sp-CTx native molecular mass, performed by size exclusion chromatography, demonstrated that it is a 121 kDa protein Further physicochemical studies revealed its glycoproteic nature and dimeric constitution, comprising subunits of approximately 65 kDa (MALDI-TOF-MS). Such protein has proved to possess a potent hemolytic activity on washed rabbit erythrocytes (EC50 0.46 nM), whose effect was strongly reduced after treatment with antivenom raised against stonefish venom - Synanceja trachynis (SFAV). This cross-reactivity has been confirmed by western blotting. Like S plumieri whole venom (100 mu g/mL), Sp-CTx (1-50 nM) caused a biphasic response on phenylephrine pre-contracted rat aortic rings, characterized by an endothelium- and dose-dependent relaxation phase followed by a contractile phase. The vasorelaxant activity has been abolished by L-NAME, demonstrating the involvement of nitric oxide on the response We report here the first isolation of a cytolytic/vasoactive protein from scorpionfish venom and the data provided suggest structural and functional similarities between Sp-CTx and previously published stonefish hemolytic toxins (C) 2010 Elsevier Ltd. All rights reserved
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