A potent vasoactive cytolysin isolated from Scorpaena plumieri scorpionfish venom

Abstract

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 (EC(50) 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 microg/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.

A review on the Scorpaena plumieri fish venom and its bioactive compounds

“…SpV was found to perform lethal, hemolytic, cardiovascular, inflammatory, integrin-binding-inhibitory and proteolytic activities [20, 22–24, 27, 29]. This spectrum of activities — observed in experimental animals — resembles those of other fish venoms previously described [1, 2].…”

“…Nevertheless, the major hindrance to elucidating the nature of the venom has been the instability of its active components, which could be partially due to the presence of endogenous proteolytic enzymes [20, 24]. …”

“…Considerable progress has been made in relation to the biochemical and pharmacological properties of the crude venom extract [20–23] and a few bioactive molecules have been isolated and analysed [20, 24–28]. In this review, we will focus on the discussion of the chemical and physio-pharmacological properties of S. plumieri venom along with those of the bioactive molecules isolated so far.…”

Isolation of a novel lectin from the dorsal spines of the devil stinger, Inimicus japonicus

“…Venomous scorpaeniform fish include the lionfish and scorpionfish from the family Scorpaenidae, devil stinger and stonefish from the family Synanceiidae, and waspfish from the family Tetrarogidae (Kiriake et al 2013). These fish possess 11-17 dorsal, 2 pelvic, and 3 anal spines, with the venom secretory complex being located within the anterolateral grooves of these spines (Russell 1965;Halstead 1988;Haddad et al 2003;Smith and Wheeler 2006;Andrich et al 2010).…”

Expressed sequence tags in venomous tissue of Scorpaena plumieri (Scorpaeniformes: Scorpaenidae)

“…Sp-CTx displays potent hemolytic activity on washed rabbit erythrocytes (EC 50 0.46 nM); its effect is antagonized by antivenom raised against stonefish venom -Synanceia trachynis (SFAV). Like S. plumieri whole venom (100 µg/mL), Sp-CTx (1-50 nM) causes a biphasic response on phenylephrine pre-contracted rat aortic rings, characterized by an endothelium-and dose-dependent relaxation phase followed by a contractile phase (Andrich et al, 2010).…”