Abstract

A novel lectin was purified from the dorsal spines of the devil stinger, Inimicus japonicus using a combination of affinity chromatography techniques. A single band was detected on a native PAGE gel with a relative molecular mass of 97 kDa. The N-terminal partial amino acid of the intact 75 kDa subunit of the 97 kDa lectin was found to be DHEDS. The agglutination of rabbit erythrocytes by the 97 kDa lectin was inhibited most effectively by methyl α-D-mannoside. The 97 kDa lectin stimulated mitogenesis in murine splenocytes. This is the first study to examine the dorsal lectin of I. japonicus and one of the very few studies on venom lectins from venomous scorpaeniform fish. These results suggest that the devil stinger, I. japonicus, may be a novel resource for biologically active substances.

Highlights

  • A large number of venomous and poisonous animals exist in aquatic environments worldwide

  • We attempted to isolate a lectin from the dorsal spines of I. japonicus using a combination of affinity chromatography techniques (Fig. 2a, b)

  • A novel lectin was isolated from the dorsal spines of I. japonicus using a combination of affinity chromatography techniques

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Summary

Introduction

A large number of venomous and poisonous animals exist in aquatic environments worldwide. 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). The devil stinger Inimicus japonicus, which belongs to the family Synanceiidae, has 17 dorsal, 1 pelvic, and 2 anal spines, which contain venom glands that are covered by an integumentary sheath (Tange 1954). We examined the dorsal venom of the devil stinger, I. japonicus using column chromatography and, for the first time, separated a novel lectin that induced mitogenic activity

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