Metalloproteinases and NAD(P)H-dependent oxidoreductase within of Bay nettle (Chrysaora chesapeakei) venom

Abstract

The venom of jellyfish has been a source of biologically active substances, so it is interesting to study the components of the venom of Chrysaora chesapeakei from the estuaries of the Gulf of Mexico. Proteomic techniques in this study identified the most abundant venom proteins (100, 50, and 37 kDa). Homology searches suggest that the main toxins in this venom correspond to metalloproteinase-zinc disintegrin, astacin-type metalloprotease, and NAD (P) H-dependent oxidoreductases, which could be responsible for the main effects of this jellyfish venom; The tentacles were also identified as containing nonpoisonous metalloproteinases in connective tissue.

Keywords:

• Astacin-like metalloprotease
• Chrysaora
• metalloproteinase-disintegrin
• NAD(P)H-dependent oxidoreductases
• venom

Acknowledgments

The authors of this work thank Tania Gazca Vázquez for technical assistance and Saúl López Vite for taking pictures of the jellyfish.

Disclosure statement

No potential conflict of interest was reported by the author(s).