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

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.

Automated summary

Proteomic techniques were used to identify the most abundant proteins in the venom of Chrysaora chesapeakei from the Gulf of Mexico estuaries, revealing main toxins including metalloproteinase-zinc disintegrin and astacin-type metalloprotease. These components could be responsible for the main effects of this jellyfish venom. Additionally, nonpoisonous metalloproteinases were found in the connective tissue of the tentacles.