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Abstract
Background: Medusozoans utilize explosively discharging penetrant nematocysts to inject venom into prey. These venoms are composed of highly complex proteins and peptides with extensive bioactivities, as observed in vitro. Diverse enzymatic toxins have been putatively identified in the venom of jellyfish, Nemopilema nomurai and Cyanea nozakii, through examination of their proteomes and transcriptomes. However, functional examination of putative enzymatic components identified in proteomic approaches to elucidate potential bioactivities is critically needed. Methods: In this study, enzymatic toxins were functionally identified using a combined approach consisting of in gel zymography and liquid chromatography tandem mass spectrometry (LC-MS/MS). The potential roles of metalloproteinases and lipases in hemolytic activity were explored using specific inhibitors. Results: Zymography indicated that nematocyst venom possessed protease-, lipase- and hyaluronidase-class activities. Further, proteomic approaches using LC-MS/MS indicated sequence homology of proteolytic bands observed in zymography to extant zinc metalloproteinase-disintegrins and astacin metalloproteinases. Moreover, pre-incubation of the metalloproteinase inhibitor batimastat with N. nomurai nematocyst venom resulted in an approximate 62% reduction of hemolysis compared to venom exposed sheep erythrocytes, suggesting that metalloproteinases contribute to hemolytic activity. Additionally, species within the molecular mass range of 14–18 kDa exhibited both egg yolk and erythrocyte lytic activities in gel overlay assays. Conclusion: For the first time, our findings demonstrate the contribution of jellyfish venom metalloproteinase and suggest the involvement of lipase species to hemolytic activity. Investigations of this relationship will facilitate a better understanding of the constituents and toxicity of jellyfish venom.
Highlights
Jellyfish belong to the phylum Cnidaria, and comprise hydrozoans, scyphozoans and cubozoans [1,2]
Specific inhibitors, batimastat and varespladib, were found to inhibit metalloproteinases and lipolytic enzymes in jellyfish venom, which strongly suggest the provisional identities assigned by LC‐MS/MS data. These identity assignments are still tentative because we found the concentration range of varespladib required for phospholipase A2 (PLA2) inhibition was far higher than that required for snake secretory PLA2
LC-MS/MS identification data further elucidate the functional basis of jellyfish venom on various substrates in zymography assays and an emerging picture suggests that metalloproteinases, lipases and hyaluronidases are key components
Summary
Jellyfish belong to the phylum Cnidaria, and comprise hydrozoans, scyphozoans and cubozoans [1,2]. Jellyfish nematocyst venom, composed of highly complex and toxic mixtures of proteins and peptides, is the underlying basis of severe envenomations. Medusozoans utilize explosively discharging penetrant nematocysts to inject venom into prey. These venoms are composed of highly complex proteins and peptides with extensive bioactivities, as observed in vitro. Diverse enzymatic toxins have been putatively identified in the venom of jellyfish, Nemopilema nomurai and Cyanea nozakii, through examination of their proteomes and transcriptomes. Functional examination of putative enzymatic components identified in proteomic approaches to elucidate potential bioactivities is critically needed. Methods: In this study, enzymatic toxins were functionally identified using a combined approach consisting of in gel zymography and liquid chromatography tandem mass spectrometry (LC-MS/MS). Results: Zymography indicated that nematocyst venom possessed protease-, lipase- and hyaluronidase-class activities.
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