Conus magus vs. Irukandji syndrome: A computational approach of a possible new therapy

Pelagia noctiluca is the most venomous jellyfish in the Mediterranean Sea where it forms dense blooms. Although there is several published research on this species, until now none of the works has been focused on a complete protein profile of the all body constituents of this organism. Here, we have performed a detailed proteomics characterization of the major protein components expressed by P. noctiluca. With that aim, we have considered the study of jellyfish proteins involved in defense, body constituents and metabolism, and furthered explore the significance and potential application of such bioactive molecules. P. noctiluca body proteins were separated by1D SDS-PAGE and 2DE followed by characterization by nanoLC-MS/MS and MALDI-TOF/TOF techniques. Altogether, both methods revealed 68 different proteins, including a Zinc Metalloproteinase, a Red Fluorescent Protein (RFP) and a Peroxiredoxin. These three proteins were identified for the first time in P. noctiluca. Zinc Metalloproteinase was previously reported in the venom of other jellyfish species. Besides the proteins described above, the other 65 proteins found in P. noctiluca body content were identified and associated with its clinical significance. Among all the proteins identified in this work we highlight: Zinc metalloproteinase, which has a ShK toxin domain and therefore should be implicated in the sting toxicity of P. noctiluca.; the RFP which are a very important family of proteins due to its possible application as molecular markers; and last but not least the discovery of a Peroxiredoxin in this organism makes it a new natural resource of antioxidant and anti-UV radiation agents.

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Analysis of Pelagia noctiluca proteome Reveals a Red Fluorescent Protein, a Zinc Metalloproteinase and a Peroxiredoxin

Frazão

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Osório

et al. 2017

Protein J

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Intracellular Ca2+ Overload Induced by Extracellular Ca2+ Entry Plays an Important Role in Acute Heart Dysfunction by Tentacle Extract from the Jellyfish Cyanea capillata

et al. 2014

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The exact mechanism of acute heart dysfunction caused by jellyfish venom remains unclear for the moment. In the present study, we examined the problem caused by the tentacle extract (TE) from the jellyfish Cyanea capillata at the levels of whole animal, isolated heart, primarily cultured cardiomyocytes, and intracellular Ca(2+). The heart indexes, including HR, APs, LVPs, and MMLs, were all decreased significantly by TE in both whole animal and Langendorff-perfused isolated heart model. Imbalance of cardiac oxygen supply and demand also took place. In both Ca(2+)-containing and Ca(2+)-free bathing solutions, TE could cause obvious cytoplasmic Ca(2+) overload in NRVMs, but the cytoplasmic Ca(2+) increased faster, Ca(2+) overload peaks arrived earlier, and the morphological changes were more severe under the extracellular Ca(2+)-containing condition. L-type Ca(2+) channel blockers, as well as the inhibitor of ryanodine receptor (ryanodine), could improve the viability of NRVMs. Moreover, diltiazem significantly inhibited the acute heart dysfunction caused by TE in both Langendorff isolated heart model and whole animal. These results suggested that intracellular Ca(2+) overload induced by extracellular Ca(2+) entry plays an important role in acute heart failure by TE from the jellyfish C. capillata. Inhibition of extracellular Ca(2+) influx is a promising antagonistic alternative for heart damage by jellyfish venom.

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Conus magus vs. Irukandji syndrome: A computational approach of a possible new therapy

Cited by 2 publications

References 115 publications

Analysis of Pelagia noctiluca proteome Reveals a Red Fluorescent Protein, a Zinc Metalloproteinase and a Peroxiredoxin

Analysis of Pelagia noctiluca proteome Reveals a Red Fluorescent Protein, a Zinc Metalloproteinase and a Peroxiredoxin

Intracellular Ca2+ Overload Induced by Extracellular Ca2+ Entry Plays an Important Role in Acute Heart Dysfunction by Tentacle Extract from the Jellyfish Cyanea capillata

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