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Toxins 2019, 11(3), 153; https://doi.org/10.3390/toxins11030153

Proteomic Analysis of Novel Components of Nemopilema nomurai Jellyfish Venom: Deciphering the Mode of Action

1
College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Korea
2
Institute of Animal Medicine, Gyeongsang National University, Jinju 52828, Korea
3
Southeast Sea Fisheries Research Institute, National Institute of Fisheries Science, Tongyeong 53085, Korea
4
Marine Environmental Research and Information Laboratory, B1101, 17 Gosan-ro 148beon-gil, Gunpo-si, Gyeonggi-do 15850, Korea
5
Headquarters for Marine Environment, National Fisheries Research & Development Institute, Shiran-ri, Gijang-eup, Gijang-gun, Busan 619-705, Korea
6
Ecological Risk Research Division, Korea Institute of Ocean Science and Technology (KIOST), Geoje 53201, Korea
7
Faculty of Marine Environmental Science, University of Science and Technology (UST), Geoje 53201, Korea
*
Author to whom correspondence should be addressed.
Received: 16 January 2019 / Revised: 1 March 2019 / Accepted: 1 March 2019 / Published: 8 March 2019
(This article belongs to the Section Animal Venoms)
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Abstract

Nowadays, proliferation of jellyfish has become a severe matter in many coastal areas around the world. Jellyfish Nemopilema nomurai is one of the most perilous organisms and leads to significant deleterious outcomes such as harm to the fishery, damage the coastal equipment, and moreover, its envenomation can be hazardous to the victims. Till now, the components of Nemopilema nomurai venom (NnV) are unknown owing to scant transcriptomics and genomic data. In the current research, we have explored a proteomic approach to identify NnV components and their interrelation with pathological effects caused by the jellyfish sting. Altogether, 150 proteins were identified, comprising toxins and other distinct proteins that are substantial in nematocyst genesis and nematocyte growth by employing two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI/TOF/MS). The identified toxins are phospholipase A2, phospholipase D Li Sic Tox beta IDI, a serine protease, putative Kunitz-type serine protease inhibitor, disintegrin and metalloproteinase, hemolysin, leukotoxin, three finger toxin MALT0044C, allergens, venom prothrombin activator trocarin D, tripeptide Gsp 9.1, and along with other toxin proteins. These toxins are relatively well characterized in the venoms of other poisonous species to induce pathogenesis, hemolysis, inflammation, proteolysis, blood coagulation, cytolysis, hemorrhagic activity, and type 1 hypersensitivity, suggesting that these toxins in NnV can also cause similar deleterious consequences. Our proteomic works indicate that NnV protein profile represents valuable source which leads to better understanding the clinical features of the jellyfish stings. As one of the largest jellyfish in the world, Nemopilema nomurai sting is considered to be harmful to humans due to its potent toxicity. The identification and functional characterization of its venom components have been poorly described and are beyond our knowledge. Here is the first report demonstrating the methodical overview of NnV proteomics research, providing significant information to understand the mechanism of NnV envenomation. Our proteomics findings can provide a platform for novel protein discovery and development of practical ways to deal with jellyfish stings on human beings. View Full-Text
Keywords: Jellyfish; Nemopilema nomurai; NnV; 2-DE; MALDI/TOF/MS Jellyfish; Nemopilema nomurai; NnV; 2-DE; MALDI/TOF/MS
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Choudhary, I.; Hwang, D.H.; Lee, H.; Yoon, W.D.; Chae, J.; Han, C.H.; Yum, S.; Kang, C.; Kim, E. Proteomic Analysis of Novel Components of Nemopilema nomurai Jellyfish Venom: Deciphering the Mode of Action. Toxins 2019, 11, 153.

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