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

DC Field Value Language
dc.contributor.author Choudhary, Indu -
dc.contributor.author Hwang, Du Hyeon -
dc.contributor.author Lee, Hyunkyoung -
dc.contributor.author Yoon, Won Duk -
dc.contributor.author Chae, Jinho -
dc.contributor.author Han, Chang Hoon -
dc.contributor.author Yum, Seungshic -
dc.contributor.author Kang, Changkeun -
dc.contributor.author Kim, Euikyung -
dc.date.accessioned 2020-04-16T08:15:18Z -
dc.date.available 2020-04-16T08:15:18Z -
dc.date.created 2020-02-26 -
dc.date.issued 2019-03-08 -
dc.identifier.issn 2072-6651 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/664 -
dc.description.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. -
dc.description.uri 1 -
dc.language English -
dc.publisher MDPI -
dc.subject HOUSE-DUST-MITE -
dc.subject BOX JELLYFISH -
dc.subject PARTIAL-PURIFICATION -
dc.subject SERINE-PROTEASE -
dc.subject ACTINOBACILLUS-PLEUROPNEUMONIAE -
dc.subject FUNCTIONAL-CHARACTERIZATION -
dc.subject MOLECULAR CHARACTERIZATION -
dc.subject IDENTIFICATION -
dc.subject TOXINS -
dc.subject PROTEINS -
dc.title Proteomic Analysis of Novel Components of Nemopilema nomurai Jellyfish Venom: Deciphering the Mode of Action -
dc.type Article -
dc.citation.title TOXINS -
dc.citation.volume 11 -
dc.citation.number 3 -
dc.contributor.alternativeName 염승식 -
dc.identifier.bibliographicCitation TOXINS, v.11, no.3 -
dc.identifier.doi 10.3390/toxins11030153 -
dc.identifier.scopusid 2-s2.0-85062868525 -
dc.identifier.wosid 000464474800001 -
dc.type.docType Article -
dc.description.journalClass 1 -
dc.subject.keywordPlus HOUSE-DUST-MITE -
dc.subject.keywordPlus BOX JELLYFISH -
dc.subject.keywordPlus PARTIAL-PURIFICATION -
dc.subject.keywordPlus SERINE-PROTEASE -
dc.subject.keywordPlus ACTINOBACILLUS-PLEUROPNEUMONIAE -
dc.subject.keywordPlus FUNCTIONAL-CHARACTERIZATION -
dc.subject.keywordPlus MOLECULAR CHARACTERIZATION -
dc.subject.keywordPlus IDENTIFICATION -
dc.subject.keywordPlus TOXINS -
dc.subject.keywordPlus PROTEINS -
dc.subject.keywordAuthor Jellyfish -
dc.subject.keywordAuthor Nemopilema nomurai -
dc.subject.keywordAuthor NnV -
dc.subject.keywordAuthor 2-DE -
dc.subject.keywordAuthor MALDI -
dc.subject.keywordAuthor TOF -
dc.subject.keywordAuthor MS -
dc.relation.journalWebOfScienceCategory Food Science & Technology -
dc.relation.journalWebOfScienceCategory Toxicology -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.relation.journalResearchArea Food Science & Technology -
dc.relation.journalResearchArea Toxicology -
Appears in Collections:
South Sea Research Institute > Risk Assessment Research Center > 1. Journal Articles
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