Nemopilema nomurai
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA486695 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR7754710_1.fastq.gz | Fastqsanger.gz | |||
| SRR7754710_2.fastq.gz | Fastqsanger.gz | |||
| SRR7754711_1.fastq.gz | Fastqsanger.gz | |||
| SRR7754711_2.fastq.gz | Fastqsanger.gz | |||
| SRR7754712_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 6 |
Similar Datasets
Project description:The scyphozoan jellyfish Nemopilema nomurai are common blooming species in China.The venomous characteristics of jellyfish Nemopilema nomurai is largely attributed to their complex and elaborate venom delivery system: the stinging cells, or nematocytes. These specialized cells synthesize and secrete unique intracellular organelles called nematocysts. Nematocysts with heterogeneous sizes and morphologies may contain different toxic components that exert diverse pharmacological and physiological activities such as hemolysis, cytolysis and proteolysis for defense and prey capture. We modified the previous method of nematocyst preparation using density centrifugation to purify undischarged nematocysts from jellyfish Nemopilema nomurai tentacles. Ultimately, isorhiza-type were successfully purified.Then we used purified nematocysts for proteomic study to identify sting-related toxins in Nemopilema nomurai nematocysts.
2018-11-30 | PXD011684 | Pride
Project description:Transcriptome of Nemopilema nomurai
| PRJNA498198 | ENA
Project description:Nemopilema nomurai isolate:NNO-Tongyong01 Genome sequencing and assembly
| PRJNA415234 | ENA
Project description:Proteome Analysis of the antivenom for Jellyfish Nemopilema nomurai
2019-06-19 | PXD014306 | iProX
Project description:Proteome data of lethal fraction from the venom of jellyfish Nemopilema nomurai
2020-02-21 | PXD017680 | iProX
Project description:This data article restrains data associated to the Choudhary et al. [1]. Nemopilema nomurai Jellyfish venom (NnV) can lead to cardiac toxicity. Here we analyzed the effect of NnV on rat cardiomyocytes cell line H9c2 at the proteome level using two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS). This analysis resulted in 34 proteins with differential expression. Here we provide the dataset for the proteins with amplified or reduced level as compare to control.
| S-EPMC4669470 | biostudies-literature
Project description:An enzyme in a nematocyst extract of the Nemopilema nomurai jellyfish, caught off the coast of the Republic of Korea, catalyzed the cleavage of chymotrypsin substrate in an amidolytic kinetic assay, and this activity was inhibited by the serine protease inhibitor, phenylmethanesulfonyl fluoride. We isolated the full-length cDNA sequence of this enzyme, which contains 850 nucleotides, with an open reading frame of 801 encoding 266 amino acids. A blast analysis of the deduced amino acid sequence showed 41% identity with human chymotrypsin-like (CTRL) and the CTRL-1 precursor. Therefore, we designated this enzyme N. nomurai CTRL-1. The primary structure of N. nomurai CTRL-1 includes a leader peptide and a highly conserved catalytic triad of His(69), Asp(117), and Ser(216). The disulfide bonds of chymotrypsin and the substrate-binding sites are highly conserved compared with the CTRLs of other species, including mammalian species. Nemopilema nomurai CTRL-1 is evolutionarily more closely related to Actinopterygii than to Scyphozoan (Aurelia aurita) or Hydrozoan (Hydra vulgaris). The N. nomurai CTRL1 was amplified from the genomic DNA with PCR using specific primers designed based on the full-length cDNA, and then sequenced. The N. nomurai CTRL1 gene contains 2434 nucleotides and four distinct exons. The 5' donor splice (GT) and 3' acceptor splice sequences (AG) are wholly conserved. This is the first report of the CTRL1 gene and cDNA structures in the jellyfish N. nomurai.
| S-EPMC4963838 | biostudies-literature
Project description: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.
| S-EPMC6468547 | biostudies-literature