Application of nanoLC–MS/MS to the shotgun proteomic analysis of the nematocyst proteins from jellyfish Stomolophus meleagris

Li, Rongfeng; Yu, Huan; Xing, Ronge; Liu, Song; Qing, Yukun; Li, Kecheng; Li, Bing; Meng, Xiangtao; Cui, Jinhui; Li, Pengcheng

doi:10.1016/j.jchromb.2012.05.006

Cited by 30 publications

(17 citation statements)

References 18 publications

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“…Jellyfish venom is mainly composed of proteins [ 18 ] and may provide B. mori with nutrition for growth. In addition, according to our previous studies [ 19 , 20 ], the protein molecular weights of Fr-1 and SFV ranged from 90 kDa to 300 kDa and from 10 kDa to 300 kDa, respectively. The protein molecular weight of Fr-2 was similar to the protein molecular weight of SFV, but the color of the bands from 10 kDa to 90 kDa was lighter than the color bands of SFV.…”

Section: Resultsmentioning

confidence: 69%

Effect of Venom from the Jellyfish Nemopilema nomurai on the Silkworm Bombyx mori L.

Chen

et al. 2015

Toxins

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The silkworm Bombyx mori L. (B. mori) has a significant impact on the economy by producing more than 80% of the globally produced raw silk. The exposure of silkworm to pesticides may cause adverse effects on B. mori, such as a reduction in the production and quality of silk. This study aims to assay the effect of venom from the jellyfish Nemopilema nomurai on growth, cuticle and acetylcholinesterase (AChE) activity of the silkworm B. mori by the leaf dipping method. The experimental results revealed that the four samples caused neither antifeeding nor a lethal effect on B. mori. The sample SFV inhibited B. mori growth after 6 days of treatment in a dose-dependent manner. The samples SFV, DSFV and Fr-1 inhibited the precipitation and synthesis of chitin in the cuticle after 12 and 14 days of treatment. In the case of the four samples, the AChE was significantly improved after 14 days of treatment.

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Section: Resultsmentioning

confidence: 69%

Effect of Venom from the Jellyfish Nemopilema nomurai on the Silkworm Bombyx mori L.

Chen

et al. 2015

Toxins

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“…Potential metalloproteinases identified in C. fuscescens were mainly disintegrin-like and astacin-like metalloproteinases. Disintegrin-like proteins have been identified in the venoms of S. meleagris and O. sambaquiensis [ 20 , 78 ] where they could cause severe inflammation by disrupting capillary vessels and tissue [ 20 ]. Astacin-like metalloproteinases have been identified in the cnidarian venom proteomes of N. vectensis [ 25 ], H. vulgaris [ 79 ], A. digitifera [ 54 ], S. meleagris [ 23 ] and C. fleckeri [ 26 ], where they may act as spreading agents or be involved in the proteolytic processing of other venom proteins [ 80 ].…”

Section: Resultsmentioning

confidence: 99%

Tentacle Transcriptome and Venom Proteome of the Pacific Sea Nettle, Chrysaora fuscescens (Cnidaria: Scyphozoa)

Ponce

Brinkman

Potriquet

et al. 2016

Toxins

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Jellyfish venoms are rich sources of toxins designed to capture prey or deter predators, but they can also elicit harmful effects in humans. In this study, an integrated transcriptomic and proteomic approach was used to identify putative toxins and their potential role in the venom of the scyphozoan jellyfish Chrysaora fuscescens. A de novo tentacle transcriptome, containing more than 23,000 contigs, was constructed and used in proteomic analysis of C. fuscescens venom to identify potential toxins. From a total of 163 proteins identified in the venom proteome, 27 were classified as putative toxins and grouped into six protein families: proteinases, venom allergens, C-type lectins, pore-forming toxins, glycoside hydrolases and enzyme inhibitors. Other putative toxins identified in the transcriptome, but not the proteome, included additional proteinases as well as lipases and deoxyribonucleases. Sequence analysis also revealed the presence of ShKT domains in two putative venom proteins from the proteome and an additional 15 from the transcriptome, suggesting potential ion channel blockade or modulatory activities. Comparison of these potential toxins to those from other cnidarians provided insight into their possible roles in C. fuscescens venom and an overview of the diversity of potential toxin families in cnidarian venoms.

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“…Here we reviewed relevant information on several jellyfish species including Aurelia aurita [ 8 , 9 , 10 , 11 ], Carybdea alata [ 12 ], Carybdea rastoni [ 13 ], Chironex fleckeri [ 14 , 15 , 16 , 17 , 18 , 19 ], Chiropsalmus quadrigatus [ 20 ], Chiropsalmus sp. [ 14 ], Chiropsella bronzie [ 17 ], Cyanea capillata [ 21 , 22 ], Cyanea nozakii [ 11 , 23 , 24 ], Nemopilema nomurai [ 11 , 25 , 26 ], Pelagia noctiluca [ 27 , 28 , 29 , 30 , 31 , 32 , 33 ], Rhopilema esculentum [ 11 , 34 , 35 ], Rhopilema nomadica [ 36 ], Stomolophus meleagris [ 37 , 38 , 39 , 40 , 41 ] and deep-sea jellyfish [ 42 ]. Apart from the true jellyfish, there are also Hydrozoa members that have different evolutionary histories [ 43 ] and are colonial free-swimming organisms resembling jellyfish.…”

Section: Proteomics In Jellyfishmentioning

confidence: 99%

Jellyfish Bioactive Compounds: Methods for Wet-Lab Work

Frazão

Antunes

2016

Marine Drugs

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The study of bioactive compounds from marine animals has provided, over time, an endless source of interesting molecules. Jellyfish are commonly targets of study due to their toxic proteins. However, there is a gap in reviewing successful wet-lab methods employed in these animals, which compromises the fast progress in the detection of related biomolecules. Here, we provide a compilation of the most effective wet-lab methodologies for jellyfish venom extraction prior to proteomic analysis—separation, identification and toxicity assays. This includes SDS-PAGE, 2DE, gel chromatography, HPLC, DEAE, LC-MS, MALDI, Western blot, hemolytic assay, antimicrobial assay and protease activity assay. For a more comprehensive approach, jellyfish toxicity studies should further consider transcriptome sequencing. We reviewed such methodologies and other genomic techniques used prior to the deep sequencing of transcripts, including RNA extraction, construction of cDNA libraries and RACE. Overall, we provide an overview of the most promising methods and their successful implementation for optimizing time and effort when studying jellyfish.

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Application of nanoLC–MS/MS to the shotgun proteomic analysis of the nematocyst proteins from jellyfish Stomolophus meleagris

Cited by 30 publications

References 18 publications

Effect of Venom from the Jellyfish Nemopilema nomurai on the Silkworm Bombyx mori L.

Effect of Venom from the Jellyfish Nemopilema nomurai on the Silkworm Bombyx mori L.

Tentacle Transcriptome and Venom Proteome of the Pacific Sea Nettle, Chrysaora fuscescens (Cnidaria: Scyphozoa)

Jellyfish Bioactive Compounds: Methods for Wet-Lab Work

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