First Report of a Peroxiredoxin Homologue in Jellyfish: Molecular Cloning, Expression and Functional Characterization of CcPrx4 from Cyanea capillata

Ruan, Zengliang; Liu, Guoyan; Wang, Beilei; Zhou, Yonghong; Lu, Jia; Wang, Qianqian; Zhao, Jie; Zhang, Liming

doi:10.3390/md12010214

Cited by 16 publications

(14 citation statements)

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“…Similarly, it has been proposed that peroxiredoxins in snake venom eliminate peroxides generated during metabolism and thus maintain redox homeostasis [ 35 ]. Therefore the two peroxiredoxins identified in C. fleckeri could play a similar role, as is the case in the scyphozoan jellyfish Cyanea capillata [ 36 ]. Conversely, proteins not designated as potential toxins at the transcript level, were identified in the proteome and could be toxins.…”

Section: Discussionmentioning

confidence: 99%

Transcriptome and venom proteome of the box jellyfish Chironex fleckeri

et al. 2015

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BackgroundThe box jellyfish, Chironex fleckeri, is the largest and most dangerous cubozoan jellyfish to humans. It produces potent and rapid-acting venom and its sting causes severe localized and systemic effects that are potentially life-threatening. In this study, a combined transcriptomic and proteomic approach was used to identify C. fleckeri proteins that elicit toxic effects in envenoming.ResultsMore than 40,000,000 Illumina reads were used to de novo assemble ∼ 34,000 contiguous cDNA sequences and ∼ 20,000 proteins were predicted based on homology searches, protein motifs, gene ontology and biological pathway mapping. More than 170 potential toxin proteins were identified from the transcriptome on the basis of homology to known toxins in publicly available sequence databases. MS/MS analysis of C. fleckeri venom identified over 250 proteins, including a subset of the toxins predicted from analysis of the transcriptome. Potential toxins identified using MS/MS included metalloproteinases, an alpha-macroglobulin domain containing protein, two CRISP proteins and a turripeptide-like protease inhibitor. Nine novel examples of a taxonomically restricted family of potent cnidarian pore-forming toxins were also identified. Members of this toxin family are potently haemolytic and cause pain, inflammation, dermonecrosis, cardiovascular collapse and death in experimental animals, suggesting that these toxins are responsible for many of the symptoms of C. fleckeri envenomation.ConclusionsThis study provides the first overview of a box jellyfish transcriptome which, coupled with venom proteomics data, enhances our current understanding of box jellyfish venom composition and the molecular structure and function of cnidarian toxins. The generated data represent a useful resource to guide future comparative studies, novel protein/peptide discovery and the development of more effective treatments for jellyfish stings in humans. (Length: 300).Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-015-1568-3) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Transcriptome and venom proteome of the box jellyfish Chironex fleckeri

et al. 2015

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“…Bioinformatics analyses were performed following methods we have described previously [ 7 ]. Briefly, the ORF Finder program ( http://www.ncbi.nlm.nih.gov/gorf/gorf.html ) and SignalP 4.1 Server ( http://www.cbs.dtu.dk/services/SignalP/ ) were used to search for the open reading frames and signal peptides, respectively, in the sequences.…”

Section: Methodsmentioning

confidence: 99%

“…Antioxidant activity of the giant jellyfish Nemopilema nomurai was observed by Kazuki [ 5 ]. We previously reported the first peroxiredoxin (Prx) and thioredoxin (Trx) genes from the jellyfish Cyanea capillata ; both of these genes exhibit general intracellular antioxidant activity [ 6 – 7 ]. The jellyfish body also contains abundant collagens, which have immunostimulatory effects without inducing allergic complications [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

Global Transcriptome Analysis of the Tentacle of the Jellyfish Cyanea capillata Using Deep Sequencing and Expressed Sequence Tags: Insight into the Toxin- and Degenerative Disease-Related Transcripts

et al. 2015

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BackgroundJellyfish contain diverse toxins and other bioactive components. However, large-scale identification of novel toxins and bioactive components from jellyfish has been hampered by the low efficiency of traditional isolation and purification methods.ResultsWe performed de novo transcriptome sequencing of the tentacle tissue of the jellyfish Cyanea capillata. A total of 51,304,108 reads were obtained and assembled into 50,536 unigenes. Of these, 21,357 unigenes had homologues in public databases, but the remaining unigenes had no significant matches due to the limited sequence information available and species-specific novel sequences. Functional annotation of the unigenes also revealed general gene expression profile characteristics in the tentacle of C. capillata. A primary goal of this study was to identify putative toxin transcripts. As expected, we screened many transcripts encoding proteins similar to several well-known toxin families including phospholipases, metalloproteases, serine proteases and serine protease inhibitors. In addition, some transcripts also resembled molecules with potential toxic activities, including cnidarian CfTX-like toxins with hemolytic activity, plancitoxin-1, venom toxin-like peptide-6, histamine-releasing factor, neprilysin, dipeptidyl peptidase 4, vascular endothelial growth factor A, angiotensin-converting enzyme-like and endothelin-converting enzyme 1-like proteins. Most of these molecules have not been previously reported in jellyfish. Interestingly, we also characterized a number of transcripts with similarities to proteins relevant to several degenerative diseases, including Huntington’s, Alzheimer’s and Parkinson’s diseases. This is the first description of degenerative disease-associated genes in jellyfish.ConclusionWe obtained a well-categorized and annotated transcriptome of C. capillata tentacle that will be an important and valuable resource for further understanding of jellyfish at the molecular level and information on the underlying molecular mechanisms of jellyfish stinging. The findings of this study may also be used in comparative studies of gene expression profiling among different jellyfish species.

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“…Peroxiredoxin, also called thioredoxin peroxidase or alkyl hydroperoxide reductase, has been proposed as antioxidant protein [ 62 , 63 , 64 ]. Both proteins, seem to play an important role by protecting the cells against reactive oxygen species [ 65 ], so they are likely to be natural anti-Ultraviolet (UV) radiation agents [ 66 ]. Similarly, superoxide dismutase is another relevant antioxidant protein [ 65 , 67 ].…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analyses of the Unexplored Sea Anemone Bunodactis verrucosa

et al. 2018

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Cnidarian toxic products, particularly peptide toxins, constitute a promising target for biomedicine research. Indeed, cnidarians are considered as the largest phylum of generally toxic animals. However, research on peptides and toxins of sea anemones is still limited. Moreover, most of the toxins from sea anemones have been discovered by classical purification approaches. Recently, high-throughput methodologies have been used for this purpose but in other Phyla. Hence, the present work was focused on the proteomic analyses of whole-body extract from the unexplored sea anemone Bunodactis verrucosa. The proteomic analyses applied were based on two methods: two-dimensional gel electrophoresis combined with MALDI-TOF/TOF and shotgun proteomic approach. In total, 413 proteins were identified, but only eight proteins were identified from gel-based analyses. Such proteins are mainly involved in basal metabolism and biosynthesis of antibiotics as the most relevant pathways. In addition, some putative toxins including metalloproteinases and neurotoxins were also identified. These findings reinforce the significance of the production of antimicrobial compounds and toxins by sea anemones, which play a significant role in defense and feeding. In general, the present study provides the first proteome map of the sea anemone B. verrucosa stablishing a reference for future studies in the discovery of new compounds.

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First Report of a Peroxiredoxin Homologue in Jellyfish: Molecular Cloning, Expression and Functional Characterization of CcPrx4 from Cyanea capillata

Cited by 16 publications

References 55 publications

Transcriptome and venom proteome of the box jellyfish Chironex fleckeri

Transcriptome and venom proteome of the box jellyfish Chironex fleckeri

Global Transcriptome Analysis of the Tentacle of the Jellyfish Cyanea capillata Using Deep Sequencing and Expressed Sequence Tags: Insight into the Toxin- and Degenerative Disease-Related Transcripts

Proteomic Analyses of the Unexplored Sea Anemone Bunodactis verrucosa

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