Sea nettle (Chrysaora quinquecirrha) nematocyst venom: Mechanism of action on muscle

Shryock, John C.; Bianchi, C. Paul

doi:10.1016/0041-0101(83)90052-1

Cited by 13 publications

(1 citation statement)

References 41 publications

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“…Chrysaora fuscescens ( Figure 1 ) is common on the western seaboard of Canada, United States of America and Mexico and despite possessing a painful sting [ 9 ], no study has been devoted to characterization of its venom. Early studies have examined some other Chrysaora venoms [ 10 , 11 ], particularly from Chrysaora quinquecirrha , which can cause cardiotoxicity, dermonecrosis, myotoxicity, haemolysis, neurotoxicity, hepatotoxicity and lethality in experimental animals [ 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 ]. Although these reports describe the clinical and experimental effects of some Chrysaora venoms, the molecular mechanisms underlying these toxic effects are poorly understood, partly because the composition of sea nettle venoms has not been fully elucidated and individual toxin components have not been characterized.…”

Section: Introductionmentioning

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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