Abstract:Many polypeptides isolated from shallow water cnidarian species have been utilized as valuable biochemical tools in both basic and applied biological sciences. Deepwater cnidarian species might be another potential resource for novel biochemical tools. However, because of limited access to cnidarian samples from deep-sea environments, bioactive polypeptides have never before been reported from this group. In this study, we collected twelve deep-sea jellyfish species (nine hydrozoans and three scyphozoans) usin… Show more
“…A hemolytic activity test was conducted as described previously [20]. Sample solutions (50 μl) were incubated in microtubes with a 400-μl suspension of 0.8% sheep red blood cells (Nippon Biotest Lab., Tokyo, Japan) in 10 m M PBS at 37°C for 2 h. Cell suspensions were centrifuged at 2,000 g for 10 min.…”
Background: Jellyfish stings cause painful, papular-urticarial eruptions due to the immediate allergic, acute toxic and persistent inflammatory responses. In spite of many marine accidents and their economic impact, modes of first-aid treatment remain conventional and specific allergen and medical treatment are not yet available. The purpose of this study was to define the specific allergen of the box jellyfish Chironex yamaguchii and to study the precise mechanism of the resulting dermatitis. Methods: We comprehensively studied the immunoglobulin-binding molecules from the box jellyfish C. yamaguchii with a purification procedure and Western blotting, using sera from 1 patient and from several controls. Results: From the nematocyst wall and spine, we detected IgG-binding acidic glycoprotein (of 66 and 30 kDa) as determined by Western blot and ion-exchange chromatography. In addition, the 66-kDa protein was found to be an asparagine residue-coupled N-linked glycoprotein and the epitope resided in the protein fraction. We found that CqTX-A, the major toxic protein of the nematocyst, is also a heat-stable IgE-binding allergen. This was confirmed as a 45-kDa protein by Western blot from both nematocyst extracts and purified CqTX-A. Conclusions: The detection of these proteins may, in part, explain the combined immediate allergic-toxic and persistent allergic responses. Hopefully, our findings will lead to the development of specific venom immunotherapy for marine professional workers and tourists for jellyfish-sting dermatitis and anaphylaxis.
“…A hemolytic activity test was conducted as described previously [20]. Sample solutions (50 μl) were incubated in microtubes with a 400-μl suspension of 0.8% sheep red blood cells (Nippon Biotest Lab., Tokyo, Japan) in 10 m M PBS at 37°C for 2 h. Cell suspensions were centrifuged at 2,000 g for 10 min.…”
Background: Jellyfish stings cause painful, papular-urticarial eruptions due to the immediate allergic, acute toxic and persistent inflammatory responses. In spite of many marine accidents and their economic impact, modes of first-aid treatment remain conventional and specific allergen and medical treatment are not yet available. The purpose of this study was to define the specific allergen of the box jellyfish Chironex yamaguchii and to study the precise mechanism of the resulting dermatitis. Methods: We comprehensively studied the immunoglobulin-binding molecules from the box jellyfish C. yamaguchii with a purification procedure and Western blotting, using sera from 1 patient and from several controls. Results: From the nematocyst wall and spine, we detected IgG-binding acidic glycoprotein (of 66 and 30 kDa) as determined by Western blot and ion-exchange chromatography. In addition, the 66-kDa protein was found to be an asparagine residue-coupled N-linked glycoprotein and the epitope resided in the protein fraction. We found that CqTX-A, the major toxic protein of the nematocyst, is also a heat-stable IgE-binding allergen. This was confirmed as a 45-kDa protein by Western blot from both nematocyst extracts and purified CqTX-A. Conclusions: The detection of these proteins may, in part, explain the combined immediate allergic-toxic and persistent allergic responses. Hopefully, our findings will lead to the development of specific venom immunotherapy for marine professional workers and tourists for jellyfish-sting dermatitis and anaphylaxis.
“…L1210 mouse leukemia cells were used for the cytotoxicity assay of 1 and 2 , as previously described [ 35 ]. Five microliters of each sample or methanol alone were placed into individual wells of a 96-well microtiter plate.…”
The toxin-producing cyanobacterium, Moorea producens, is a known causative organism of food poisoning and seaweed dermatitis (also known as “swimmer’s itch”). Two new toxic compounds were isolated and structurally elucidated from an ethyl acetate extract of M. producens collected from Hawaii. Analyses of HR-ESI-MS and NMR spectroscopies, as well as optical rotations and CD spectra indicated two new lyngbyatoxin derivatives, 2-oxo-3(R)-hydroxy-lyngbyatoxin A (1) and 2-oxo-3(R)-hydroxy-13-N-desmethyl-lyngbyatoxin A (2). The cytotoxicity and lethal activities of 1 and 2 were approximately 10- to 150-times less potent than lyngbyatoxin A. Additionally, the binding activities of 1 and 2 possessed 10,000-times lower affinity for the protein kinase Cδ (PKCδ)-C1B peptide when compared to lyngbyatoxin A. These findings suggest that these new lyngbyatoxin derivatives may mediate their acute toxicities through a non-PKC activation pathway.
“…These have included several investigations of jellyfish constituents and toxins, some of which have important biomedical and pharmacological properties (e.g., Ovchinnikova et al 2006;Yu et al 2006;Masuda et al 2007;Ohta et al 2009;Balamurugan et al 2010;Mariottini and Pane 2010;Zhuang et al 2010;Morishige et al 2011;Zhuang et al 2012a, b;Kawabata et al 2013;Leone et al 2015). Research on some groups of jellyfish has led to a better understanding of ocular evolution (Nilsson et al 2005), as well as two Nobel Prizes: one in 1913 for the discovery of anaphylaxis, and another in 2008 for the discovery and development of green fluorescent protein (GFP).…”
Jellyfish (primarily scyphomedusae) fisheries have a long history in Asia, where jellyfish have been caught and processed as food for centuries. More recently, jellyfish fisheries have expanded to the Western Hemisphere, often driven by demand from Asian buyers and collapses of more traditional local fish stocks. Jellyfish fisheries have been attempted in numerous countries in North, Central, and South America, with varying degrees of success. Here, we chronicle the arrival of jellyfish fisheries in the Americas and summarize relevant information on jellyfish fishing, processing, and management. Processing technology for edible jellyfish has not advanced, and presents major concerns for environmental and human health. The development of alternative processing technologies would help to eliminate these concerns and may open up new opportunities for markets and species. We also examine the biodiversity of jellyfish species that are targeted for fisheries in the Americas. Establishment of new jellyfish fisheries appears possible, but requires a specific combination of factors including high
123Rev Fish Biol Fisheries DOI 10.1007/s11160-016-9445-y abundances of particular species, processing knowledge dictated by the target market, and either inexpensive labor or industrialized processing facilities. More often than not, these factors are not altogether evaluated prior to attempting a new jellyfish fishery. As such, jellyfish fisheries are currently expanding much more rapidly than research on the subject, thereby putting ecosystems and stakeholders' livelihoods at risk.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.