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The toxicity of ribbon worms: alpha-nemertides or tetrodotoxin, or both?
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. (Linnaeus University Centre for Biomaterials Chemistry)ORCID iD: 0000-0003-1241-8888
Uppsala University. (Department of Pharmacognosy)
Uppsala University. (Department of Pharmacognosy)
Lund University. (Department of Biotechnology)
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2016 (English)Conference paper, Poster (with or without abstract) (Other academic)
Abstract [en]

The marine ribbon worms (nemerteans) are predators which capture their prey by everting a proboscis carrying a mixture of toxins which brings on rapid paralysis [1]. Moreover, ribbon worms have a thick layer of epidermal mucus of similar constitution. Tetrodotoxin (TTX) has been identified as one of these toxins [2]. The extreme toxicity of TTX (lethal by ingestion of 0.5-2 mg) is due to its ability to block voltage-gated sodium channels. Although several bacterial species (among these Vibrio sp.) have been linked to its synthesis, the biogenic origin and biosynthesis is unclear. One hypothesis is that TTX production occurs in a symbiotic relationship with its host, in this case the ribbon worm [3]. We have made significant effort to identify TTX in a setup for production through the cultivation of Vibrio alginolyticus in nutrient broth infused with mucus from the ribbon worm Lineus longissimus. Toxicity was demonstrated by fraction injections into shore crabs, but no TTX was found, and it could be shown conclusively that toxicity was unrelated to TTX and the Vibrio culture itself, and rather a constituent of the ribbon worm mucus [4]. The following studies led us to the discovery of a new class of peptides, the alpha-nemertides, in the mucus of the ribbon worms, which could be directly linked to the toxic effects. A literature review of the available evidence for TTX in ribbon worms show that the evidence in most cases are indirect, although notable exceptions exist. This points to the necessity to further investigate the presence and roles of TTX and alpha-nemertides in ribbon worms.

Place, publisher, year, edition, pages
2016. P549
National Category
Biochemistry and Molecular Biology
Research subject
Chemistry, Medical Chemistry
Identifiers
URN: urn:nbn:se:lnu:diva-56306OAI: oai:DiVA.org:lnu-56306DiVA: diva2:957618
Conference
Joint Natural Products Conference, July 25-27, Copenhagen, Denmark
Funder
Swedish Research CouncilThe Crafoord Foundation
Available from: 2016-09-02 Created: 2016-09-02 Last updated: 2017-04-18Bibliographically approved

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Andersson, Håkan S.Strand, MalinGöransson, Ulf
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CiteExportLink to record
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Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
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More styles
Language
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