ArticleThe journal of venomous animals and toxins including tropical diseases2024
Isolation and cDNA cloning of four peptide toxins from the sea anemone
Article in The journal of venomous animals and toxins including tropical diseases, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Stable yet shifting: Early toxin dynamics in typical and atypical clownfish-anemone symbioses.Toxicon: X · 2026Article
- Cnidarian Venoms in the Omics Era: Toxin Discovery and Bioactive Potential.Marine drugs · 2026Review
- Marine natural products.Natural product reports · 2026Review
- Transcriptomics-driven exploration of genetic variation and peptide discovery in the sea anemones Anthopleura midori and Actinia equina.Scientific reports · 2025Article
- Cnidarian toxins: omics approaches and recombinant proteins.The journal of venomous animals and toxins including tropical diseases · 2025Article
- First Anti-Inflammatory Peptide AnmTX Sco 9a-1 from the Swimming Sea AnemoneBiomolecules · 2022Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Sea anemones are well known to contain multiple peptide toxins. However, of more than 1100 species of sea anemones distributed worldwide, only a little over 50 have been studied for peptide toxins. Therefore, innumerable unique and novel peptide toxins remain to be discovered in unstudied sea anemones. Methods: Isolation of peptide toxins in the sea anemone Results: Hau I and IV were potently lethal to crabs, whereas Hau II and III were only paralytic. The precursor proteins of the four toxins were commonly composed of a signal peptide, a propart, and the remaining region including a mature peptide. Interestingly, four and two copies of the mature peptide were present in the precursor proteins of Hau II and III, respectively. Homology searches revealed that Hau I (30 amino acid residues) is a novel peptide toxin, although it has the same cysteine pattern CXXC-C-C as the boundless β-hairpin (BBH) family. Hau II (27 amino acid residues) and III (28 amino acid residues) were homologous with the BBH family, whereas Hau IV (49 amino acid residues) was a new member of the well-known type 1 sodium channel toxin family. Conclusion: This study showed that a novel class of toxin (Hau I), two BBH family toxins (Hau II and III), and a type 1 sodium channel toxin (Hau IV) are present in the toxin of the sea anemone
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