ArticleToxins2015
Mutagenesis and functional analysis of the pore-forming toxin HALT-1 from Hydra magnipapillata.
Article in Toxins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Recombinant HALT-1 induces mitochondrial-associated apoptotic mechanism in HeLa cells.Scientific reports · 2025Article
- The Biological Role of Conoporins, Actinoporin-like Pore-Forming Toxins from Cone Snails.Toxins · 2025Review
- Cnidarian toxins: omics approaches and recombinant proteins.The journal of venomous animals and toxins including tropical diseases · 2025Article
- Enhanced production of recombinant HALT-1 pore-forming toxin using two-step chromatographic procedure.MethodsX · 2023Article
- Structural and functional analysis of Hydra Actinoporin-Like Toxin 1 (HALT-1).Scientific reports · 2021Article
- Article
- Evaluation of Hydra HALT-1 as a toxin moiety for recombinant immunotoxin.BMC biotechnology · 2020Article
- Article
- Response of Cellular Innate Immunity to Cnidarian Pore-Forming Toxins.Molecules (Basel, Switzerland) · 2018Review
- The chemical armament of reef-building corals: inter- and intra-specific variation and the identification of an unusual actinoporin in Stylophora pistilata.Scientific reports · 2018Article
- Pharmacological characterization of cnidarian extracts from the Caribbean Sea: evaluation of anti-snake venom and antitumor properties.The journal of venomous animals and toxins including tropical diseases · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actinoporins are small 18.5 kDa pore-forming toxins. A family of six actinoporin genes has been identified in the genome of Hydra magnipapillata, and HALT-1 (Hydra actinoporin-like toxin-1) has been shown to have haemolytic activity. In this study, we have used site-directed mutagenesis to investigate the role of amino acids in the pore-forming N-terminal region and the conserved aromatic cluster required for cell membrane binding. A total of 10 mutants of HALT-1 were constructed and tested for their haemolytic and cytolytic activity on human erythrocytes and HeLa cells, respectively. Insertion of 1-4 negatively charged residues in the N-terminal region of HALT-1 strongly reduced haemolytic and cytolytic activity, suggesting that the length or charge of the N-terminal region is critical for pore-forming activity. Moreover, substitution of amino acids in the conserved aromatic cluster reduced haemolytic and cytolytic activity by more than 80%, suggesting that these aromatic amino acids are important for attachment to the lipid membrane as shown for other actinoporins. The results suggest that HALT-1 and other actinoporins share similar mechanisms of pore formation and that it is critical for HALT-1 to maintain an amphipathic helix at the N-terminus and an aromatic amino acid-rich segment at the site of membrane binding.
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