ArticleThe Biochemical journal2004
Membrane insertion of the N-terminal alpha-helix of equinatoxin II, a sea anemone cytolytic toxin.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 52 citations in OpenAlex.
- Elucidating the structure and assembly mechanism of actinoporin pores in complex membrane environments.Science advances · 2025Article
- Sea Anemones, Actinoporins, and Cholesterol.International journal of molecular sciences · 2022Review
- Structural and functional analysis of Hydra Actinoporin-Like Toxin 1 (HALT-1).Scientific reports · 2021Article
- Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea AnemoneInternational journal of molecular sciences · 2020Review
- Sequence Diversity in the Pore-Forming Motifs of the Membrane-Damaging Protein Toxins.The Journal of membrane biology · 2020Review
- Evaluation of Hydra HALT-1 as a toxin moiety for recombinant immunotoxin.BMC biotechnology · 2020Article
- Sticholysin, Sphingomyelin, and Cholesterol: A Closer Look at a Tripartite Interaction.Biophysical journal · 2019Article
- Sea Anemone Toxins: A Structural Overview.Marine drugs · 2019Review
- Article
- Multigene Family of Pore-Forming Toxins from Sea AnemoneMarine drugs · 2018Article
- Article
- Identification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of Actinoporins.The Journal of biological chemistry · 2016Article
- Sphingomyelin is sorted at the trans Golgi network into a distinct class of secretory vesicle.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Ancient Venom Systems: A Review on Cnidaria Toxins.Toxins · 2015Review
- Characterization of the Lipid-Binding Site of Equinatoxin II by NMR and Molecular Dynamics Simulation.Biophysical journal · 2015Article
- Mutagenesis and functional analysis of the pore-forming toxin HALT-1 from Hydra magnipapillata.Toxins · 2015Article
- Inactivation of the pore-forming toxin Sticholysin I by peroxynitrite: protection by cys groups incorporated in the toxin.The protein journal · 2014Article
- Functional characterization of sticholysin I and W111C mutant reveals the sequence of the actinoporin's pore assembly.PloS one · 2014Article
- Effect of human serum albumin upon the permeabilizing activity of sticholysin II, a pore forming toxin from Stichodactyla heliantus.The protein journal · 2013Article
- Membrane damage by an α-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered steps.The Journal of biological chemistry · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Equinatoxin II (Eqt-II) is a member of the actinoporins, a unique family of cytotoxins comprising 20 kDa pore-forming proteins isolated from sea anemones. Actinoporins bind preferentially to lipid membranes containing sphingomyelin, and create cation-selective pores by oligomerization of three to four monomers. Previous studies have shown that regions of Eqt-II crucial for its cytolytic mechanism are an exposed aromatic cluster and the N-terminal region containing an amphipathic alpha-helix. In the present study, we have investigated the transfer of the N-terminal alpha-helix into the lipid membrane by the use of three mutants containing an additional tryptophan residue in different positions within the amphipathic alpha-helix (Ile18-->Trp, Val22-->Trp and Ala25-->Trp). The interaction of the mutants with different model systems, such as lipid monolayers, erythrocytes and ghost membranes, was extensively characterized. Intrinsic fluorescence measurements and the use of vesicles containing brominated phospholipids indicated a deep localization of the N-terminal amphipathic helix in the lipid bilayer, except for the case of Val22-->Trp. This mutant is stabilized in a state immediately prior to final pore formation. The introduction of additional tryptophan residues in the sequence of Eqt-II has proved to be a suitable approach to monitor the new environments that surround defined regions of the molecule upon membrane interaction.
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