ArticleThe Journal of biological chemistry2016
Identification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of Actinoporins.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Stepwise assembly of α-hemolysin from intermediates to the mature pore in native erythrocytes.The Journal of cell biology · 2026Article
- Through the holes: the biotechnological potential of actinoporins (and other PFPs).Biophysical reviews · 2026Review
- Elucidating the structure and assembly mechanism of actinoporin pores in complex membrane environments.Science advances · 2025Article
- The Biological Role of Conoporins, Actinoporin-like Pore-Forming Toxins from Cone Snails.Toxins · 2025Review
- Cryo-EM structures of a protein pore reveal a cluster of cholesterol molecules and diverse roles of membrane lipids.Nature communications · 2025Article
- Sea Anemones, Actinoporins, and Cholesterol.International journal of molecular sciences · 2022Review
- Challenges and approaches to studying pore-forming proteins.Biochemical Society transactions · 2021Review
- Panorama of the Intracellular Molecular Concert Orchestrated by Actinoporins, Pore-Forming Toxins from Sea Anemones.Toxins · 2021Review
- Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea AnemoneInternational journal of molecular sciences · 2020Review
- Actinoporins: From the Structure and Function to the Generation of Biotechnological and Therapeutic Tools.Biomolecules · 2020Review
- Article
- Pore-Forming Proteins from Cnidarians and Arachnids as Potential Biotechnological Tools.Toxins · 2019Article
- Identification of a pore-forming protein from sea anemoneThe journal of venomous animals and toxins including tropical diseases · 2019Article
- Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone.Biophysical reviews · 2017Review
- Haemolytic actinoporins interact with carbohydrates using their lipid-binding module.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Article
- Disrupting a key hydrophobic pair in the oligomerization interface of the actinoporins impairs their pore-forming activity.Protein science : a publication of the Protein Society · 2017Article
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10 authors.
Funding
Abstract
Pore-forming toxins (PFTs) are cytolytic proteins belonging to the molecular warfare apparatus of living organisms. The assembly of the functional transmembrane pore requires several intermediate steps ranging from a water-soluble monomeric species to the multimeric ensemble inserted in the cell membrane. The non-lytic oligomeric intermediate known as prepore plays an essential role in the mechanism of insertion of the class of β-PFTs. However, in the class of α-PFTs, like the actinoporins produced by sea anemones, evidence of membrane-bound prepores is still lacking. We have employed single-particle cryo-electron microscopy (cryo-EM) and atomic force microscopy to identify, for the first time, a prepore species of the actinoporin fragaceatoxin C bound to lipid vesicles. The size of the prepore coincides with that of the functional pore, except for the transmembrane region, which is absent in the prepore. Biochemical assays indicated that, in the prepore species, the N terminus is not inserted in the bilayer but is exposed to the aqueous solution. Our study reveals the structure of the prepore in actinoporins and highlights the role of structural intermediates for the formation of cytolytic pores by an α-PFT.
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