ArticleThe Journal of biological chemistry2015
A pore-forming toxin requires a specific residue for its activity in membranes with particular physicochemical properties.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- TseCurrent research in microbial sciences · 2026Article
- 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
- Sequence Diversity in the Pore-Forming Motifs of the Membrane-Damaging Protein Toxins.The Journal of membrane biology · 2020Review
- Actinoporins: From the Structure and Function to the Generation of Biotechnological and Therapeutic Tools.Biomolecules · 2020Review
- Effects of membrane lipid composition on Mycobacterium tuberculosis EsxA membrane insertion: A dual play of fluidity and charge.Tuberculosis (Edinburgh, Scotland) · 2019Article
- Article
- Piercing Fishes: Porin Expansion and Adaptation to Hematophagy in the Vampire Snail Cumia reticulata.Molecular biology and evolution · 2018Article
- Cholesterol promotes Cytolysin A activity by stabilizing the intermediates during pore formation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Multigene Family of Pore-Forming Toxins from Sea AnemoneMarine drugs · 2018Article
- 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
- Haemolytic actinoporins interact with carbohydrates using their lipid-binding module.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Article
- Identification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of Actinoporins.The Journal of biological chemistry · 2016Article
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5 authors.
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Abstract
The physicochemical landscape of the bilayer modulates membrane protein function. Actinoporins are a family of potent hemolytic proteins from sea anemones acting at the membrane level. This family of cytolysins preferentially binds to target membranes containing sphingomyelin, where they form lytic pores giving rise to cell death. Although the cytolytic activity of the actinoporin fragaceatoxin C (FraC) is sensitive to vesicles made of various lipid compositions, it is far from clear how this toxin adjusts its mechanism of action to a broad range of physiochemical landscapes. Herein, we show that the conserved residue Phe-16 of FraC is critical for pore formation in cholesterol-rich membranes such as those of red blood cells. The interaction of a panel of muteins of Phe-16 with model membranes composed of raft-like lipid domains is inactivated in cholesterol-rich membranes but not in cholesterol-depleted membranes. These results indicate that actinoporins recognize different membrane environments, resulting in a wider repertoire of susceptible target membranes (and preys) for sea anemones. In addition, this study has unveiled promising candidates for the development of protein-based biosensors highly sensitive to the concentration of cholesterol within the membrane.
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