ArticleBiophysical journal2001
Differential interaction of equinatoxin II with model membranes in response to lipid composition.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 76 citations in OpenAlex.
- Through the holes: the biotechnological potential of actinoporins (and other PFPs).Biophysical reviews · 2026Review
- Determination of the boundary lipids of sticholysins using tryptophan quenching.Scientific reports · 2022Article
- 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
- Lipid interactions of an actinoporin pore-forming oligomer.Biophysical journal · 2021Article
- Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea AnemoneInternational journal of molecular sciences · 2020Review
- 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
- Identification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of Actinoporins.The Journal of biological chemistry · 2016Article
- Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores.The Journal of biological chemistry · 2016Article
- A pore-forming toxin requires a specific residue for its activity in membranes with particular physicochemical properties.The Journal of biological chemistry · 2015Article
- Structural basis for self-assembly of a cytolytic pore lined by protein and lipid.Nature communications · 2015Article
- A cholesterol recognition motif in human phospholipid scramblase 1.Biophysical journal · 2014Article
- The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition.Journal of biosciences · 2011Article
- Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence.Biophysical journal · 2008Article
- Membranes: a meeting point for lipids, proteins and therapies.Journal of cellular and molecular medicine · 2008Review
- Infrared spectroscopy study on the conformational changes leading to pore formation of the toxin sticholysin II.Biophysical journal · 2007Article
- Membrane binding of zebrafish actinoporin-like protein: AF domains, a novel superfamily of cell membrane binding domains.The Biochemical journal · 2006Article
- Membrane insertion of the N-terminal alpha-helix of equinatoxin II, a sea anemone cytolytic toxin.The Biochemical journal · 2004Article
- Effects of the eukaryotic pore-forming cytolysin Equinatoxin II on lipid membranes and the role of sphingomyelin.Biophysical journal · 2003Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Equinatoxin II is a 179-amino-acid pore-forming protein isolated from the venom of the sea anemone Actinia equina. Large unilamellar vesicles and lipid monolayers of different lipid compositions have been used to study its interaction with membranes. The critical pressure for insertion is the same in monolayers made of phosphatidylcholine or sphingomyelin (approximately 26 mN m(-1)) and explains why the permeabilization of large unilamellar vesicles by equinatoxin II with these lipid compositions is null or moderate. In phosphatidylcholine-sphingomyelin (1:1) monolayers, the critical pressure is higher (approximately 33 mN m(-1)), thus permitting the insertion of equinatoxin II in large unilamellar vesicles, a process that is accompanied by major conformational changes. In the presence of vesicles made of phosphatidylcholine, a fraction of the protein molecules remains associated with the membranes. This interaction is fully reversible, does not involve major conformational changes, and is governed by the high affinity for membrane interfaces of the protein region comprising amino acids 101-120. We conclude that although the presence of sphingomyelin within the membrane creates conditions for irreversible insertion and pore formation, this lipid is not essential for the initial partitioning event, and its role as a specific receptor for the toxin is not so clear-cut.
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