Perfringolysin O Theta Toxin as a Tool to Monitor the Distribution and Inhomogeneity of Cholesterol in Cellular Membranes [PDF]
Toxins, 2016 Cholesterol is an essential structural component of cellular membranes in eukaryotes. Cholesterol in the exofacial leaflet of the plasma membrane is thought to form membrane nanodomains with sphingolipids and specific proteins.
Masashi Maekawa +2 more
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Inflammasome Activation Induced by Perfringolysin O of Clostridium perfringens and Its Involvement in the Progression of Gas Gangrene [PDF]
Frontiers in Microbiology, 2019 Clostridium perfringens (C. perfringens) is Gram-positive anaerobic, spore-forming rod-shaped bacterial pathogen that is widely distributed in nature. This bacterium is known as the causative agent of a foodborne illness and of gas gangrene.
Kiyonobu Yamamura +8 more
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Interaction of Cholesterol with Perfringolysin O: What Have We Learned from Functional Analysis? [PDF]
Toxins, 2017 Cholesterol-dependent cytolysins (CDCs) constitute a family of pore-forming toxins secreted by Gram-positive bacteria. These toxins form transmembrane pores by inserting a large β-barrel into cholesterol-containing membranes.
Sergey N. Savinov, Alejandro P. Heuck
doaj +2 more sources
Antibody-mediated neutralization of perfringolysin o for intracellular protein delivery. [PDF]
Mol Pharm, 2015 Perfringolysin O (PFO) is a member of the cholesterol-dependent cytolysin (CDC) family of bacterial pore-forming proteins, which are highly efficient in delivering exogenous proteins to the cytoplasm. However, the indiscriminate and potent cytotoxicity of PFO limits its practical use as an intracellular delivery system.
Yang NJ +5 more
europepmc +5 more sources
Preparation and utility of asymmetric lipid vesicles for studies of perfringolysin O-lipid interactions. [PDF]
Methods Enzymol, 2021 Studying the interaction of pore-forming toxins, including perfringolysin O (PFO), with lipid is crucial to understanding how they insert into membranes, assemble, and associate with membrane domains. In almost all past studies, symmetric lipid bilayers, i.e., bilayers having the same lipid composition in each monolayer (leaflet), have been used to ...
Kakuda S, Li B, London E.
europepmc +4 more sources
The Barrier Disruption and Pyroptosis of Intestinal Epithelial Cells Caused by Perfringolysin O (PFO) from Clostridium perfringens [PDF]
CellsClostridium perfringens (C. perfringens), a Gram-positive bacterium, produces a variety of toxins and extracellular enzymes that can lead to disease in both humans and animals.
Zhankui Liu +10 more
doaj +2 more sources
Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins. [PDF]
J Mol Biol, 2007 Cholesterol-dependent cytolysins (CDCs), a large family of bacterial toxins, are secreted as water-soluble monomers and yet are capable of generating oligomeric pores in membranes. Previous work has demonstrated that large scale structural rearrangements occur during this transition but the detailed mechanism by which these changes take place remains a
Rossjohn J +5 more
europepmc +4 more sources
Functional Dissection of Leishmania major Membrane Components in Resistance to Cholesterol-Dependent Cytolysins [PDF]
ToxinsBacteria use cholesterol-dependent cytolysins (CDCs) to damage eukaryotes. While well-studied in mammals, the mechanisms by which CDCs bind to and kill protozoans remain unclear.
Chaitanya S. Haram +5 more
doaj +2 more sources
Perfringolysin O association with ordered lipid domains: implications for transmembrane protein raft affinity. [PDF]
Biophys J, 2010 Upon interaction with cholesterol, perfringolysin O (PFO) inserts into membranes and forms a rigid transmembrane (TM) β-barrel. PFO is believed to interact with liquid ordered lipid domains (lipid rafts). Because the origin of TM protein affinity for rafts is poorly understood, we investigated PFO raft affinity in vesicles having coexisting ordered and
Nelson LD, Chiantia S, London E.
europepmc +4 more sources
The solution structure and oligomerization behavior of two bacterial toxins: pneumolysin and perfringolysin O. [PDF]
Biophys J, 2004 Pneumolysin (PLY), an important protein virulence factor of the human bacterial pathogen Streptococcus pneumoniae, could be a candidate for inclusion in a new anti-streptococcal vaccine. PLY solution species from monomer via multimeric intermediates to ring-shaped oligomers were studied with time-dependent sedimentation velocity in the analytical ...
Solovyova AS +3 more
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