Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin
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The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assemblyCholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O bindingCharacterization of a streptococcal cholesterol-dependent cytolysin with a lewis y and b specific lectin domainMultifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenesThe pore-forming haemolysins of bacillus cereus: a reviewCellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracisStructural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent CytolysinsCryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin.Disentangling the roles of cholesterol and CD59 in intermedilysin pore formation.The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support β-Barrel Pore Insertion.An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysinsDisulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins.Membrane assembly of the cholesterol-dependent cytolysin pore complex.Imaging enzyme-triggered self-assembly of small molecules inside live cellsOnly two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.Arcanolysin is a cholesterol-dependent cytolysin of the human pathogen Arcanobacterium haemolyticum.Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin OConformational changes that effect oligomerization and initiate pore formation are triggered throughout perfringolysin O upon binding to cholesterol.The cholesterol-dependent cytolysin pneumolysin from Streptococcus pneumoniae binds to lipid raft microdomains in human corneal epithelial cellsStructural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.The cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.Crystal structure of cytotoxin protein suilysin from Streptococcus suis.The helix-loop-helix motif at the N terminus of HalI is essential for its immunity function against halocin C8.Clostridial toxins.Bacterial toxins and the nervous system: neurotoxins and multipotential toxins interacting with neuronal cells.Identification of the high affinity binding site in the Streptococcus intermedius toxin intermedilysin for its membrane receptor, the human complement regulator CD59.Taurine Boosts Cellular Uptake of Small D-Peptides for Enzyme-Instructed Intracellular Molecular Self-AssemblyIntermedilysin-receptor interactions during assembly of the pore complex: assembly intermediates increase host cell susceptibility to complement-mediated lysisGILT is a critical host factor for Listeria monocytogenes infection.The diversity of receptor recognition in cholesterol-dependent cytolysins.Genetic and biochemical diversity of Gardnerella vaginalis strains isolated from women with bacterial vaginosis.
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Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 05 April 2007
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Specific protein-membrane cont ...... holesterol-dependent cytolysin
@en
Specific protein-membrane cont ...... olesterol-dependent cytolysin.
@nl
type
label
Specific protein-membrane cont ...... holesterol-dependent cytolysin
@en
Specific protein-membrane cont ...... olesterol-dependent cytolysin.
@nl
prefLabel
Specific protein-membrane cont ...... holesterol-dependent cytolysin
@en
Specific protein-membrane cont ...... olesterol-dependent cytolysin.
@nl
P2093
P2860
P356
P1476
Specific protein-membrane cont ...... holesterol-dependent cytolysin
@en
P2093
Arthur E Johnson
Casie E Soltani
Eileen M Hotze
Rodney K Tweten
P2860
P304
15709-15716
P356
10.1074/JBC.M701173200
P407
P577
2007-04-05T00:00:00Z