Search results for "Oligomerisation"

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Lipid and phase specificity of α-toxin from S. aureus

2013

AbstractThe pore forming toxin Hla (α-toxin) from Staphylococcus aureus is an important pathogenic factor of the bacterium S. aureus and also a model system for the process of membrane-induced protein oligomerisation and pore formation. It has been shown that binding to lipid membranes at neutral or basic pH requires the presence of a phosphocholine-headgroup. Thus, sphingomyelin and phosphatidylcholine may serve as interaction partners in cellular membranes. Based on earlier studies it has been suggested that rafts of sphingomyelin are particularly efficient in toxin binding. In this study we compared the oligomerisation of Hla on liposomes of various lipid compositions in order to identif…

Staphylococcus aureusPore formationLiquid ordered phaseBacterial ToxinsLipid BilayersBiophysicsBiologyBiochemistryPhase Transitionchemistry.chemical_compoundHemolysin ProteinsMembrane LipidsMembrane MicrodomainsPhosphatidylcholineBinding siteLipid raftUnilamellar LiposomesPore-forming toxinLiposomeArtificial membranesBinding SitesCell MembraneOligomerisationCell BiologyS. aureusSphingomyelinsMembraneBiochemistrychemistryMicroscopy FluorescenceMutationPhosphatidylcholineslipids (amino acids peptides and proteins)Protein MultimerizationToxinSphingomyelinBiochimica et Biophysica Acta (BBA) - Biomembranes
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