Fusogenic activity of delta-haemolysin from Staphylococcus aureus in phospholipid vesicles in the liquid-crystalline phase.
A study has been conducted of the interaction of the lytic toxin delta-haemolysin with vesicles of phospholipid, using electron microscopy, fluorescence depolarisation and excimer fluorescence. The peptide is shown to be a fusogen towards phosphatidylcholine vesicles in fluid phases. In the presence of gel phase lipid, fusion between fluid and gel phases is not seen. Fluid phase lipid vesicles are fused together to form large multilamellar structures, and initial vesicle size does not appear to be important since small unilamellar vesicles and large unilamellar vesicles are similarly affected. Fusogenic activity of delta-haemolysin is compared to that of melittin. The former is a progressive fusogen for fluid phase lipid, while the latter causes vesicle fusion in a manner related to occurrence of a lipid phase transition.
D015060:1,2-Dipalmitoylphosphatidylcholine; D001426:Bacterial Proteins / Q000494:pharmacology*; D004161:Diphenylhexatriene; D005454:Fluorescence Polarization; D005456:Fluorescent Dyes; D006460:Hemolysin Proteins; D008081:Liposomes; D008555:Melitten / Q000494:pharmacology; D008560:Membrane Fluidity; D008561:Membrane Fusion / Q000187:drug effects*; D008854:Microscopy, Electron; D013050:Spectrometry, Fluorescence
D001426:Bacterial Proteins; D005456:Fluorescent Dyes; D006460:Hemolysin Proteins; D008081:Liposomes; D004161:Diphenylhexatriene; D008555:Melitten; D015060:1,2-Dipalmitoylphosphatidylcholine; C025994:delta hemolysin protein, Staphylococcus aureus