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Pneumolysin, a virulence factor from the human pathogen Streptococcus pneumoniae, is a water-soluble protein which forms ring-shaped oligomeric structures upon binding to cholesterol-containing lipid membranes. It induces vesicle aggregation, membrane pore formation and withdrawal of lipid material into non-bilayer proteolipid complexes. Solid-state magic angle spinning and wideline static NMR, together with freeze-fracture electron microscopy, are used to characterize the phase changes in fully hydrated cholesterol-containing lipid membranes induced by the addition of pneumolysin. A structural model for the proteolipid complexes is proposed where a 30-50-meric pneumolysin ring lines the inside of a lipid torus. Cholesterol is found to be essential to the fusogenic action of pneumolysin.

Type

Journal article

Journal

Molecular Membrane Biology

Publication Date

2000

Volume

17

Pages

229 - 235

Keywords

pneumolysin solid-state nmr freeze-fracture electron microscopy protein-lipid interactions cholesterol cytochrome-c interactions pore-forming toxin streptococcus-pneumoniae phospholipid-membranes complement activation perfringolysin-o streptolysin-o lipid bilayers protein toxin nmr