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In this paper we describe reconstructions by electron cryo-microscopy of two oligomeric states of the pore-forming toxin pneumolysin. The results are interpreted by the fitting of atomic models of separated domains to the 3-dimensional electron density maps, revealing two steps in the mechanism of pore formation by the family of cholesterol-binding toxins. We briefly describe the observation of the toxin pore in model membranes and contrast the apparent mechanism of pneumolysin with that of other pore-forming toxins.

Original publication




Journal article


Int J Med Microbiol

Publication Date





389 - 394


Bacterial Proteins, Bacterial Toxins, Cholesterol, Cytotoxins, Hemolysin Proteins, Microscopy, Electron, Protein Conformation, Protein Subunits, Streptolysins