Prepore for a breakthrough.

10.1038/nsmb0505-385

A key to understanding bacterial pathogenicity is the mechanism by which water-soluble protein toxins assemble on cell membranes to form oligomeric bilayer-spanning pores. The recent reconstructions from cryo-electron micrographs of three-dimensional pore and prepore structures of the cholesterol-dependent toxin pneumolysin shed new light on the later steps of the assembly of large toxin pores.