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Prepore for a breakthrough

Nature Structural & Molecular Biology volume 12, pages 385–386 (2005)Cite this article

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.

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Figure 1: Pore formation by CDCs.
Figure 2: A general pathway for the assembly of PFTs that form β-barrels.

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Authors and Affiliations

  1. Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, England, UK

    Hagan Bayley, Lakmal Jayasinghe & Mark Wallace

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Bayley, H., Jayasinghe, L. & Wallace, M. Prepore for a breakthrough. Nat Struct Mol Biol 12, 385–386 (2005). https://doi.org/10.1038/nsmb0505-385

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