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The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism

Author

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  • Marcus Mueller

    (Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland
    Present addresses: Paul Scherrer Institut, 5232 Villigen PSI, Switzerland (M.M.); Formulation R&D Biologics, Pharmaceutical and Analytical R&D, F. Hoffmann-La Roche Ltd, 4070 Basel, Switzerland (U.G.).)

  • Ulla Grauschopf

    (Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland
    Present addresses: Paul Scherrer Institut, 5232 Villigen PSI, Switzerland (M.M.); Formulation R&D Biologics, Pharmaceutical and Analytical R&D, F. Hoffmann-La Roche Ltd, 4070 Basel, Switzerland (U.G.).)

  • Timm Maier

    (Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland)

  • Rudi Glockshuber

    (Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland)

  • Nenad Ban

    (Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland)

Abstract

α-helical toxin assembly Some toxins exert cytotoxicity by assembling into multimeric pores in the membranes of their host cells. The bacterial α-helical toxin cytolysin A, responsible for the haemolytic phenotype of several Escherichia coli and Salmonella enterica strains, is one such pore-forming toxin, whose soluble structure is known. Here Mueller et al. describe the structure of its assembled dodecameric pore. The authors propose a sequential mechanism for the large rearrangements that the monomers undergo to form the α-helical pore.

Suggested Citation

  • Marcus Mueller & Ulla Grauschopf & Timm Maier & Rudi Glockshuber & Nenad Ban, 2009. "The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism," Nature, Nature, vol. 459(7247), pages 726-730, June.
    • Handle: RePEc:nat:nature:v:459:y:2009:i:7247:d:10.1038_nature08026
    DOI: 10.1038/nature08026
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