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The assembly dynamics of the cytolytic pore toxin ClyA

Author

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  • Stephan Benke

    (University of Zurich)

  • Daniel Roderer

    (ETH Zurich, Institute of Molecular Biology and Biophysics)

  • Bengt Wunderlich

    (University of Zurich)

  • Daniel Nettels

    (University of Zurich)

  • Rudi Glockshuber

    (ETH Zurich, Institute of Molecular Biology and Biophysics)

  • Benjamin Schuler

    (University of Zurich)

Abstract

Pore-forming toxins are protein assemblies used by many organisms to disrupt the membranes of target cells. They are expressed as soluble monomers that assemble spontaneously into multimeric pores. However, owing to their complexity, the assembly processes have not been resolved in detail for any pore-forming toxin. To determine the assembly mechanism for the ring-shaped, homododecameric pore of the bacterial cytolytic toxin ClyA, we collected a diverse set of kinetic data using single-molecule spectroscopy and complementary techniques on timescales from milliseconds to hours, and from picomolar to micromolar ClyA concentrations. The entire range of experimental results can be explained quantitatively by a surprisingly simple mechanism. First, addition of the detergent n-dodecyl-β-D-maltopyranoside to the soluble monomers triggers the formation of assembly-competent toxin subunits, accompanied by the transient formation of a molten-globule-like intermediate. Then, all sterically compatible oligomers contribute to assembly, which greatly enhances the efficiency of pore formation compared with simple monomer addition.

Suggested Citation

  • Stephan Benke & Daniel Roderer & Bengt Wunderlich & Daniel Nettels & Rudi Glockshuber & Benjamin Schuler, 2015. "The assembly dynamics of the cytolytic pore toxin ClyA," Nature Communications, Nature, vol. 6(1), pages 1-15, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7198
    DOI: 10.1038/ncomms7198
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