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Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation

Author

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  • Stefan Köster

    (Max Planck Institute of Biophysics)

  • Katharina van Pee

    (Max Planck Institute of Biophysics)

  • Martina Hudel

    (Institute for Medical Microbiology, German Centre for Infection Research (DZIF) Partner site Giessen-Marburg-Langen, Justus-Liebig University)

  • Martin Leustik

    (Institute for Medical Microbiology, German Centre for Infection Research (DZIF) Partner site Giessen-Marburg-Langen, Justus-Liebig University)

  • Daniel Rhinow

    (Max Planck Institute of Biophysics)

  • Werner Kühlbrandt

    (Max Planck Institute of Biophysics)

  • Trinad Chakraborty

    (Institute for Medical Microbiology, German Centre for Infection Research (DZIF) Partner site Giessen-Marburg-Langen, Justus-Liebig University)

  • Özkan Yildiz

    (Max Planck Institute of Biophysics)

Abstract

Listeriolysin O (LLO) is an essential virulence factor of Listeria monocytogenes that causes listeriosis. Listeria monocytogenes owes its ability to live within cells to the pH- and temperature-dependent pore-forming activity of LLO, which is unique among cholesterol-dependent cytolysins. LLO enables the bacteria to cross the phagosomal membrane and is also involved in activation of cellular processes, including the modulation of gene expression or intracellular Ca2+ oscillations. Neither the pore-forming mechanism nor the mechanisms triggering the signalling processes in the host cell are known in detail. Here, we report the crystal structure of LLO, in which we identified regions important for oligomerization and pore formation. Mutants were characterized by determining their haemolytic and Ca2+ uptake activity. We analysed the pore formation of LLO and its variants on erythrocyte ghosts by electron microscopy and show that pore formation requires precise interface interactions during toxin oligomerization on the membrane.

Suggested Citation

  • Stefan Köster & Katharina van Pee & Martina Hudel & Martin Leustik & Daniel Rhinow & Werner Kühlbrandt & Trinad Chakraborty & Özkan Yildiz, 2014. "Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation," Nature Communications, Nature, vol. 5(1), pages 1-14, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4690
    DOI: 10.1038/ncomms4690
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    Cited by:

    1. Rupert L. Mayer & Rein Verbeke & Caroline Asselman & Ilke Aernout & Adillah Gul & Denzel Eggermont & Katie Boucher & Fabien Thery & Teresa M. Maia & Hans Demol & Ralf Gabriels & Lennart Martens & Chri, 2022. "Immunopeptidomics-based design of mRNA vaccine formulations against Listeria monocytogenes," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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