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

Stefan Köster, Katharina van Pee, Martina Hudel, Martin Leustik, Daniel Rhinow, Werner Kühlbrandt, Trinad Chakraborty and Özkan Yildiz ()
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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

Nature Communications, 2014, vol. 5, issue 1, 1-14

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms4690

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