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Berlin 2018 – scientific programme

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BP: Fachverband Biologische Physik

BP 15: Postersession III

BP 15.2: Poster

Tuesday, March 13, 2018, 14:00–16:00, Poster B

The Role of Lipids in Membrane Docking and Pore Formation of Pneumolysin — •Martin Vögele1, Ramachandra Bhaskara1, Katharina van Pee2, Özkan Yildiz2, Werner Kühlbrandt2, and Gerhard Hummer1,31Department of Theoretical Biophysics, Max Planck Institute of Biophysics — 2Department of Structural Biology, Max Planck Institute of Biophysics — 3Institute for Biophysics, Goethe University, Frankfurt am Main

Streptococcous pneumoniae employs pneumolysin (PLY) to infect its human host. The specificity of PLY to cholesterol-rich membranes targets this virulence factor to mammalian cells. PLY is released in a water-soluble monomeric form. Subsequent docking and oligomerization of PLY result in the formation of membrane-embedded ring-like structures that induce cytolytic pores. Recent structural studies have resolved the structure of PLY rings in pore and pre-pore conformations on membranes. However, the detailed mechanism of pore formation and the role of lipids remain unclear.

Using large-scale coarse-grained molecular dynamics simulations, we study (1) the docking of PLY to membranes and (2) the subsequent formation of cytolytic pores. In simulations of large rings, we investigate the behavior of lipids during pore formation. We also perform all-atom molecular dynamics simulations of monomeric PLY in solution and of various membrane-docked states to understand conformational changes. These simulations, along with structural modeling, shed light on the mechanism of PLY-induced formation of membrane pores.

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