Multi-scale molecular dynamics study of cholera pentamer binding to a GM1-phospholipid membrane |
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| Affiliation: | 1. Physics Department, Humboldt University Berlin, Newtonstr. 15, 12489 Berlin, Germany;2. Frascati National Laboratory, National Institute for Nuclear Physics, Via Enrico Fermi 40, 00044 Frascati (Rome), Italy;3. Bogoliubov Laboratory of Theoretical Physics, Joint Institute for Nuclear Research, Joliot-Curie Str. 6, 141980 Dubna, Russia;1. Physics Department, Brookhaven National Laboratory, Upton, NY 11973, USA;2. Physik Department, Technische Universität München, D-85748 Garching, Germany;1. Center for Theoretical Physics, MIT, Cambridge MA 02139, USA;2. Institute for Theoretical Physics and Center for Extreme Matter and Emergent Phenomena, Utrecht University, Leuvenlaan 4, 3584 CE Utrecht, The Netherlands;1. Cyclotron Institute and Department of Physics & Astronomy, Texas A&M University, College Station, TX 77843-3366, USA;2. Department of Applied Physics, Nanjing University of Science and Technology, Nanjing, China;1. Department of Physics, Sejong University, Seoul 143-747, Republic of Korea;2. Physics Department, Brookhaven National Laboratory, Upton, NY 11973, USA;3. Institute for Theoretical Physics, Heidelberg University, Philosophenweg 16, 69120 Heidelberg, Germany |
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| Abstract: | The AB5 type toxin produced by the Vibrio cholerae bacterium is the causative agent of the cholera disease. The cholera toxin (CT) has been shown to bind specifically to GM1 glycolipids on the membrane surface. This binding of CT to the membrane is the initial step in its endocytosis and has been postulated to cause significant disruption to the membrane structure. In this work, we have carried out a combination of coarse-grain and atomistic simulations to study the binding of CT to a membrane modelled as an asymmetrical GM1-DPPC bilayer. Simulation results indicate that the toxin binds to the membrane through only three of its five B subunits, in effect resulting in a tilted bound configuration. Additionally, the binding of the CT can increase the area per lipid of GM1 leaflet, which in turn can cause the membrane regions interacting with the bound subunits to experience significant bilayer thinning and lipid tail disorder across both the leaflets. |
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| Keywords: | Protein-lipid interactions Molecular dynamics simulation Cholera toxin GM1 ganglioside Membrane curvature |
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