Structures of the Pore-Forming Toxin Monalysin solved by X-ray crystallography and electron microscopy

Abstract

Event Abstract Back to Event Structures of the Pore-Forming Toxin Monalysin solved by X-ray crystallography and electron microscopy Philippe Leone1*, Cecilia Bebeacua1, Onya Opota2, Christine Kellenberger1, Bruno Lemaitre3 and Alain Roussel1 1 Architecture et Fonction des Macromolecules Biologiques (AFMB), UMR 7257 CNRS et Aix-Marseille Université, France 2 Institute of Microbiology, University of Lausanne and University Hospital Center, Switzerland 3 Global Health Institute, Ecole Polytechnique Fédérale Lausanne (EPFL), Switzerland Pore Forming Toxins (PFT) represent the largest class of bacterial protein toxins and are often important virulence factors of a pathogen. These proteins are initially produced as soluble molecules and association with a target membrane, generally via specific receptors, induces their oligomerization in a ring-like structure. Subsequent structural rearrangements of each protomer lead to the formation of a water-filed pore. Depending on the PFT, pore formation is aimed at permeabilizing the target membrane or can serve as a translocation channel to introduce other virulence factors into the target cell. The structure of several PFT has been determined, but for only one the structures of both the soluble and the pore form are available. Nevertheless, the molecular mechanisms involved in the soluble to transmenbrane form transition of PFT are still unknown. Monalysin was recently identified as a new virulence factor secreted by the Drosophila pathogen Pseudomonas entomophila. The studies we carried out highlighted that Monalysin is a PFT involved in the ability of the pathogen to induce intestinal cell damages into the host gut. Here we present the structures of pro-Monalysin, cleaved form and inactive mutant that have been solved by X-ray crystallography or electron microscopy. On the basis of these structures a possible mechanism of action for Monalysin is presented. Keywords: Host-Pathogen Interactions, entomo pathogen, Pore-Forming-Toxin, X-ray crystallography, Electron microscopy Conference: 15th International Congress of Immunology (ICI), Milan, Italy, 22 Aug - 27 Aug, 2013. Presentation Type: Abstract Topic: Host-pathogen interactions Citation: Leone P, Bebeacua C, Opota O, Kellenberger C, Lemaitre B and Roussel A (2013). Structures of the Pore-Forming Toxin Monalysin solved by X-ray crystallography and electron microscopy. Front. Immunol. Conference Abstract: 15th International Congress of Immunology (ICI). doi: 10.3389/conf.fimmu.2013.02.00852 Copyright: The abstracts in this collection have not been subject to any Frontiers peer review or checks, and are not endorsed by Frontiers. They are made available through the Frontiers publishing platform as a service to conference organizers and presenters. The copyright in the individual abstracts is owned by the author of each abstract or his/her employer unless otherwise stated. Each abstract, as well as the collection of abstracts, are published under a Creative Commons CC-BY 4.0 (attribution) licence (https://creativecommons.org/licenses/by/4.0/) and may thus be reproduced, translated, adapted and be the subject of derivative works provided the authors and Frontiers are attributed. For Frontiers’ terms and conditions please see https://www.frontiersin.org/legal/terms-and-conditions. Received: 19 Jun 2013; Published Online: 22 Aug 2013. * Correspondence: Dr. Philippe Leone, Architecture et Fonction des Macromolecules Biologiques (AFMB), UMR 7257 CNRS et Aix-Marseille Université, Marseille, France, Philippe.Leone@afmb.univ-mrs.fr Login Required This action requires you to be registered with Frontiers and logged in. To register or login click here. Abstract Info Abstract The Authors in Frontiers Philippe Leone Cecilia Bebeacua Onya Opota Christine Kellenberger Bruno Lemaitre Alain Roussel Google Philippe Leone Cecilia Bebeacua Onya Opota Christine Kellenberger Bruno Lemaitre Alain Roussel Google Scholar Philippe Leone Cecilia Bebeacua Onya Opota Christine Kellenberger Bruno Lemaitre Alain Roussel PubMed Philippe Leone Cecilia Bebeacua Onya Opota Christine Kellenberger Bruno Lemaitre Alain Roussel Related Article in Frontiers Google Scholar PubMed Abstract Close Back to top Javascript is disabled. Please enable Javascript in your browser settings in order to see all the content on this page.