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          Institute: MPI für Infektionsbiologie     Collection: Department of Molecular Biology     Display Documents



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ID: 442414.0, MPI für Infektionsbiologie / Department of Molecular Biology
Bacterial Porin Disrupts Mitochondrial Membrane Potential and Sensitizes Host Cells to Apoptosis
Authors:Kozjak-Pavlovic, Vera; Dian-Lothrop, Elke A.; Meinecke, Michael; Kepp, Oliver; Ross, Katharina; Rajalingam, Krishnaraj; Harsman, Anke; Hauf, Eva; Brinkmann, Volker; Günther, Dirk; Herrmann, Ines; Hurwitz, Robert; Rassow, Joachim; Wagner, Richard; Rudel, Thomas
Language:English
Date of Publication (YYYY-MM-DD):2009-10
Title of Journal:PLoS Pathogens
Volume:5
Issue / Number:10
Sequence Number of Article:e1000629
Copyright:© 2009 Kozjak-Pavlovic et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:The bacterial PorB porin, an ATP-binding beta-barrel protein of pathogenic Neisseria gonorrhoeae, triggers host cell apoptosis by an unknown mechanism. PorB is targeted to and imported by host cell mitochondria, causing the breakdown of the mitochondrial membrane potential (Delta psi(m)). Here, we show that PorB induces the condensation of the mitochondrial matrix and the loss of cristae structures, sensitizing cells to the induction of apoptosis via signaling pathways activated by BH3-only proteins. PorB is imported into mitochondria through the general translocase TOM but, unexpectedly, is not recognized by the SAM sorting machinery, usually required for the assembly of beta-barrel proteins in the mitochondrial outer membrane. PorB integrates into the mitochondrial inner membrane, leading to the breakdown of Delta psi(m). The PorB channel is regulated by nucleotides and an isogenic PorB mutant defective in ATP-binding failed to induce Delta psi(m) loss and apoptosis, demonstrating that dissipation of Delta psi(m) is a requirement for cell death caused by neisserial infection.
External Publication Status:published
Document Type:Article
Communicated by:Hilmar Fünning
Affiliations:MPI für Infektionsbiologie/Department of Molecular Biology
MPI für Infektionsbiologie/Core Facilities
External Affiliations:Biocenter, Chair of Microbiology, University of Würzburg, Würzburg, Germany; Institute for Physiological Chemistry, Ruhr-University Bochum, Bochum, Germany; Department of Biology/Chemistry, Division of Biophysics, University of Osnabrück, Osnabrück, Germany.
Identifiers:ISI:000272033300033 [ID No:1]
ISSN:1553-7366 [ID No:2]
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