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  Bacterial Porin Disrupts Mitochondrial Membrane Potential and Sensitizes Host Cells to Apoptosis

Kozjak-Pavlovic, V., Dian-Lothrop, E. A., Meinecke, M., Kepp, O., Ross, K., Rajalingam, K., et al. (2009). Bacterial Porin Disrupts Mitochondrial Membrane Potential and Sensitizes Host Cells to Apoptosis. PLoS Pathogens, 5(10): e1000629.

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PLoS_Pathogens_2009_5_e1000629.pdf (Publisher version), 912KB
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© 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.
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Kozjak-Pavlovic, Vera1, Author
Dian-Lothrop, Elke A., Author
Meinecke, Michael, Author
Kepp, Oliver2, Author              
Ross, Katharina2, Author              
Rajalingam, Krishnaraj2, Author              
Harsman, Anke3, Author              
Hauf, Eva4, Author              
Brinkmann, Volker4, Author              
Günther, Dirk2, Author              
Herrmann, Ines2, Author              
Hurwitz, Robert5, Author              
Rassow, Joachim, Author
Wagner, Richard, Author
Rudel, Thomas2, Author              
Affiliations:
1Max Planck Society, ou_persistent13              
2Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664147              
3Core Facilities / Proteinanalysis, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664143              
4Core Facilities / Microscopy, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664142              
5Core Facilities / Proteinpurification, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664144              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2009-10
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: eDoc: 442414
ISI: 000272033300033
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Title: PLoS Pathogens
Source Genre: Journal
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Pages: - Volume / Issue: 5 (10) Sequence Number: e1000629 Start / End Page: - Identifier: ISSN: 1553-7366