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  Targeting of a Chlamydial Protease Impedes Intracellular Bacterial Growth

Christian, J. G., Heymann, J., Paschen, S. A., Vier, J., Schauenburg, L., Rupp, J., et al. (2011). Targeting of a Chlamydial Protease Impedes Intracellular Bacterial Growth. PLoS Pathogens, 7(9): e1002283. doi:10.1371/journal.ppat.1002283.

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Genre: Journal Article
Alternative Title : PLoS Pathog.

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PLOS_Pathogens_2011_7_e1002283.pdf (Publisher version), 5MB
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Copyright: © 2011 Christian 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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 Creators:
Christian, Jan G., Author
Heymann, Julia1, Author              
Paschen, Stefan A., Author
Vier, Juliane, Author
Schauenburg, Linda, Author
Rupp, Jan, Author
Meyer, Thomas F.1, Author              
Häcker, Georg, Author
Heuer, Dagmar1, Author              
Affiliations:
1Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664147              

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 Abstract: Chlamydiae are obligate intracellular bacteria that propagate in a cytosolic vacuole. Recent work has shown that growth of Chlamydia induces the fragmentation of the Golgi apparatus (GA) into ministacks, which facilitates the acquisition of host lipids into the growing inclusion. GA fragmentation results from infection-associated cleavage of the integral GA protein, golgin-84. Golgin-84-cleavage, GA fragmentation and growth of Chlamydia trachomatis can be blocked by the peptide inhibitor WEHD-fmk. Here we identify the bacterial protease chlamydial protease-like activity factor (CPAF) as the factor mediating cleavage of golgin-84 and as the target of WEHD-fmk-inhibition. WEHD-fmk blocked cleavage of golgin-84 as well as cleavage of known CPAF targets during infection with C. trachomatis and C. pneumoniae. The same effect was seen when active CPAF was expressed in non-infected cells and in a cell-free system. Ectopic expression of active CPAF in noninfected cells was sufficient for GA fragmentation. GA fragmentation required the small GTPases Rab6 and Rab11 downstream of CPAF-activity. These results define CPAF as the first protein that is essential for replication of Chlamydia. We suggest that this role makes CPAF a potential anti-infective therapeutic target.

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Language(s): eng - English
 Dates: 2011-09
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 574265
ISI: 000295409000075
DOI: 10.1371/journal.ppat.1002283
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Title: PLoS Pathogens
  Alternative Title : PLoS Pathog.
Source Genre: Journal
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Publ. Info: SAN FRANCISCO : PUBLIC LIBRARY SCIENCE
Pages: - Volume / Issue: 7 (9) Sequence Number: e1002283 Start / End Page: - Identifier: ISSN: 1553-7366