The Chlamydia protease CPAF regulates host and bacterial proteins to maintain pathogen vacuole integrity and promote virulence

The obligate intracellular bacterial pathogen Chlamydia trachomatis injects numerous effector proteins into the epithelial cell cytoplasm to manipulate host functions important for bacterial survival. In addition, the bacterium secretes a serine protease, chlamydial protease-like activity factor (CP...

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Published inCell host & microbe Vol. 10; no. 1; pp. 21 - 32
Main Authors Jorgensen, Ine, Bednar, Maria M, Amin, Vishar, Davis, Beckley K, Ting, Jenny P Y, McCafferty, Dewey G, Valdivia, Raphael H
Format Journal Article
LanguageEnglish
Published United States 21.07.2011
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Abstract The obligate intracellular bacterial pathogen Chlamydia trachomatis injects numerous effector proteins into the epithelial cell cytoplasm to manipulate host functions important for bacterial survival. In addition, the bacterium secretes a serine protease, chlamydial protease-like activity factor (CPAF). Although several CPAF targets are reported, the significance of CPAF-mediated proteolysis is unclear due to the lack of specific CPAF inhibitors and the diversity of host targets. We report that CPAF also targets chlamydial effectors secreted early during the establishment of the pathogen-containing vacuole ("inclusion"). We designed a cell-permeable CPAF-specific inhibitory peptide and used it to determine that CPAF prevents superinfection by degrading early Chlamydia effectors translocated during entry into a preinfected cell. Prolonged CPAF inhibition leads to loss of inclusion integrity and caspase-1-dependent death of infected epithelial cells. Thus, CPAF functions in niche protection, inclusion integrity and pathogen survival, making the development of CPAF-specific protease inhibitors an attractive antichlamydial therapeutic strategy.
AbstractList The obligate intracellular bacterial pathogen Chlamydia trachomatis injects numerous effector proteins into the epithelial cell cytoplasm to manipulate host functions important for bacterial survival. In addition, the bacterium secretes a serine protease, c hlamydial p rotease-like a ctivity f actor (CPAF). Although several CPAF targets are reported, the significance of CPAF-mediated proteolysis is unclear due to the lack of specific CPAF inhibitors and the diversity of host targets. We report that CPAF also targets chlamydial effectors secreted early during the establishment of the pathogen-containing vacuole (“inclusion”). We designed a cell-permeable CPAF-specific inhibitory peptide and used it to determine that CPAF prevents superinfection by degrading early Chlamydia effectors translocated during entry into a pre-infected cell. Prolonged CPAF inhibition leads to loss of inclusion integrity and caspase-1-dependent death of infected epithelial cells. Thus, CPAF functions in niche protection, inclusion integrity and pathogen survival, making the development of CPAF-specific protease inhibitors an attractive anti-chlamydial therapeutic strategy.
The obligate intracellular bacterial pathogen Chlamydia trachomatis injects numerous effector proteins into the epithelial cell cytoplasm to manipulate host functions important for bacterial survival. In addition, the bacterium secretes a serine protease, chlamydial protease-like activity factor (CPAF). Although several CPAF targets are reported, the significance of CPAF-mediated proteolysis is unclear due to the lack of specific CPAF inhibitors and the diversity of host targets. We report that CPAF also targets chlamydial effectors secreted early during the establishment of the pathogen-containing vacuole ("inclusion"). We designed a cell-permeable CPAF-specific inhibitory peptide and used it to determine that CPAF prevents superinfection by degrading early Chlamydia effectors translocated during entry into a preinfected cell. Prolonged CPAF inhibition leads to loss of inclusion integrity and caspase-1-dependent death of infected epithelial cells. Thus, CPAF functions in niche protection, inclusion integrity and pathogen survival, making the development of CPAF-specific protease inhibitors an attractive antichlamydial therapeutic strategy.
Author Amin, Vishar
Bednar, Maria M
Ting, Jenny P Y
Davis, Beckley K
Jorgensen, Ine
Valdivia, Raphael H
McCafferty, Dewey G
AuthorAffiliation 1 Department of Molecular Genetics and Microbiology, Duke University Medical Center at Chapel Hill
2 Department of Chemistry, Duke University at Chapel Hill
3 Center for Infectious Diseases, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill
AuthorAffiliation_xml – name: 1 Department of Molecular Genetics and Microbiology, Duke University Medical Center at Chapel Hill
– name: 2 Department of Chemistry, Duke University at Chapel Hill
– name: 3 Center for Infectious Diseases, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill
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Snippet The obligate intracellular bacterial pathogen Chlamydia trachomatis injects numerous effector proteins into the epithelial cell cytoplasm to manipulate host...
The obligate intracellular bacterial pathogen Chlamydia trachomatis injects numerous effector proteins into the epithelial cell cytoplasm to manipulate host...
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SubjectTerms Amino Acid Chloromethyl Ketones - pharmacology
Amino Acid Sequence
Animals
Antigens, Bacterial - metabolism
Bacterial Proteins - metabolism
Bacterial Secretion Systems
Caspase 1 - metabolism
Cell Death - physiology
Cell Membrane Permeability
Chlamydia trachomatis - metabolism
Chlamydia trachomatis - pathogenicity
Endopeptidases - metabolism
Epithelial Cells - microbiology
Host-Pathogen Interactions
Mice
Molecular Sequence Data
Peptides - metabolism
Protease Inhibitors - pharmacology
Protein Transport
Virulence Factors - metabolism
Title The Chlamydia protease CPAF regulates host and bacterial proteins to maintain pathogen vacuole integrity and promote virulence
URI https://www.ncbi.nlm.nih.gov/pubmed/21767809
https://pubmed.ncbi.nlm.nih.gov/PMC3147293
Volume 10
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