ArticleJournal of bacteriology2008
Characterization of the putative type III secretion ATPase CdsN (Cpn0707) of Chlamydophila pneumoniae.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Complete Genome Sequencing ofPathogens (Basel, Switzerland) · 2021Article
- Dominant negative effects by inactive Spa47 mutants inhibit T3SS function and Shigella virulence.PloS one · 2020Article
- Interfacial amino acids support Spa47 oligomerization and shigella type three secretion system activation.Proteins · 2019Article
- Novel insights into the mechanism of SepL-mediated control of effector secretion in enteropathogenic Escherichia coli.MicrobiologyOpen · 2018Article
- MxiN Differentially Regulates Monomeric and Oligomeric Species of the Shigella Type Three Secretion System ATPase Spa47.Biochemistry · 2018Article
- Structural and Biochemical Characterization of Spa47 Provides Mechanistic Insight into Type III Secretion System ATPase Activation and Shigella Virulence Regulation.The Journal of biological chemistry · 2016Article
- Spa47 is an oligomerization-activated type three secretion system (T3SS) ATPase from Shigella flexneri.Protein science : a publication of the Protein Society · 2016Article
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- Escherichia coli Type III Secretion System 2 ATPase EivC Is Involved in the Motility and Virulence of Avian Pathogenic Escherichia coli.Frontiers in microbiology · 2016Article
- Chlamydia psittaci comparative genomics reveals intraspecies variations in the putative outer membrane and type III secretion system genes.Microbiology (Reading, England) · 2015Article
- Recombinant Cpn 0810 stimulates proinflammatory cytokine expression and apoptosis in human monocytes.Experimental and therapeutic medicine · 2015Article
- Identification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo.The Journal of biological chemistry · 2014Article
- EscO, a functional and structural analog of the flagellar FliJ protein, is a positive regulator of EscN ATPase activity of the enteropathogenic Escherichia coli injectisome.Journal of bacteriology · 2014Article
- Chlamydia pneumoniae CopD translocator protein plays a critical role in type III secretion (T3S) and infection.PloS one · 2014Article
- Functional characterization of the type III secretion ATPase SsaN encoded by Salmonella pathogenicity island 2.PloS one · 2014Article
- The Yersinia pestis type III secretion system: expression, assembly and role in the evasion of host defenses.Immunologic research · 2013Review
- Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Microbiology and molecular biology reviews : MMBR · 2012Review
- Structural characterization of a novel Chlamydia pneumoniae type III secretion-associated protein, Cpn0803.PloS one · 2012Article
- Quantitative proteomics reveals metabolic and pathogenic properties of Chlamydia trachomatis developmental forms.Molecular microbiology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type III secretion (T3S) is utilized by a wide range of gram-negative bacterial pathogens to allow the efficient delivery of effector proteins into the host cell cytoplasm through the use of a syringe-like injectisome. Chlamydophila pneumoniae is a gram-negative, obligate intracellular pathogen that has the structural genes coding for a T3S system, but the functionality of the system has not yet been demonstrated. T3S is dependent on ATPase activity, which catalyzes the unfolding of proteins and the secretion of effector proteins through the injectisome. CdsN (Cpn0707) is predicted to be the T3S ATPase of C. pneumoniae based on sequence similarity to other T3S ATPases. Full-length CdsN and a C-terminal truncation of CdsN were cloned as glutathione S-transferase (GST)-tagged constructs and expressed in Escherichia coli. The GST-tagged C-terminal truncation of CdsN possessed ATPase activity, catalyzing the release of ADP and P(i) from ATP at a rate of 0.55 +/- 0.07 micromol min(-1) mg(-1) in a time- and dose-dependent manner. CdsN formed oligomers and high-molecular-weight multimers, as assessed by formaldehyde fixation and nondenaturing polyacrylamide gel electrophoresis. Using bacterial two-hybrid and GST pull-down assays, CdsN was shown to interact with CdsD, CdsL, CdsQ, and CopN, four putative structural components of the C. pneumoniae T3S system. CdsN also interacted with an unannotated protein, Cpn0706, a putative CdsN chaperone. Interactions between CdsN, CdsD, and CopN represent novel interactions not previously reported for other bacterial T3S systems and may be important in the localization and/or function of the ATPase at the inner membrane of C. pneumoniae.
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