ArticleFrontiers in microbiology2011
Chlamydia Pneumoniae CdsL Regulates CdsN ATPase Activity, and Disruption with a Peptide Mimetic Prevents Bacterial Invasion.
Article in Frontiers in microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Differential regulation ofFrontiers in cellular and infection microbiology · 2023Article
- Peptidomimetics as Potential Anti-Virulence Drugs Against Resistant Bacterial Pathogens.Frontiers in microbiology · 2022Review
- CRISPR Interference To Inducibly Repress Gene Expression in Chlamydia trachomatis.Infection and immunity · 2021Article
- Molecular Targets and Strategies for Inhibition of the Bacterial Type III Secretion System (T3SS); Inhibitors Directly Binding to T3SS Components.Biomolecules · 2021Review
- Antibodies Inhibiting the Type III Secretion System of Gram-Negative Pathogenic Bacteria.Antibodies (Basel, Switzerland) · 2020Review
- Novel Noncompetitive Type Three Secretion System ATPase Inhibitors Shut DownBiochemistry · 2020Article
- The SPLUNC1-βENaC complex prevents Burkholderia cenocepacia invasion in normal airway epithelia.Respiratory research · 2020Article
- Peptide mimetics of immunoglobulin A (IgA) and FcαRI block IgA-induced human neutrophil activation and migration.European journal of immunology · 2017Article
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
- Hypothetical protein CT398 (CdsZ) interacts with σ(54) (RpoN)-holoenzyme and the type III secretion export apparatus in Chlamydia trachomatis.Protein science : a publication of the Protein Society · 2015Article
- The bacterial type III secretion system as a target for developing new antibiotics.Chemical biology & drug design · 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
- Functional characterization of the type III secretion ATPase SsaN encoded by Salmonella pathogenicity island 2.PloS one · 2014Article
- Modulation of host signaling and cellular responses by Chlamydia.Cell communication and signaling : CCS · 2013Review
- Article
- Structural characterization of a novel Chlamydia pneumoniae type III secretion-associated protein, Cpn0803.PloS one · 2012Article
- The obligate intracellular lifestyle.Frontiers in microbiology · 2011Article
Corrections and comments
- Erratum issuedCorrigendum:2021
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chlamydiae are obligate intracellular pathogens that likely require type III secretion (T3S) to invade cells and replicate intracellularly within a cytoplasmic vacuole called an inclusion body. Chlamydia pneumoniae possess a YscL ortholog, CdsL, that has been shown to interact with the T3S ATPase (CdsN). In this report we demonstrate that CdsL down-regulates CdsN enzymatic activity in a dose-dependent manner. Using Pepscan epitope mapping we identified two separate binding domains to which CdsL binds viz. CdsN(221-229) and CdsN(265-270). We confirmed the binding domains using a pull-down assay and showed that GST-CdsN(221-270), which encompasses these peptides, co-purified with His-CdsL. Next, we used orthology modeling based on the crystal structure of a T3S ATPase ortholog from Escherichia coli, EscN, to map the binding domains on the predicted 3D structure of CdsN. The CdsL binding domains mapped to the catalytic domain of the ATPase, one in the central channel of the ATPase hexamer and one on the outer face. Since peptide mimetics have been used to disrupt essential protein interactions of the chlamydial T3S system and inhibit T3S-mediated invasion of HeLa cells, we hypothesized that if CdsL-CdsN binding is essential for regulating T3S then a CdsN peptide mimetic could be used to potentially block T3S and chlamydial invasion. Treatment of elementary body with a CdsN peptide mimetic inhibited C. pneumoniae invasion into HeLa cells in a dose-dependent fashion. This report represents the first use of Pepscan technology to identify binding domains for specific T3S proteins viz. CdsL on the ATPase, CdsN, and demonstrates that peptide mimetics can be used as anti-virulence factors to block bacterial invasion.
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