ArticleJournal of bacteriology2008
Interactions between CdsD, CdsQ, and CdsL, three putative Chlamydophila pneumoniae type III secretion proteins.
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 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Emerging Insights into Protein Post-Translational Modifications in Chlamydia-Host Interactions.The American journal of pathology · 2025Review
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- The YscE/YscG chaperone and YscF N-terminal sequences target YscF to the Yersinia pestis type III secretion apparatus.Microbiology (Reading, England) · 2018Article
- The extended structure of the periplasmic region of CdsD, a structural protein of the type III secretion system of Chlamydia trachomatis.Protein science : a publication of the Protein Society · 2016Article
- Characterisation of Shigella Spa33 and Thermotoga FliM/N reveals a new model for C-ring assembly in T3SS.Molecular microbiology · 2016Article
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- New frontiers in type III secretion biology: the Chlamydia perspective.Infection and immunity · 2014Review
- 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
- Structure of the cytoplasmic domain of Yersinia pestis YscD, an essential component of the type III secretion system.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Two translation products of Yersinia yscQ assemble to form a complex essential to type III secretion.Biochemistry · 2012Article
- Structural characterization of a novel Chlamydia pneumoniae type III secretion-associated protein, Cpn0803.PloS one · 2012Article
- HrcQ provides a docking site for early and late type III secretion substrates from Xanthomonas.PloS one · 2012Article
- Quantitative proteomics reveals metabolic and pathogenic properties of Chlamydia trachomatis developmental forms.Molecular microbiology · 2011Article
- Quantitative proteomic analysis reveals formation of an EscL-EscQ-EscN type III complex in enteropathogenic Escherichia coli.Journal of bacteriology · 2011Article
- A C-terminal region of Yersinia pestis YscD binds the outer membrane secretin YscC.Journal of bacteriology · 2011Article
- Chlamydia Pneumoniae CdsL Regulates CdsN ATPase Activity, and Disruption with a Peptide Mimetic Prevents Bacterial Invasion.Frontiers in microbiology · 2011Article
- Interactions between flagellar and type III secretion proteins in Chlamydia pneumoniae.BMC microbiology · 2010Article
- The Chlamydial Type III Secretion Mechanism: Revealing Cracks in a Tough Nut.Frontiers in microbiology · 2010Article
- Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis.The Journal of biological chemistry · 2009Article
- The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex.PLoS pathogens · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chlamydophila pneumoniae is a gram-negative obligate intracellular bacterial pathogen that causes pneumonia and bronchitis and may contribute to atherosclerosis. The developmental cycle of C. pneumoniae includes a morphological transition from an infectious extracellular elementary body (EB) to a noninfectious intracellular reticulate body (RB) that divides by binary fission. The C. pneumoniae genome encodes a type III secretion (T3S) apparatus that may be used to infect eukaryotic cells and to evade the host immune response. In the present study, Cpn0712 (CdsD), Cpn0704 (CdsQ), and Cpn0826 (CdsL), three C. pneumoniae genes encoding yersiniae T3S YscD, YscQ, and YscL homologs, respectively, were cloned and expressed as histidine- and glutathione S-transferase (GST)-tagged proteins in Escherichia coli. Purified recombinant proteins were used to raise hyper-immune polyclonal antiserum and were used in GST pull-down and copurification assays to identify protein-protein interactions. CdsD was detected in both EB and RB lysates by Western blot analyses, and immunofluorescent staining demonstrated the presence of CdsD within inclusions. Triton X-114 solubilization and phase separation of chlamydial EB proteins indicated that CdsD partitions with cytoplasmic proteins, suggesting it is not an integral membrane protein. GST pull-down assays indicated that recombinant CdsD interacts with CdsQ and CdsL, and copurification assays with chlamydial lysates confirmed that native CdsD interacts with CdsQ and CdsL. To the best of our knowledge, this is the first report demonstrating interactions between YscD, YscQ, and YscL homologs of bacterial T3S systems. These novel protein interactions may play important roles in the assembly or function of the chlamydial T3S apparatus.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.