ArticleMedical microbiology and immunology2004
Expression and localization of type III secretion-related proteins of Chlamydia pneumoniae.
Article in Medical microbiology and immunology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 47 citations in OpenAlex.
- Robust Heat Shock Response inFrontiers in microbiology · 2021Article
- Insight into microtubule nucleation from tubulin-capping proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Recombinant Cpn 0810 stimulates proinflammatory cytokine expression and apoptosis in human monocytes.Experimental and therapeutic medicine · 2015Article
- Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae.The Journal of biological chemistry · 2014Article
- Electron tomography and cryo-SEM characterization reveals novel ultrastructural features of host-parasite interaction during Chlamydia abortus infection.Histochemistry and cell biology · 2014Article
- Genus-optimized strategy for the identification of chlamydial type III secretion substrates.Pathogens and disease · 2013Article
- Article
- Biochemical and localization analyses of putative type III secretion translocator proteins CopB and CopB2 of Chlamydia trachomatis reveal significant distinctions.Infection and immunity · 2011Article
- Analysis of Chlamydia pneumoniae infection in mononuclear cells by reverse transcription-PCR targeted to chlamydial gene transcripts.Medical microbiology and immunology · 2011Article
- The Chlamydial Type III Secretion Mechanism: Revealing Cracks in a Tough Nut.Frontiers in microbiology · 2010Article
- Accurate prediction of secreted substrates and identification of a conserved putative secretion signal for type III secretion systems.PLoS pathogens · 2009Article
- Characterization and intracellular localization of putative Chlamydia pneumoniae effector proteins.Medical microbiology and immunology · 2008Article
- Article
- Chlamydial effector proteins localized to the host cell cytoplasmic compartment.Infection and immunity · 2008Article
- Characterization of the putative type III secretion ATPase CdsN (Cpn0707) of Chlamydophila pneumoniae.Journal of bacteriology · 2008Article
- Interactions between CdsD, CdsQ, and CdsL, three putative Chlamydophila pneumoniae type III secretion proteins.Journal of bacteriology · 2008Article
- Type III secretion systems and disease.Clinical microbiology reviews · 2007Review
- Induction of type III secretion by cell-free Chlamydia trachomatis elementary bodies.Microbial pathogenesisArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The entire developmental cycle of the obligate intracellular bacteria Chlamydia pneumoniae takes place within the inclusion body. As many gram negative bacteria, Chlamydia possess a type III-secretion system (TTSS), which allows them to target effector molecules into the host cell. The expression and localization of several proteins constituting the TTSS apparatus and of proteins supposed to be secreted by the TTSS have been investigated. For the TTSS-constituting proteins, we selected representatives such as YscN (ATPase), LcrE (putative "lid" of the TTSS) and LcrH1 (postulated to be a chaperone). Furthermore, we focused on the putative effector proteins IncA, IncB, IncC, Cpn0809 and Cpn1020. Expression of these proteins was detected by reverse transcriptase-PCR followed by immunoblot analysis using antisera that were generated against the corresponding recombinant proteins. Thereby, expression could be detected on the RNA and/or protein level. Intracellular localization of proteins under investigation was determined by immunofluorescence assays using the respective antisera. YscN was shown to be distributed equally throughout the inclusion body, whereas LcrE gave a more prominent staining of the inclusion membrane. IncA was detected mainly on the membrane of the inclusion body, whereas IncB and IncC were shown to be located within the inclusion. Immunofluorescence assays with antisera raised against Cpn0809 and Cpn1020 showed completely different labeling. Signals corresponding to Cpn0809 and Cpn1020 were distributed within the host cell rather than inside the inclusions. Taken together, the different localization patterns of the effector proteins indicate differences in function and interplay with the host cell.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.