ArticleJournal of bacteriology2005
Interaction between components of the type III secretion system of Chlamydiaceae.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Work Patterns of MamXY Proteins during Magnetosome Formation inApplied and environmental microbiology · 2019Article
- Chlamydial Infection From Outside to Inside.Frontiers in microbiology · 2019Review
- Future of human Chlamydia vaccine: potential of self-adjuvanting biodegradable nanoparticles as safe vaccine delivery vehicles.Expert review of vaccines · 2018Review
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- Multipart Chaperone-Effector Recognition in the Type III Secretion System of Chlamydia trachomatis.The Journal of biological chemistry · 2015Article
- Chlamydia trachomatis Type III Secretion Proteins Regulate Transcription.Journal of bacteriology · 2015Article
- A gatekeeper chaperone complex directs translocator secretion during type three secretion.PLoS pathogens · 2014Article
- New frontiers in type III secretion biology: the Chlamydia perspective.Infection and immunity · 2014Review
- Structural characterization of a novel Chlamydia pneumoniae type III secretion-associated protein, Cpn0803.PloS one · 2012Article
- The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly.The Journal of biological chemistry · 2011Article
- Biochemical and localization analyses of putative type III secretion translocator proteins CopB and CopB2 of Chlamydia trachomatis reveal significant distinctions.Infection and immunity · 2011Article
- Scc1 (CP0432) and Scc4 (CP0033) function as a type III secretion chaperone for CopN of Chlamydia pneumoniae.Journal of bacteriology · 2011Article
- Chlamydia trachomatis secretion of hypothetical protein CT622 into host cell cytoplasm via a secretion pathway that can be inhibited by the type III secretion system inhibitor compound 1.Microbiology (Reading, England) · 2011Article
- The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex.PLoS pathogens · 2009Article
- Article
- Characterization and intracellular localization of putative Chlamydia pneumoniae effector proteins.Medical microbiology and immunology · 2008Article
- Interactions between CdsD, CdsQ, and CdsL, three putative Chlamydophila pneumoniae type III secretion proteins.Journal of bacteriology · 2008Article
- Bioinformatic and biochemical evidence for the identification of the type III secretion system needle protein of Chlamydia trachomatis.Journal of bacteriology · 2008Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the family Chlamydiaceae possess at least 13 genes, distributed throughout the chromosome, that are homologous with genes of known type III secretion systems (TTS). The aim of this study was to use putative TTS proteins of Chlamydophila pneumoniae, whose equivalents in other bacterial TTS function as chaperones, to identify interactions between chlamydial proteins. Using the BacterioMatch Two-Hybrid Vector system (Stratagene, La Jolla, Calif.), lcrH-2 and sycE, positions 1021 and 0325, respectively, from C. pneumoniae CM-1 were used as "bait" to identify target genes (positions 0324, 0705, 0708, 0808 to 0810, 1016 to 1020, and 1022) in close proximity on the chromosome. Interaction between the products of the lcrH-2 (1021) and lcrE (copN) (0324) genes was detected and confirmed by pull-down experiments and enzyme immunoassays using recombinant LcrH-2 and LcrE. As further confirmation of this interaction, the homologous genes from Chlamydia trachomatis, serovar E, and Chlamydophila psittaci, Texas turkey, were also cloned in the two-hybrid system to determine if LcrH-2 and LcrE would interact with their orthologs in other species. Consistent with their genetic relatedness, LcrH-2 from C. pneumoniae interacted with LcrE produced from the three species of Chlamydiaceae; LcrH-2 from C. psittaci reacted with LcrE from C. pneumoniae but not from C. trachomatis; and C. trachomatis LcrH-2 did not react with LcrE from the other two species. Deletions from the N and C termini of LcrE from C. pneumoniae identified the 50 C-terminal amino acids as essential for the interaction with LcrH-2. Thus, it appears that in the Chlamydiaceae TTS, LcrH-2 interacts with LcrE, and therefore it may serve as a chaperone for this protein.
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