ArticlePLoS pathogens2009
The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex.
Article in PLoS pathogens, 2009. 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 70 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
70 citing papers in PubMed, 98 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Inclusion Membrane Proteins ofMicroorganisms · 2026Review
- ThemBio · 2026Article
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- Effect of tryptophan starvation on inclusion membrane composition and chlamydial-host interactions.Infection and immunity · 2025Article
- Article
- Cytosolic sorting platform complexes shuttle type III secretion system effectors to the injectisome in Yersinia enterocolitica.Nature microbiology · 2024Article
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- ThemBio · 2023Article
- Chlamydia trachomatis Alters Mitochondrial Protein Composition and Secretes Effector Proteins That Target Mitochondria.mSphere · 2022Article
- Regulation of T3SS synthesis, assembly and secretion in Pseudomonas aeruginosa.Archives of microbiology · 2022Article
- Recognition of a translocation motif in the regulator HpaA fromFrontiers in plant science · 2022Article
- A Dynamic, Ring-Forming Bactofilin Critical for Maintaining Cell Size in the Obligate Intracellular Bacterium Chlamydia trachomatis.Infection and immunity · 2021Article
- The T3SS Effector Protease NleC Is Active withinPathogens (Basel, Switzerland) · 2021Article
- Robust Heat Shock Response inFrontiers in microbiology · 2021Article
- Chain-Selective Isotopic Labeling of the Heterodimeric Type III Secretion Chaperone, Scc4:Scc1, Reveals the Total Structural Rearrangement of theBiomolecules · 2020Article
- Backbone and sidechain resonance assignments and secondary structure of Scc4 from Chlamydia trachomatis.Biomolecular NMR assignments · 2020Article
- Article
- Multiple proteins arising from a single gene: The role of the Spa33 variants in Shigella T3SS regulation.MicrobiologyOpen · 2019Article
- Purification of Tag-FreeBiochemistry · 2019Article
10 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In Gram-negative bacterial pathogens, specialized chaperones bind to secreted effector proteins and maintain them in a partially unfolded form competent for translocation by type III secretion systems/injectisomes. How diverse sets of effector-chaperone complexes are recognized by injectisomes is unclear. Here we describe a new mechanism of effector-chaperone recognition by the Chlamydia injectisome, a unique and ancestral line of these evolutionarily conserved secretion systems. By yeast two-hybrid analysis we identified networks of Chlamydia-specific proteins that interacted with the basal structure of the injectisome, including two hubs of protein-protein interactions that linked known secreted effector proteins to CdsQ, the putative cytoplasmic C-ring component of the secretion apparatus. One of these protein-interaction hubs is defined by Ct260/Mcsc (Multiple cargo secretion chaperone). Mcsc binds to and stabilizes at least two secreted hydrophobic proteins, Cap1 and Ct618, that localize to the membrane of the pathogenic vacuole ("inclusion"). The resulting complexes bind to CdsQ, suggesting that in Chlamydia, the C-ring of the injectisome mediates the recognition of a subset of inclusion membrane proteins in complex with their chaperone. The selective recognition of inclusion membrane proteins by chaperones may provide a mechanism to co-ordinate the translocation of subsets of inclusion membrane proteins at different stages in infection.
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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.