ArticlePloS one2013
Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 47 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
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- ThebioRxiv : the preprint server for biology · 2025Article
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- Effect of tryptophan starvation on inclusion membrane composition and chlamydial-host interactions.Infection and immunity · 2025Article
- Insights into Chlamydia Development and Host Cells Response.Microorganisms · 2024Review
- Bacterial One- and Two-Hybrid Assays to Monitor Transmembrane Helix Interactions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- In Search of a Mechanistic Link between Chlamydia trachomatis-Induced Cellular Pathophysiology and Oncogenesis.Infection and immunity · 2023Review
- Article
- Got mutants? How advances in chlamydial genetics have furthered the study of effector proteins.Pathogens and disease · 2021Review
- A predation assay using amoebae to screen for virulence factors unearthed the first W. chondrophila inclusion membrane protein.Scientific reports · 2019Article
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
- CteG is a Chlamydia trachomatis effector protein that associates with the Golgi complex of infected host cells.Scientific reports · 2019Article
- Chlamydial Infection From Outside to Inside.Frontiers in microbiology · 2019Review
- Article
- Regulation of Effector Delivery by Type III Secretion Chaperone Proteins inFrontiers in microbiology · 2018Article
- Subversion of the Endocytic and Secretory Pathways by Bacterial Effector Proteins.Frontiers in cell and developmental biology · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chlamydia trachomatis is an obligate intracellular bacterial pathogen of humans that uses a type III secretion (T3S) system to manipulate host cells through the delivery of effector proteins into their cytosol and membranes. The function of T3S systems depends on small bacterial cytosolic chaperone-like proteins, which bind T3S substrates and ensure their appropriate secretion. To find novel T3S chaperone-substrate complexes of C. trachomatis we first searched its genome for genes encoding proteins with features of T3S chaperones. We then systematically tested for interactions between candidate chaperones and chlamydial T3S substrates by bacterial two-hybrid. This revealed interactions between Slc1 (a known T3S chaperone) or CT584 and several T3S substrates. Co-immunoprecipitation after protein expression in Yersinia enterocolitica and protein overlay binding assays indicated that Slc1 interacted with the N-terminal region of the known T3S substrates Tarp (a previously described substrate of Slc1), CT694, and CT695, and that CT584 interacted with a central region of CT082, which we identified as a C. trachomatis T3S substrate using Y. enterocolitica as a heterologous system. Further T3S assays in Yersinia indicated that Slc1 or CT584 increased the amount of secreted Tarp, CT694, and CT695, or CT082, respectively. Expression of CT584 increased the intra-bacterial stability of CT082, while Slc1 did not affect the stability of its substrates. Overall, this indicated that in C. trachomatis Slc1 is a chaperone of multiple T3S substrates and that CT584 is a chaperone of the newly identified T3S substrate CT082.
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