ArticleMicrobiologyOpen2018
Novel insights into the mechanism of SepL-mediated control of effector secretion in enteropathogenic Escherichia coli.
Article in MicrobiologyOpen, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Oligomeric assembly of the gatekeeper InvE orchestrates hierarchical type III protein secretion inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Calcium controls type III secretion switch through an SctV-SctW interplay.Frontiers in microbiology · 2026Article
- On the role of the sorting platform in hierarchical type III secretion regulation in enteropathogenicJournal of bacteriology · 2025Article
- Morphogenetic penicillin-binding proteins control virulence-associated type III secretion systems inInfection and immunity · 2025Article
- Article
- BopN is a Gatekeeper of theMicrobiology spectrum · 2023Article
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- The Transcription of Flagella of EnteropathogenicMicroorganisms · 2022Article
- Structural and Functional Analysis of SsaV Cytoplasmic Domain and Variable Linker States in the Context of the InvA-SsaV Chimeric Protein.Microbiology spectrum · 2021Article
- Structure of the cytoplasmic domain of SctV (SsaV) from the Salmonella SPI-2 injectisome and implications for a pH sensing mechanism.Journal of structural biology · 2021Article
- CesL Regulates Type III Secretion Substrate Specificity of the EnteropathogenicMicroorganisms · 2021Article
- The Role of the Membrane-Associated Domain of the Export Apparatus Protein, EscV (SctV), in the Activity of the Type III Secretion System.Frontiers in microbiology · 2021Article
- The PopN Gate-keeper Complex Acts on the ATPase PscN to Regulate the T3SS Secretion Switch from Early to Middle Substrates in Pseudomonas aeruginosa.Journal of molecular biology · 2020Article
- A Reporter System for Fast Quantitative Monitoring of Type 3 Protein Secretion in EnteropathogenicMicroorganisms · 2020Article
- Plant Aquaporins in Infection by and Immunity Against Pathogens - A Critical Review.Frontiers in plant science · 2019Article
- Article
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
- Novel insights into the mechanism of SepL-mediated control of effector secretion in enteropathogenic Escherichia coli.MicrobiologyOpen · 2018Article
- Environment Controls LEE Regulation in EnteropathogenicFrontiers in microbiology · 2018Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type three secretion systems (T3SSs) are virulence determinants employed by several pathogenic bacteria as molecular syringes to inject effector proteins into host cells. Diarrhea-producing enteropathogenic Escherichia coli (EPEC) uses a T3SS to colonize the intestinal tract. T3S is a highly coordinated process that ensures hierarchical delivery of three classes of substrates: early (inner rod and needle subunits), middle (translocators), and late (effectors). Translocation of effectors is triggered upon host-cell contact in response to different environmental cues, such as calcium levels. The T3S substrate specificity switch from middle to late substrates in EPEC is regulated by the SepL and SepD proteins, which interact with each other and form a trimeric complex with the chaperone CesL. In this study, we investigated the link between calcium concentration and secretion regulation by the gatekeeper SepL. We found that calcium depletion promotes late substrate secretion in a translocon-independent manner. Furthermore, the stability, formation, and subcellular localization of the SepL/SepD/CesL regulatory complex were not affected by the absence of calcium. In addition, we demonstrate that SepL interacts in a calcium-independent manner with the major export gate component EscV, which in turn interacts with both middle and late secretion substrates, providing a docking site for T3S. These results suggest that EscV serves as a binding platform for both the SepL regulatory protein and secreted substrates during the ordered assembly of the T3SS.
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