ArticleInfection and immunity2004
The serine protease motif of EspC from enteropathogenic Escherichia coli produces epithelial damage by a mechanism different from that of Pet toxin from enteroaggregative E. coli.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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
37 citing papers in PubMed, 74 citations in OpenAlex.
- Trial
- The crystal structure of the toxin EspC from enteropathogenicGut microbes · 2025Article
- Repurposing of Furin Inhibitors to Reduce PathogenicAntibiotics (Basel, Switzerland) · 2025Article
- Predisposition factors and control strategies of avian pathogenicFrontiers in veterinary science · 2024Review
- Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function.Nature communications · 2023Article
- IgG BindsFrontiers in immunology · 2022Article
- Serine Protease Autotransporters of theMicroorganisms · 2019Review
- Blowing epithelial cell bubbles with GumB: ShlA-family pore-forming toxins induce blebbing and rapid cellular death in corneal epithelial cells.PLoS pathogens · 2019Article
- Curcumin Blocks Cytotoxicity of Enteroaggregative and EnteropathogenicFrontiers in cellular and infection microbiology · 2019Article
- Intestinal cell migration damage induced by enteropathogenic Escherichia coli strains.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2018Article
- Article
- Article
- Molecular Characterization of the Vacuolating Autotransporter Toxin in Uropathogenic Escherichia coli.Journal of bacteriology · 2016Article
- Determinants of Proteolysis and Cell-Binding for the Shigella flexneri Cytotoxin, SigA.Current microbiology · 2015Article
- The Serine Protease EspC from Enteropathogenic Escherichia coli Regulates Pore Formation and Cytotoxicity Mediated by the Type III Secretion System.PLoS pathogens · 2015Article
- Genome sequences of the Shiga-like toxin-producing Escherichia coli NCCP15655 and NCCP15656.Gut pathogens · 2015Article
- RNA-Seq analysis of isolate- and growth phase-specific differences in the global transcriptomes of enteropathogenic Escherichia coli prototype isolates.Frontiers in microbiology · 2015Article
- Cytochalasin E alters the cytoskeleton and decreases ENaC activity in Xenopus 2F3 cells.American journal of physiology. Renal physiology · 2014Article
- EspC promotes epithelial cell detachment by enteropathogenic Escherichia coli via sequential cleavages of a cytoskeletal protein and then focal adhesion proteins.Infection and immunity · 2014Article
- Role of class 1 serine protease autotransporter in the pathogenesis of Citrobacter rodentium colitis.Infection and immunity · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
EspC (Escherichia coli secreted protein C) of enteropathogenic E. coli (EPEC) shows the three classical domains of the autotransporter proteins and has a conserved serine protease motif belonging to the SPATE (serine protease autotransporters of Enterobacteriaceae) subfamily. EspC and its homolog Pet in enteroaggregative E. coli (EAEC) bear the same sequence within the serine protease motif, and both proteins produce enterotoxic effects, suggesting that like Pet, EspC could be internalized to reach and cleave the calmodulin-binding domain of fodrin, causing actin cytoskeleton disruption. Even though both proteins cause cytoskeleton damage by virtue of their serine protease motifs, the following evidence supports the hypothesis that the mechanisms are different. (i) To obtain similar cytotoxic and cytoskeletal effects, a threefold-higher EspC concentration and a twofold-higher exposure time are needed. (ii) EspC internalization into epithelial cells takes more time (6 h) than Pet internalization (30 min), and the distributions of the two proteins inside the cells are also different. (iii) Both proteins have affinity for fodrin and cleave it, but the cleavage sites are different; EspC produces two cleavages, while Pet produces just one. (iv) EspC does not cause fodrin redistribution within epithelial cells. (v) An EspC serine protease motif mutant, but not a Pet serine protease mutant, competes with EspC by blocking cytoskeletal damage. All these data suggest that the protein conformational structure is very important for the activity of the catalytic site, influencing its interaction with the target protein and its internalization. The differences between these proteins may explain the reduced ability of EspC to cause cytopathic effects. However, these differences may confer a specialized role on EspC in the pathogenesis of EPEC, which is different from that of Pet in EAEC pathogenesis.
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.