ArticleEnvironmental microbiology2011
Enterohaemorrhagic Escherichia coli haemolysin is cleaved and inactivated by serine protease EspPα.
Article in Environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Substrate secretion by different EHEC secretion systems during their interaction with epithelial cells.Virulence · 2026Article
- Microbial proteases and endothelial barrier disruption in sepsis: A neglected nexus.Virulence · 2026Review
- IgG BindsFrontiers in immunology · 2022Article
- Serine Protease Autotransporters of theMicroorganisms · 2019Review
- Bacterial Control of Pores Induced by the Type III Secretion System: Mind the Gap.Frontiers in immunology · 2016Review
- Article
- The Serine Protease EspC from Enteropathogenic Escherichia coli Regulates Pore Formation and Cytotoxicity Mediated by the Type III Secretion System.PLoS pathogens · 2015Article
- Characterization of urinary tract infection-associated Shiga toxin-producing Escherichia coli.Infection and immunity · 2014Article
- Article
- Article
- Recent advances in understanding enteric pathogenic Escherichia coli.Clinical microbiology reviews · 2013Review
- Facing glycosphingolipid-Shiga toxin interaction: dire straits for endothelial cells of the human vasculature.Cellular and molecular life sciences : CMLS · 2013Review
- Review
- Crystal structure of the passenger domain of the Escherichia coli autotransporter EspP.Journal of molecular biology · 2011Article
- EHEC Adhesins.Microbiology spectrumArticle
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The haemolysin from enterohaemorrhagic Escherichia coli (EHEC-Hly) and the serine protease EspPα are putative virulence factors of EHEC. We investigated the interplay between these secreted factors and demonstrate that EspPα cleaves the 107 kDa large EHEC-Hly. Degradation was observed when purified EspPα was added to a growing culture of an EHEC-Hly-expressing strain, with isolated proteins and with coexpressing strains, and was independent of the EHEC serotype. EHEC-Hly breakdown occurred as a multistage process with the formation of characteristic fragments with relative molecular masses of ~82 kDa and/or ~84 kDa and ~34 kDa. The initial cleavage occurred in the N-terminal hydrophobic domain of EHEC-Hly between Leu(235) and Ser(236) and abolished its haemolytic activity. In a cellular infection system, the cytolytic potential of EHEC-Hly-secreting recombinant strains was abolished when EspPα was coexpressed. EHEC in contact with human intestinal epithelial cells simultaneously upregulated their EHEC-Hly and EspP indicating that both molecules might interact under physiological conditions. We propose the concept of bacterial effector molecule interference (BEMI), reflecting the concerted interplay of virulence factors. Interference between effector molecules might be an additional way to regulate virulence functions and increases the complexity of monomolecular phenotypes.
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