ArticleApplied and environmental microbiology2007
Subtypes of the plasmid-encoded serine protease EspP in Shiga toxin-producing Escherichia coli: distribution, secretion, and proteolytic activity.
Article in Applied and environmental microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 58 citations in OpenAlex.
- Bacterial serine protease EspP induces differentiation and expansion of enteroendocrine cells in human colonoids.Physiological genomics · 2026Article
- AnMicrobiology spectrum · 2026Article
- Comparative genomics of Shiga toxin-producingFrontiers in veterinary science · 2025Article
- Prevalence and Characteristics of Plasmid-Encoded Serine Protease EspP in Clinical Shiga Toxin-ProducingMicroorganisms · 2024Article
- IgG BindsFrontiers in immunology · 2022Article
- Serine Protease Autotransporters of theMicroorganisms · 2019Review
- EnterohemorrhagicToxins · 2018Article
- Host cell interactions of outer membrane vesicle-associated virulence factors of enterohemorrhagic Escherichia coli O157: Intracellular delivery, trafficking and mechanisms of cell injury.PLoS pathogens · 2017Article
- Variation in the Distribution of Putative Virulence and Colonization Factors in Shiga Toxin-ProducingFrontiers in cellular and infection microbiology · 2017Article
- Plasmids from Shiga Toxin-Producing Escherichia coli Strains with Rare Enterohemolysin Gene (ehxA) Subtypes Reveal Pathogenicity Potential and Display a Novel Evolutionary Path.Applied and environmental microbiology · 2016Article
- EnterohemorrhagicCellular and molecular gastroenterology and hepatology · 2016Article
- Article
- Characterization of urinary tract infection-associated Shiga toxin-producing Escherichia coli.Infection and immunity · 2014Article
- Article
- Heteropathogenic virulence and phylogeny reveal phased pathogenic metamorphosis in Escherichia coli O2:H6.EMBO molecular medicine · 2014Article
- Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence.Cellular and molecular life sciences : CMLS · 2014Review
- Article
- Comparative proteomic analysis of the membrane proteins of two Haemophilus parasuis strains to identify proteins that may help in habitat adaptation and pathogenesis.Proteome science · 2014Article
- Recent advances in understanding enteric pathogenic Escherichia coli.Clinical microbiology reviews · 2013Review
- Enterohemorrhagic Escherichia coli as causes of hemolytic uremic syndrome in the Czech Republic.PloS one · 2013Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We investigated the prevalence, distribution, and structure of espP in Shiga toxin-producing Escherichia coli (STEC) and assessed the secretion and proteolytic activity of the encoded autotransporter protein EspP (extracellular serine protease, plasmid encoded). espP was identified in 56 of 107 different STEC serotypes. Sequencing of a 3,747-bp region of the 3,900-bp espP gene distinguished four alleles (espPalpha, espPbeta, espPgamma, and espPdelta), with 99.9%, 99.2%, 95.3%, and 95.1% homology, respectively, to espP of E. coli O157:H7 strain EDL933. The espPbeta, espPgamma, and espPdelta genes contained unique insertions and/or clustered point mutations that enabled allele-specific PCRs; these demonstrated the presence of espPalpha, espPbeta, espPgamma, and espPdelta in STEC isolates belonging to 17, 16, 15, and 8 serotypes, respectively. Among four subtypes of EspP encoded by these alleles, EspPalpha (produced by enterohemorrhagic E. coli [EHEC] O157:H7 and the major non-O157 EHEC serotypes) and EspPgamma cleaved pepsin A, human coagulation factor V, and an oligopeptide alanine-alanine-proline-leucine-para-nitroaniline, whereas EspPbeta and EspPdelta either were not secreted or were proteolytically inactive. The lack of proteolysis correlated with point mutations near the active serine protease site. We conclude that espP is widely distributed among STEC strains and displays genetic heterogeneity, which can be used for subtyping and which affects EspP activity. The presence of proteolytically active EspP in EHEC serogroups O157, O26, O111, and O145, which are bona fide human pathogens, suggests that EspP might play a role as an EHEC virulence factor.
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