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http://purl.uniprot.org/citations/12123444http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12123444http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12123444http://www.w3.org/2000/01/rdf-schema#comment"Escherichia coli O157:H7 causes diarrhoea, haemorrhagic colitis, and the haemolytic uraemic syndrome. We have identified a protein of previously unknown function encoded on the pO157 virulence plasmid of E. coli O157:H7, which is the first described protease that specifically cleaves C1 esterase inhibitor (C1-INH), a member of the serine protease inhibitor family. The protein, named StcE for secreted protease of C1 esterase inhibitor from EHEC (formerly Tagn), cleaves C1-INH to produce (unique) approximately 60-65 kDa fragments. StcE does not digest other serine protease inhibitors, extracellular matrix proteins or universal protease targets. We also observed that StcE causes the aggregation of cultured human T cells but not macrophage-like cells or B cells. Substitution of aspartic acid for glutamic acid at StcE position 435 within the consensus metalloprotease active site ablates its abilities to digest C1-INH and to aggregate T cells. StcE is secreted by the etp type II secretion pathway encoded on pO157, and extracellular StcE levels are positively regulated by the LEE-encoded regulator, Ler. StcE antigen and activity were detected in the faeces of a child with an E. coli O157:H7 infection, demonstrating the expression of StcE during human disease. Cleavage of C1-INH by StcE could plausibly cause localized pro-inflammatory and coagulation responses resulting in tissue damage, intestinal oedema and thrombotic abnormalities."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-2958.2002.02997.x"xsd:string
http://purl.uniprot.org/citations/12123444http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-2958.2002.02997.x"xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Torres A.G."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Torres A.G."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Welch R.A."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Welch R.A."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Kaper J.B."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Kaper J.B."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Tarr P.I."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Tarr P.I."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Grys T.E."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Grys T.E."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Lathem W.W."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Lathem W.W."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Witowski S.E."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/author"Witowski S.E."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/pages"277-288"xsd:string
http://purl.uniprot.org/citations/12123444http://purl.uniprot.org/core/pages"277-288"xsd:string