Source:http://linkedlifedata.com/resource/pubmed/id/12123444
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2002-7-18
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| pubmed:abstractText |
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.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C1 Inactivator Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0950-382X
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
45
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
277-88
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:12123444-Blood Proteins,
pubmed-meshheading:12123444-Cell Aggregation,
pubmed-meshheading:12123444-Cells, Cultured,
pubmed-meshheading:12123444-Child,
pubmed-meshheading:12123444-Complement C1 Inactivator Proteins,
pubmed-meshheading:12123444-Consensus Sequence,
pubmed-meshheading:12123444-Diarrhea,
pubmed-meshheading:12123444-Escherichia coli,
pubmed-meshheading:12123444-Escherichia coli Infections,
pubmed-meshheading:12123444-Escherichia coli Proteins,
pubmed-meshheading:12123444-Feces,
pubmed-meshheading:12123444-Humans,
pubmed-meshheading:12123444-Jurkat Cells,
pubmed-meshheading:12123444-Metalloendopeptidases,
pubmed-meshheading:12123444-Plasmids,
pubmed-meshheading:12123444-T-Lymphocytes,
pubmed-meshheading:12123444-Trans-Activators,
pubmed-meshheading:12123444-Virulence
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| pubmed:year |
2002
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| pubmed:articleTitle |
StcE, a metalloprotease secreted by Escherichia coli O157:H7, specifically cleaves C1 esterase inhibitor.
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| pubmed:affiliation |
Department of Medical Microbiology and Immunology, University of Wisconsin, Madison, WI 53706, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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