Source:http://linkedlifedata.com/resource/pubmed/id/16548888
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
2006-3-21
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| pubmed:abstractText |
The pathogenesis of enteropathogenic Escherichia coli (EPEC) is characterized by the type III secretion system-dependent exploitation of target cells that results in attaching and effacing (A/E) lesions, actin rearrangements and pedestal formation. This pathology is mediated by effector proteins which are translocated by the type III secretion system into the host cell such as the translocated intimin receptor (Tir) and several E. coli secreted proteins (Esp). Secretion of virulence proteins of EPEC is tightly regulated. In response to Ca(2+), Esp secretion is drastically reduced, whereas secretion of Tir is increased. Membrane insertion of Tir, secreted under low Ca(2+) conditions, is therefore independent of Esp. Furthermore, espB and espD mutant strains of EPEC, unable to form the translocation pore, still translocate Tir into host cells membranes. This autointegrated Tir is functional, as it is able to complement a tir mutant strain in recruiting actin to bacterial contact sites. The uptake of Tir into the host cell appears to depend on the C-terminal part of the protein, as deletion of this part of Tir prevents autointegration. Together, our results demonstrate that under conditions of limited Ca(2+) an alternative mechanism for Tir integration can trigger the induction of A/E lesions.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/EaeB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/EspD protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Tir protein, E coli
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
|
| pubmed:issn |
1462-5814
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
8
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
625-33
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:16548888-Actins,
pubmed-meshheading:16548888-Bacterial Adhesion,
pubmed-meshheading:16548888-Bacterial Outer Membrane Proteins,
pubmed-meshheading:16548888-Caco-2 Cells,
pubmed-meshheading:16548888-Calcium,
pubmed-meshheading:16548888-Cell Membrane,
pubmed-meshheading:16548888-Diarrhea,
pubmed-meshheading:16548888-Enterocytes,
pubmed-meshheading:16548888-Escherichia coli,
pubmed-meshheading:16548888-Escherichia coli Infections,
pubmed-meshheading:16548888-Escherichia coli Proteins,
pubmed-meshheading:16548888-HeLa Cells,
pubmed-meshheading:16548888-Humans,
pubmed-meshheading:16548888-Microscopy, Electron, Transmission,
pubmed-meshheading:16548888-Mutation,
pubmed-meshheading:16548888-Protein Structure, Tertiary,
pubmed-meshheading:16548888-Protein Transport,
pubmed-meshheading:16548888-Receptors, Cell Surface
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| pubmed:year |
2006
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| pubmed:articleTitle |
Esp-independent functional integration of the translocated intimin receptor (Tir) of enteropathogenic Escherichia coli (EPEC) into host cell membranes.
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| pubmed:affiliation |
Institut für Infektiologie, Zentrum für Molekularbiologie der Entzündung (ZMBE), Universität Münster, Von-Esmarch-Strasse 56, 48149 Münster, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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