Source:http://linkedlifedata.com/resource/pubmed/id/17975086
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 11
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| pubmed:dateCreated |
2007-11-2
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| pubmed:abstractText |
Enterotoxigenic Escherichia coli (ETEC) causes enterotoxin-induced diarrhoea and significant mortality. The molecular mechanisms underlying how the heat-labile enterotoxin (LT) is secreted during infection are poorly understood. ETEC produce outer-membrane vesicles (OMVs) containing LT that are endocytosed into host cells. Although OMV production and protein content may be a regulated component of ETEC pathogenesis, how LT loading into OMVs is regulated is unknown. The LeoA protein plays a role in secreting LT from the bacterial periplasm. To begin to understand the function of LeoA and its role in ETEC H10407 pathogenesis, a site-directed mutant lacking the putative GTP-binding domain was constructed. The ability of wild-type and mutant LeoA to hydrolyse GTP in vitro was quantified. This domain was found to be responsible for GTP binding; it is important to LeoA's function in LT secretion, and may play a modest role in the formation and protein content of OMVs. Deletion of leoA reduced the abundance of OmpX in outer-membrane protein preparations and of LT in OMVs. Immunoprecipitation experiments revealed that LeoA interacts directly with OmpA, but that the GTP-binding domain is non-essential for this interaction. Deletion of leoA rendered ETEC H10407 non-motile, through apparent periplasmic accumulation of FliC.
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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/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/OMPA outer membrane proteins,
http://linkedlifedata.com/resource/pubmed/chemical/heat-labile enterotoxin, E coli
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
1350-0872
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
153
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3776-84
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| pubmed:dateRevised |
2008-10-3
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| pubmed:meshHeading |
pubmed-meshheading:17975086-Animals,
pubmed-meshheading:17975086-Bacterial Outer Membrane Proteins,
pubmed-meshheading:17975086-Bacterial Toxins,
pubmed-meshheading:17975086-Cell Membrane,
pubmed-meshheading:17975086-Enterotoxigenic Escherichia coli,
pubmed-meshheading:17975086-Enterotoxins,
pubmed-meshheading:17975086-Escherichia coli Proteins,
pubmed-meshheading:17975086-GTP Phosphohydrolases,
pubmed-meshheading:17975086-Gene Deletion,
pubmed-meshheading:17975086-Gene Expression Regulation, Bacterial,
pubmed-meshheading:17975086-Guanosine Triphosphate,
pubmed-meshheading:17975086-Humans,
pubmed-meshheading:17975086-Immunoprecipitation,
pubmed-meshheading:17975086-Microscopy, Electron, Transmission,
pubmed-meshheading:17975086-Mutagenesis, Site-Directed,
pubmed-meshheading:17975086-Periplasm,
pubmed-meshheading:17975086-Transport Vesicles,
pubmed-meshheading:17975086-Two-Hybrid System Techniques
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| pubmed:year |
2007
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| pubmed:articleTitle |
Biochemical characterization of the enterotoxigenic Escherichia coli LeoA protein.
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| pubmed:affiliation |
Center for Infectious Disease Research and Vaccinology, South Dakota State University, Brookings, SD 57007, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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