Source:http://linkedlifedata.com/resource/pubmed/id/11333985
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6833
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| pubmed:dateCreated |
2001-5-3
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| pubmed:abstractText |
Cell-surface heparan sulphate proteoglycans (HSPGs) are ubiquitous and abundant receptors/co-receptors of extracellular ligands, including many microbes. Their role in microbial infections is poorly defined, however, because no cell-surface HSPG has been clearly connected to the pathogenesis of a particular microbe. We have previously shown that Pseudomonas aeruginosa, through its virulence factor LasA, enhances the in vitro shedding of syndecan-1-the predominant cell-surface HSPG of epithelia. Here we show that shedding of syndecan-1 is also activated by P. aeruginosa in vivo, and that the resulting syndecan-1 ectodomains enhance bacterial virulence in newborn mice. Newborn mice deficient in syndecan-1 resist P. aeruginosa lung infection but become susceptible when given purified syndecan-1 ectodomains or heparin, but not when given ectodomain core protein, indicating that the ectodomain's heparan sulphate chains are the effectors. In wild-type newborn mice, inhibition of syndecan-1 shedding or inactivation of the shed ectodomain's heparan sulphate chains prevents lung infection. Our findings uncover a pathogenetic mechanism in which a host response to tissue injury-syndecan-1 shedding-is exploited to enhance microbial virulence apparently by modulating host defences.
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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/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Heparitin Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Sdc1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecan-1,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecans
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| pubmed:status |
MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
0028-0836
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
3
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| pubmed:volume |
411
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
98-102
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11333985-Animals,
pubmed-meshheading:11333985-Animals, Newborn,
pubmed-meshheading:11333985-Bacterial Adhesion,
pubmed-meshheading:11333985-Disease Models, Animal,
pubmed-meshheading:11333985-Heparin,
pubmed-meshheading:11333985-Heparitin Sulfate,
pubmed-meshheading:11333985-Lung,
pubmed-meshheading:11333985-Lung Diseases,
pubmed-meshheading:11333985-Membrane Glycoproteins,
pubmed-meshheading:11333985-Mice,
pubmed-meshheading:11333985-Mice, Inbred BALB C,
pubmed-meshheading:11333985-Protein Structure, Tertiary,
pubmed-meshheading:11333985-Proteoglycans,
pubmed-meshheading:11333985-Pseudomonas Infections,
pubmed-meshheading:11333985-Pseudomonas aeruginosa,
pubmed-meshheading:11333985-Syndecan-1,
pubmed-meshheading:11333985-Syndecans,
pubmed-meshheading:11333985-Virulence
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| pubmed:year |
2001
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| pubmed:articleTitle |
Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence.
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| pubmed:affiliation |
Division of Newborn Medicine, Department of Pediatrics, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA. pwpark@bcm.tmc.edu
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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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