Source:http://linkedlifedata.com/resource/pubmed/id/19943904
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2010-1-5
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pubmed:abstractText |
Virulence of nosocomial pathogen Staphylococcus epidermidis is essentially related to formation of adherent biofilms, assembled by bacterial attachment to an artificial surface and subsequent production of a matrix that mediates interbacterial adhesion. Growing evidence supports the idea that proteins are functionally involved in S. epidermidis biofilm accumulation. We found that in S. epidermidis 1585v overexpression of a 460 kDa truncated isoform of the extracellular matrix-binding protein (Embp) is necessary for biofilm formation. Embp is a giant fibronectin-binding protein harbouring 59 Found In Various Architectures (FIVAR) and 38 protein G-related albumin-binding (GA) domains. Studies using defined Embp-positive and -negative S. epidermidis strains proved that Embp is sufficient and necessary for biofilm formation. Further data showed that the FIVAR domains of Embp mediate binding of S. epidermidis to solid-phase attached fibronectin, constituting the first step of biofilm formation on conditioned surfaces. The binding site in fibronectin was assigned to the fibronectin domain type III12. Embp-mediated biofilm formation also protected S. epidermidis from phagocytosis by macrophages. Thus, Embp is a multifunctional cell surface protein that mediates attachment to host extracellular matrix, biofilm accumulation and escape from phagocytosis, and therefore is well suited for promoting implant-associated infections.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1365-2958
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pubmed:author |
pubmed-author:AepfelbacherMartinM,
pubmed-author:BuckFriedrichF,
pubmed-author:ChristnerMartinM,
pubmed-author:FrankeGefion CGC,
pubmed-author:KrollGescheG,
pubmed-author:MackDietrichD,
pubmed-author:PehlePhilipP,
pubmed-author:RohdeHolgerH,
pubmed-author:SchommerNina NNN,
pubmed-author:SchulzeChristianC,
pubmed-author:WegertKimK,
pubmed-author:WendtUlrikeU
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pubmed:issnType |
Electronic
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
187-207
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pubmed:meshHeading |
pubmed-meshheading:19943904-Amino Acid Motifs,
pubmed-meshheading:19943904-Bacterial Adhesion,
pubmed-meshheading:19943904-Bacterial Proteins,
pubmed-meshheading:19943904-Binding Sites,
pubmed-meshheading:19943904-Biofilms,
pubmed-meshheading:19943904-Carrier Proteins,
pubmed-meshheading:19943904-Fibronectins,
pubmed-meshheading:19943904-Gene Deletion,
pubmed-meshheading:19943904-Humans,
pubmed-meshheading:19943904-Macrophages,
pubmed-meshheading:19943904-Phagocytosis,
pubmed-meshheading:19943904-Protein Binding,
pubmed-meshheading:19943904-Protein Interaction Mapping,
pubmed-meshheading:19943904-Staphylococcus epidermidis
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pubmed:year |
2010
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pubmed:articleTitle |
The giant extracellular matrix-binding protein of Staphylococcus epidermidis mediates biofilm accumulation and attachment to fibronectin.
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pubmed:affiliation |
Institut für Medizinische Mikrobiologie, Virologie und Hygiene, Universitätsklinikum Hamburg-Eppendorf, Martinistrasse 52, 20246 Hamburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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