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231224s2013 xx |||||o 00| ||eng c |
| 024 |
7 |
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|a 10.1021/la4029172
|2 doi
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|a pubmed24n0772.xml
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|a (DE-627)NLM231566719
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|a (NLM)24111821
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Herman, Philippe
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Forces driving the attachment of Staphylococcus epidermidis to fibrinogen-coated surfaces
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|c 2013
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 06.06.2014
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|a Date Revised 22.10.2013
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Cell surface proteins of bacteria play essential roles in mediating the attachment of pathogens to host tissues and, therefore, represent key targets for anti-adhesion therapy. In the opportunistic pathogen Staphylococcus epidermidis , the adhesion protein SdrG mediates attachment of bacteria to the blood plasma protein fibrinogen (Fg) through a binding mechanism that is not yet fully understood. We report the direct measurement of the forces driving the adhesion of S. epidermidis to Fg-coated substrates using single-cell force spectroscopy. We found that the S. epidermidis -Fg adhesion force is of ~150 pN magnitude and that the adhesion strength and adhesion probability strongly increase with the interaction time, suggesting that the adhesion process involves time-dependent conformational changes. Control experiments with mutant bacteria lacking SdrG and substrates coated with the Fg β(6-20) peptide, instead of the full Fg protein, demonstrate that these force signatures originate from the rupture of specific bonds between SdrG and its peptide ligand. Collectively, our results are consistent with a dynamic, multi-step ligand-binding mechanism called "dock, lock, and latch"
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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| 650 |
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7 |
|a Bacterial Proteins
|2 NLM
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| 650 |
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7 |
|a Carrier Proteins
|2 NLM
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| 650 |
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|a Fbe protein, bacteria
|2 NLM
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| 650 |
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7 |
|a Fibrinogen
|2 NLM
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| 650 |
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7 |
|a 9001-32-5
|2 NLM
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| 700 |
1 |
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|a El-Kirat-Chatel, Sofiane
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Beaussart, Audrey
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Geoghegan, Joan A
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Vanzieleghem, Thomas
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Foster, Timothy J
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Hols, Pascal
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Mahillon, Jacques
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Dufrêne, Yves F
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 29(2013), 42 vom: 22. Okt., Seite 13018-22
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:29
|g year:2013
|g number:42
|g day:22
|g month:10
|g pages:13018-22
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|u http://dx.doi.org/10.1021/la4029172
|3 Volltext
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