Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-3-9
pubmed:abstractText
Staphylococcus aureus is the most common etiological agent of bacterial arthritis and acute osteomyelitis and has been shown to bind to type II collagen under static and dynamic conditions. We have previously reported the effect of shear on the adhesion of S. aureus Phillips to collagen and found that this process is shear dependent (Z. Li, M. Höök, J. M. Patti, and J. M. Ross, Ann. Biomed. Eng. 24[Suppl. 1]:S-55). In this study, we used recombinant collagen adhesin fragments as well as polyclonal antibodies generated against adhesin fragments in attempts to inhibit bacterial adhesion. A parallel-plate flow chamber was used in a dynamic adhesion assay, and quantification of adhesion was accomplished by phase contrast video microscopy coupled with digital image processing. We report that both recombinant fragments studied, M19 and M55, and both polyclonal antibodies studied, alpha-M17 and alpha-M55, inhibit adhesion to varying degrees and that these processes are shear dependent. The M55 peptide and alpha-M55 cause much higher levels of inhibition than M19 and alpha-M17, respectively, at all wall shear rates studied. Our results demonstrate the importance of using a dynamic system in the assessment of inhibitory strategies and suggest the possible use of M55 and alpha-M55 in clinical applications to prevent infections caused by S. aureus adhesion to collagen.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-1311320, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-1469266, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-1744133, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-1965958, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-2142481, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-2440809, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-2792103, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-3160113, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-3722129, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-3750272, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-3883171, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-6993944, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-7014727, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-7074095, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-732875, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-7504692, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-7545162, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-7703489, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-7833055, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-7978549, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-8218209, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-8262622, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-8382334, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-875718, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-9218648, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-9334749, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-9459342, http://linkedlifedata.com/resource/pubmed/commentcorrection/9916063-9637697
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0019-9567
pubmed:author
pubmed:issnType
Print
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
589-94
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Inhibition of Staphylococcus aureus adherence to collagen under dynamic conditions.
pubmed:affiliation
Department of Chemical and Biochemical Engineering, University of Maryland Baltimore County, Baltimore, Maryland, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't