Linked Life Data

10707941

Source:http://linkedlifedata.com/resource/pubmed/id/10707941

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-3-13
pubmed:abstractText
Coagulase-negative staphylococci (CNS) are the most common infectious micro-organisms isolated from prosthetic devices. To determine whether von Willebrand factor (vWF) acts as an adhesin in bacterial recognition, bacterial binding of recombinant vWF (rvWF) was studied. Eleven CNS strains, belonging to S. epidermidis, S. haemolyticus and S. hominis species, bound soluble rvWF, but to a lesser extent than S. aureus. S. epidermidis strain H2-W bound 125I-labelled rvWF in a dose-dependent manner. The binding could be inhibited by unlabelled rvWF and thrombospondin, but not by fibrinogen, vitronectin or the carbohydrates N-acetylgalactoseamine, D-galactose, D-glucose, and D-fucose. Pre-incubation of rvWF with type I collagen and Arg-Gly-Asp-Ser (RGDS) peptides did not inhibit binding, whereas pre-incubation of rvWF with heparin decreased binding significantly. The interaction between CNS and rvWF was sensitive to proteinase treatment of bacterial cells. CNS strains bound to immobilised rvWF an extent greater or equal to the positive control strain S. aureus Cowan I. rvWF binding structures from bacterial cell wall were detected by immunoblot. Cowan I strain had 140-, 90- and 38-kDa binding molecules. S. haemolyticus strain SM131 and S. epidermidis strain H2-W had two (120 and 60 kDa) and five (120, 90, 60, 52 and 38 kDa) binding molecules, respectively. Similar binding structures were formed when cell wall extracts from these strains were incubated with thrombospondin. These results indicate that specific ligand-receptor interaction between CNS and rvWF may contribute to bacterial adhesion and colonisation on biomaterial surfaces. Heparin-binding domains of rvWF might be the crucial regions for bacterial attachment. rvWF and thrombospondin may recognise similar molecules in staphylococcal cell wall extracts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-2615
pubmed:author
pubmed:issnType
Print
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
217-25
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10707941-Bacterial Adhesion, pubmed-meshheading:10707941-Binding, Competitive, pubmed-meshheading:10707941-Carbohydrates, pubmed-meshheading:10707941-Coagulase, pubmed-meshheading:10707941-Collagen, pubmed-meshheading:10707941-Culture Media, pubmed-meshheading:10707941-Dose-Response Relationship, Drug, pubmed-meshheading:10707941-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:10707941-Endopeptidases, pubmed-meshheading:10707941-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:10707941-Fibrinogen, pubmed-meshheading:10707941-Heparin, pubmed-meshheading:10707941-Hot Temperature, pubmed-meshheading:10707941-Humans, pubmed-meshheading:10707941-Immunoblotting, pubmed-meshheading:10707941-Luminescent Measurements, pubmed-meshheading:10707941-Polystyrenes, pubmed-meshheading:10707941-Recombinant Proteins, pubmed-meshheading:10707941-Solubility, pubmed-meshheading:10707941-Staphylococcus, pubmed-meshheading:10707941-Thrombospondins, pubmed-meshheading:10707941-Vitronectin, pubmed-meshheading:10707941-von Willebrand Factor
pubmed:year
2000
pubmed:articleTitle
Binding of von Willebrand factor by coagulase-negative staphylococci.
pubmed:affiliation
Department of Infectious Diseases and Medical Microbiology, Lund University, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't