Binding of von Willebrand factor by coagulase-negative staphylococci.
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.
Li
Dai-Qing
DQ
Department of Infectious Diseases and Medical Microbiology, Lund University, Lund, Sweden.
Lundberg
Fredrik
F
Department of Infectious Diseases and Medical Microbiology, Lund University, Lund, Sweden.
Ljungh
Åsa
Å
Department of Infectious Diseases and Medical Microbiology, Lund University, Lund, Sweden.
D001422:Bacterial Adhesion / Q000187:drug effects; D001667:Binding, Competitive; D002241:Carbohydrates / Q000494:pharmacology; D003030:Coagulase; D003094:Collagen / Q000494:pharmacology; D003470:Culture Media; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D005340:Fibrinogen / Q000494:pharmacology; D006493:Heparin / Q000494:pharmacology; D006358:Hot Temperature; D006801:Humans; D015151:Immunoblotting; D008163:Luminescent Measurements; D011137:Polystyrenes / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012995:Solubility; D013210:Staphylococcus / Q000201:enzymology / Q000378:metabolism*; D019699:Thrombospondins / Q000494:pharmacology; D019096:Vitronectin / Q000494:pharmacology; D014841:von Willebrand Factor / Q000378:metabolism*
D002241:Carbohydrates; D003030:Coagulase; D003470:Culture Media; D011137:Polystyrenes; D011994:Recombinant Proteins; D019699:Thrombospondins; D019096:Vitronectin; D014841:von Willebrand Factor; D005340:Fibrinogen; D006493:Heparin; D003094:Collagen; D010450:Endopeptidases