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Binding of immobilized fibronectin by biliary drain isolates
J L Yu1, R Andersson, A Ljungh
1Department of Medical Microbiology, Lund University Hospital, Sweden.
Zentralblatt Fur Bakteriologie : International Journal of Medical Microbiology
|June 25, 1998
Summary
Bacterial adhesion to biliary stents involves fibronectin (Fn) binding by E. coli. This interaction is protein-mediated and can be inhibited by D-mannose, suggesting potential therapeutic targets.
Area of Science:
- Biomedical Engineering
- Microbiology
- Biomaterials Science
Background:
- Bacterial adhesion to biliary stents causes occlusion, a significant clinical issue.
- Biliary proteins like fibronectin (Fn) and vitronectin (Vn) are implicated in bacterial adhesion to biomaterials.
Purpose of the Study:
- To investigate the mechanism of fibronectin (Fn) binding by E. coli strains isolated from biliary sources.
- To determine if bacterial adhesion to Fn is a protein-protein interaction and identify potential inhibitory factors.
Main Methods:
- Studied Fn binding by five E. coli strains isolated from biliary drains or bile.
- Assessed bacterial adhesion to immobilized plasma Fn and ovalbumin.
- Investigated the effect of periodate treatment, mannose-containing saccharides, trypsin, and protease treatments on adhesion.
Main Results:
- E. coli strains bound immobilized plasma Fn but not soluble Fn.
- Adhesion to Fn was unaffected by ovalbumin periodate treatment but inhibited by mannose, trypsin, and bacterial protease treatment.
- Autoradiography confirmed protein-protein interactions between E. coli components and Fn.
Conclusions:
- E. coli adhesion to fibronectin (Fn) is mediated by protein-protein interactions, potentially involving fimbrial components.
- D-mannose and protease treatments effectively inhibit this adhesion, suggesting therapeutic strategies for preventing stent occlusion.