Staphylococcus epidermidis–fibronectin binding and its inhibition by heparin

We describe a method for the development of a trifunctional coating that repels contaminating bacteria, kills those that adhere, and promotes osteoblast adhesion

Carla Renata Arciola

2003

Scholarcy highlights

  • Staphylococcus epidermidis not long ago was considered a mere saprophyte, usually harboured on the skin and mucosae
  • The binding of S. epidermidis to fibronectin, a main protein of the extracellular matrix, and the effect of heparin on this interaction were studied by dynamic force spectroscopy
  • Novelties are that S. epidermidis strains analysed by DFS were clinical isolates from prosthesis-associated infections, genotyped and phenotyped for their adhesion properties to fibronectin and examined as living cells
  • Studies with fibronectin fragments demonstrated that the carboxyl terminus site has a binding affinity higher than amino terminus, but a recent investigation with atomic force microscope on intact fibronectin molecules shows that it is the amino terminus site, which is favourite for the heparin–fibronectin binding
  • The fibronectin binding was found to take place with the fibronectin adhesin on the bacterial surface, because it disappeared when adhesin was blocked by a free fibronectin molecule before the contact with the fibronectin bound to the tip
  • The best culture conditions were reached only when, 24 h following bacterial seeding, 40% of the culture medium was substituted with fresh TSB and incubation was continued for further 48 h
  • Inhibited Lipoprotein lipase is in a complex with angiopoietin-like protein 4, and upon dissociation LPL regains activity
  • Our findings suggest that angiopoietin-like protein 4 inhibits Lipoprotein lipase by binding the lid domain, which could prevent substrate catalysis at the active site

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