title: Enterococcus faecalis surface proteins determine its adhesion mechanism to bile drain materials.
abstract: An important step in infections associated with biliary drains is adhesion of micro-organisms to the surface. In this study the role of three surface proteins of Enterococcus faecalis (enterococcal surface protein, aggregation substances 1 and 373) in the adhesion to silicone rubber, fluoro-ethylene-propylene and polyethylene was examined. Four isogenic E. faecalis strains with and without aggregation substances and one strain expressing enterococcal surface protein were used. The kinetics of enterococcal adhesion to the materials was measured in situ in a parallel plate flow chamber. Initial deposition rates were similar for all strains, whereas the presence of surface proteins increased the total number of adhering bacteria. Nearest neighbour analysis demonstrated that enterococci expressing the whole sex-pheromone plasmid encoding aggregation substances 1 or 373 adhered in higher numbers through mechanisms of positive cooperativity, which means that adhesion of bacteria enhances the probability of adhesion of other bacteria near these bacteria. Enterococci with the enterococcal surface protein did not adhere through this mechanism. These findings indicate that the surface proteins of E. faecalis play a key role in the adhesion to bile drains and bile drain associated infections.
authors.affiliation: Department of Medical Microbiology1 and Department of Biomedical Engineering2, University of Groningen, Hanzeplein 1, 9713 GZ Groningen, The Netherlands.
authors.forename: Karola
authors.initials: K
authors.lastname: Waar
authors.affiliation: Department of Medical Microbiology1 and Department of Biomedical Engineering2, University of Groningen, Hanzeplein 1, 9713 GZ Groningen, The Netherlands.
authors.forename: Henny C
authors.initials: HC
authors.lastname: van der Mei
authors.affiliation: Department of Medical Microbiology1 and Department of Biomedical Engineering2, University of Groningen, Hanzeplein 1, 9713 GZ Groningen, The Netherlands.
authors.forename: Hermie J M
authors.initials: HJM
authors.lastname: Harmsen
authors.affiliation: Department of Medical Microbiology1 and Department of Biomedical Engineering2, University of Groningen, Hanzeplein 1, 9713 GZ Groningen, The Netherlands.
authors.forename: John E
authors.initials: JE
authors.lastname: Degener
authors.affiliation: Department of Medical Microbiology1 and Department of Biomedical Engineering2, University of Groningen, Hanzeplein 1, 9713 GZ Groningen, The Netherlands.
authors.forename: Henk J
authors.initials: HJ
authors.lastname: Busscher
mesh_terms: D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism*; D001646:Bile; D013293:Enterococcus faecalis / Q000737:chemistry / Q000145:classification / Q000254:growth & development / Q000502:physiology*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000378:metabolism*; D010802:Phylogeny; D020959:Polyethylene / Q000737:chemistry / Q000378:metabolism*; D011138:Polytetrafluoroethylene / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D012826:Silicone Elastomers / Q000737:chemistry / Q000378:metabolism*; D013499:Surface Properties; D005465:Fluorocarbon Polymers
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D020959:Polyethylene; D011138:Polytetrafluoroethylene; D012826:Silicone Elastomers; C065937:aggregation substance, Enterococcus faecalis; C116707:enterococcal surface protein, esp; C096305:fluorinated ethylene propylene; D005465:Fluorocarbon Polymers