Aggregation substance of Enterococcus faecalis mediates adhesion to cultured renal tubular cells.
The sex pheromone system of Enterococcus faecalis is a unique, highly efficient plasmid collection mechanism for this species. A crucial role in this system is played by an adhesin called aggregation substance which enables the cell-cell contact between donor and recipient strains. The existence of the amino acid motif Arg-Gly-Asp-Ser in the adhesin prompted us to look for a possible binding of E. faecalis cells expressing aggregation substance to eucaryotic cells. We were able to show that the adhesin mediated binding to cultured renal tubular cells (porcine cell line LLC-PK1) via light microscopic, electron microscopic, and enzyme-linked immunosorbent assay-based studies. Synthesis of the adhesin was induced by some component(s) of serum. These data are interpreted to mean that aggregation substance is an adhesin mediating not only cell-cell contact between different E. faecalis strains but also binding of E. faecalis to eucaryotic cells, and therefore it might contribute to virulence.
Kreft
B
B
Klinik für Innere Medizin, Medizinische Universität zu Lübeck, Germany.
Marre
R
R
Schramm
U
U
Wirth
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001422:Bacterial Adhesion / Q000502:physiology*; D015153:Blotting, Western; D015815:Cell Adhesion Molecules; D002450:Cell Communication / Q000502:physiology; D002478:Cells, Cultured; D013293:Enterococcus faecalis / Q000472:pathogenicity*; D004797:Enzyme-Linked Immunosorbent Assay; D015964:Gene Expression Regulation, Bacterial; D066298:In Vitro Techniques; D007684:Kidney Tubules / Q000382:microbiology*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000502:physiology; D011506:Proteins / Q000502:physiology*; D013552:Swine
D015815:Cell Adhesion Molecules; D009842:Oligopeptides; D011506:Proteins; C013065:cell aggregation factors; C043691:cAD1 bacterial sex hormone