Attachment of staphylococci to silicone catheters in vitro

APMIS. 1990 May;98(5):471-8.


The adherence of radiolabeled staphylococci to silicone catheters was investigated in vitro. Staphylococcus aureus and Staphylococcus epidermidis strains bound to the same extent to the catheters. Also, S. epidermidis strains isolated from patients with plastic-related infections showed binding similar to that of other S. epidermidis strains. By preincubation of catheters the influence of purified staphylococcal cell surface components on the binding was evaluated. The most potent inhibitors of the binding of S. aureus were the two surface proteins, clumping factor and protein A, and the cytoplasmic membrane. Surface proteins and the cell membrane of S. epidermidis also blocked the binding. Only protein-containing surface proteins inhibited the binding. The production of slime correlated with the degree of S. epidermidis binding. Human plasma and serum, as well as purified albumin and IgG, inhibited the binding of both staphylococcal species. Fibrinogen, and to a certain extent fibronectin, inhibited the binding of S. epidermidis, while both these purified plasma proteins enhanced the binding of S. aureus.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Adhesion / drug effects
  • Bacterial Adhesion / physiology*
  • Bacterial Proteins / analysis
  • Bacterial Proteins / blood
  • Bacterial Proteins / pharmacology
  • Blood Proteins / pharmacology
  • Catheters, Indwelling*
  • Cell Adhesion / drug effects
  • Cell Adhesion / physiology
  • Cell Membrane / analysis
  • Cell Membrane / physiology
  • Cell Membrane / ultrastructure
  • Humans
  • Membrane Proteins / pharmacology
  • Silicones / metabolism*
  • Staphylococcus aureus / metabolism
  • Staphylococcus aureus / physiology*
  • Staphylococcus aureus / ultrastructure
  • Staphylococcus epidermidis / metabolism
  • Staphylococcus epidermidis / physiology*
  • Staphylococcus epidermidis / ultrastructure


  • Bacterial Proteins
  • Blood Proteins
  • Membrane Proteins
  • Silicones