The inhibitory activity of serum to prevent bacterial adhesion is mainly due to apo-transferrin.

A marked, up to 5-fold, reduction in bacterial adhesion to Tecoflex polyurethane (PU) surfaces was observed in the presence of bovine/human serum or plasma at 0.5% or higher concentrations in the medium. Further investigation of the phenomenon resulted in identification, isolation, and characterization of the serum component with the ability to significantly reduce bacterial adhesion. Upon fractionation of bovine serum by an anion exchange chromatography, protein pools were made and analyzed by immunoelectrophoresis and by polyacrylamide gel electrophoresis in the presence of SDS and were examined for their effect on the adhesion of Staphylococcus epidermidis to PU surfaces. The pool exhibiting a significant inhibitory effect was subjected to further biochemical tests, which resulted in the identification of transferrin (Tf) as its predominant protein. Bacterial adhesion studies in the presence of purified Tf revealed that holo-Tf (iron-containing form) had no influence on bacterial adhesion at any concentration. Only apo-Tf (iron-lacking form) exerted the inhibitory effect, in a dose responsive manner at concentrations of 10 microg/mL or higher. Bacteria remained viable when suspended at the low apo-Tf concentrations, sufficient to prevent bacterial adhesion. Copyright 2003 Wiley Periodicals, Inc.