Lactoferrin iron levels affect attachment of Actinobacillus actinomycetemcomitans to buccal epithelial cells.

BACKGROUND: Prior reports have suggested that the iron-binding protein lactoferrin (LF) may either kill Actinobacillus actinomycetemcomitans (Aa) or interfere with its binding to host cells. Other studies have indicated that the degree of iron saturation of LF might play a role in these interactions. However, these studies utilized strains that had lost critical attachment characteristics found in well-preserved clinical isolates of Aa. The purpose of this work was to study the effect of LF iron levels on survival and attachment of well-preserved clinical isolates of Aa.
METHODS: LF containing 0%, 30%, and 100% iron saturation was tested for its ability to kill clinical isolates of Aa and to inhibit their binding to buccal epithelial cells (BECs).
RESULTS: Neither iron-free LF (apo-LF) nor iron-saturated LF killed Aa clinical isolates. Increasing the iron saturation of LF resulted in an increased inhibition of Aa binding to BECs (P < or =0.005). This effect was consistent for the 3 clinical isolates tested. Pretreatment of Aa with iron-saturated LF reduced binding to BECs by 58%, 61.8%, and 64.2%, respectively, for each of the 3 clinical strains tested (P < or =0.005). Pretreatment of Aa strains with apo-LF, iron alone, or bovine serum albumin had no effect on binding. Pretreatment of BECs with LF (either apo-LF or iron-containing LF) had no influence on Aa binding.
CONCLUSIONS: These results indicate that reduction in binding of Aa to epithelial cells is maximized by pretreatment of Aa cells with iron-saturated lactoferrin. These in vitro results suggest that patients with lactoferrin containing lowered levels of iron would be more susceptible to Aa colonization.