Characterization of lactoferrin interaction with Streptococcus mutans

Lactoferrin (LF) is an iron-binding glycoprotein common to exocrine secretions and the specific granules of neutrophils. Each molecule is capable of high-affinity coordinate-binding of two ferric ions with two bicarbonate or carbonic anions. The initial aspect of the present study was directed at determining the nature of anion involvement in LF bactericidal activity. It was found that selective anions were capable of inhibiting the expression of bactericidal activity by LF on S. mutans 10449. The ability to block LF expression was directly related to the capacity of the anion to serve as a coordinate ion in iron-binding by the transferrin molecules. These data support the hypothesis that the LF target site on the bacterial surface is anionic. There has been controversy in the literature regarding LF involvement in hydroxy radical generation. The second phase of these studies indicated that treatment of S. mutans with LF under anaerobic conditions abrogated the bactericidal effect of this molecule. LF-killing could be enhanced by the presence of thiocyanate and inhibited by catalase and lactoperoxidase; however, bovine serum albumin was equally effective as an inhibitor. The apparent requirement for oxygen in LF bactericidal effect on S. mutans is not inconsistent with a hydroxy radical mechanism.