Binding ofStreptococcus mutans, Serotype c, to Saliva-coated Hydroxyapatite in the Presence and Absence of Human Lactoferrin

Abstract

The adhesion of 3H-labelled Streptococcus mutans (serotype c) cells to spheroidal hydroxyapatite (HA) beads was studied by precoating HA with whole saliva with or without the presence of human lactoferrin (LF). Treatment of HA with LF-free saliva prevented the streptococcal adhesion more strongly than treatment with buffer alone. However, supplementation of LF-free saliva by iron-free LF (apo LF), or partly or totally Fe"-saturated LF (200 mg/l), significantly enhanced (P<0.001) the inhibition. No notable differences existed between the various forms of LF. The inhibition of bacterial adherence was dose dependent with respect to the amount of LF bound to saliva-coated HA (SHA), suggesting a non-specific protein blockage. Significant (P<0.001) inhibition was observed with apo LF concentration as low as 10 mg/l. LF-mediated inhibition of the adherence of S. mutans, serotype c, to SHA is obviously non-specific, antibacterial function for this innate defence protein which is present in human saliva, gingival crevicular fluid and also as an integral part of the acquired salivary pellicle in vivo.

Cumulative Correlations of Lysozyme, Lactoferrin, Peroxidase, S-IgA, Amylase, and Total Protein Concentrations with Adherence of Oral Viridans Streptococci to Microplates Coated with Human Saliva

“…Strain-specificity also may explain previous and present findings for lactoferrin. Soukka et al (1994) recently reported that lactoferrin mediated non-specific dose-dependent inhibition of S. mutans adherence to saliva-coated hydroxyapatite. Current results for S. sanguis 13379 appear consistent with lactoferrin inhibition of adherence.…”

“…Adherence may show redundancy in the sense that it is promoted or modulated by many pellicle proteins. The list includes acidic proline-rich proteins (Gibbons et al, 1991), statherin (Gibbons et al, 1988), amylase (Scannapieco et al, 1995), mucin glycoproteins 1 and 2 (Murray et al, 1992;Veerman et al, 1995), proline-rich glycoprotein (Murray et al, 1992), parotid salivary agglutinin (Brady et al, 1992), secretory IgA (Liljemark et al, 1979), lysozyme (Tellefson and Germaine, 1986), lactoferrin (Soukka et al, 1994), and salivary peroxidase (Roger et al, 1994). Each of those proteins has other properties, including inhibition of calcium phosphate precipitation (proline-rich proteins and statherin), starch digestion (amylase), soft tissue lubrication 759 (mucin glycoprotein 1), bacterial aggregation (proline-rich glycoprotein, parotid salivary agglutinin, secretory IgA), and cell killing or inhibition (lysozyme, lactoferrin, and salivary peroxidase) (Scannapieco, 1994;Rudney et al, 1995b).…”

Comparison of Antibacterial Adhesion When Salivary Pellicle Is Coated on Both Poly(2-hydroxyethyl-methacrylate)- and Polyethylene-glycol-methacrylate-grafted Poly(methyl methacrylate)

“…The presence of salivary pellicle on modified titanium surfaces (machined, acid-etched, and acid-etched and blasted) may result in negatively charged surfaces that attract calcium ions and facilitate the adhesion of S. mutans and Fusobacterium nucleatum to the surfaces [ 20 ]. However, studies of the adherence of S. mutans to hydroxyapatite precoated with whole saliva, with or without the presence of the antibacterial agent Lysozyme, showed a significant reduction in the adherence [ 21 , 22 ]. The aim of this study is to compare the antibacterial adhesion of pHEMA- and PEGMA-grafted PMMA when salivary pellicle is coated on the grafted PMMA.…”

Binding of Salivary Glycoprotein-Secretory Immunoglobulin A Complex to the Surface Protein Antigen of Streptococcus mutans

“…Various salivary components, such as secretory immunoglobulin A (sIgA) (36), ␤ 2 -microglobulin (12), histidine-rich polypeptides (32), a 60-kDa glycoprotein (1), lysozyme (39), lactoferrin (43), and high-molecular-mass glycoproteins (4,7,13,20), have been reported to bind to S. mutans and/or to induce agglutination of the organism. Much attention has also been focused on the interaction between PAc and salivary components (5,8,21,(27)(28)(29).…”