Salivary amylase promotes adhesion of oral streptococci to hydroxyapatite.

Recent studies have demonstrated that several species of oral streptococci, such as Streptococcus gordonii, bind soluble salivary alpha-amylase. The goal of the present study was to determine if amylase immobilized onto a surface such as hydroxyapatite can serve as an adhesion receptor for S. gordonii. Initially, human parotid saliva was fractionated on Bio-Gel P60, and fractions were screened for their ability to promote adhesion of S. gordonii to hydroxyapatite. Fractions containing alpha-amylase and proline-rich proteins promoted the adhesion of [3H]-labeled S. gordonii to hydroxyapatite. Similar findings were obtained with purified amylase and acidic proline-rich protein 1 (PRP1). Incubation of S. gordonii G9B in the presence of starch and maltotriose increased the binding of this strain to amylase-coated hydroxyapatite, while the adhesion of S. sanguis 10556 to amylase-coated hydroxyapatite was not affected by these saccharides. These results suggest that amylase may serve as a hydroxyapatite pellicle receptor for amylase-binding streptococci. Furthermore, starch and starch metabolites may enhance the adhesion of amylase-binding streptococci to amylase in dental pellicles to augment the formation of dental plaque.