title: Salivary amylase promotes adhesion of oral streptococci to hydroxyapatite.
abstract: 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.
authors.affiliation: Department of Oral Biology, School of Dental Medicine, State University of New York at Buffalo 14214, USA.
authors.forename: F A
authors.initials: FA
authors.lastname: Scannapieco
authors.forename: G I
authors.initials: GI
authors.lastname: Torres
authors.forename: M J
authors.initials: MJ
authors.lastname: Levine
mesh_terms: D018829:Adhesins, Bacterial / Q000187:drug effects / Q000378:metabolism; D000328:Adult; D000681:Amylases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D000704:Analysis of Variance; D001422:Bacterial Adhesion / Q000187:drug effects*; D044622:Dental Pellicle; D017886:Durapatite / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D008297:Male; D009055:Mouth / Q000382:microbiology*; D011485:Protein Binding / Q000187:drug effects; D011971:Receptors, Immunologic / Q000187:drug effects / Q000378:metabolism; D012463:Saliva / Q000737:chemistry / Q000201:enzymology*; D013291:Streptococcus / Q000378:metabolism / Q000472:pathogenicity*; D013298:Streptococcus sanguis / Q000378:metabolism / Q000472:pathogenicity
chemical_list: D018829:Adhesins, Bacterial; D004800:Enzymes, Immobilized; D011971:Receptors, Immunologic; C047105:bacterial adhesin receptor; D017886:Durapatite; D000681:Amylases