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- Title
Salivary Amylase Promotes Adhesion of Oral Streptococci to Hydroxyapatite.
- Authors
Scannapieco, F. A.; Torres, G. I.; Levine, M. J.
- Abstract
Recent studies have demonstrated that several species of oral streptococci, such as Streptococcus gordonii, bind soluble salivary a-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 a-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.
- Subjects
BACTERIAL adhesion; HYDROXYAPATITE; STREPTOCOCCUS; AMYLASES; SALIVA microbiology; SACCHARIDES; PAROTID glands
- Publication
Journal of Dental Research, 1995, Vol 74, Issue 7, p1360
- ISSN
0022-0345
- Publication type
Article
- DOI
10.1177/00220345950740070701