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Salivary Amylase Promotes Adhesion of Oral Streptococci to Hydroxyapatite
F.A. Scannapieco
Department of Oral Biology and Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, New York 14214
G.I. Torres
Department of General Dentistry, Eastman Dental Center, Rochester, New York 14620
M.J. Levine
Department of Oral Biology and Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, New York 14214
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.
Key Words: microbial adherence • dental plaque • salivary proteins • viridans streptococci • saliva
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Journal of Dental Research, Vol. 74, No. 7,
1360-1366 (1995)
DOI: 10.1177/00220345950740070701
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