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Infection and Immunity, November 2001, p. 7046-7056, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.7046-7056.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Role of Streptococcus gordonii Amylase-Binding Protein A in Adhesion to Hydroxyapatite, Starch Metabolism, and Biofilm Formation

Jeffrey D. Rogers,1,dagger Robert J. Palmer Jr.,2 Paul E. Kolenbrander,2 and Frank A. Scannapieco1,*

Department of Oral Biology, School of Dental Medicine, University at Buffalo, The State University of New York, Buffalo, New York 14214,1 and Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 208922

Received 1 March 2001/Returned for modification 11 April 2001/Accepted 13 June 2001

Interactions between bacteria and salivary components are thought to be important in the establishment and ecology of the oral microflora. alpha -Amylase, the predominant salivary enzyme in humans, binds to Streptococcus gordonii, a primary colonizer of the tooth. Previous studies have implicated this interaction in adhesion of the bacteria to salivary pellicles, catabolism of dietary starches, and biofilm formation. Amylase binding is mediated at least in part by the amylase-binding protein A (AbpA). To study the function of this protein, an erythromycin resistance determinant [erm(AM)] was inserted within the abpA gene of S. gordonii strains Challis and FAS4 by allelic exchange, resulting in abpA mutant strains Challis-E1 and FAS4-E1. Comparison of the wild-type and mutant strains did not reveal any significant differences in colony morphology, biochemical metabolic profiles, growth in complex or defined media, surface hydrophobicity, or coaggregation properties. Scatchard analysis of adhesion isotherms demonstrated that the wild-type strains adhered better to human parotid-saliva- and amylase-coated hydroxyapatite than did the AbpA mutants. In contrast, the mutant strains bound to whole-saliva-coated hydroxyapatite to a greater extent than did the wild-type strains. While the wild-type strains preincubated with purified salivary amylase grew well in defined medium with potato starch as the sole carbohydrate source, the AbpA mutants did not grow under the same conditions even after preincubation with amylase. In addition, the wild-type strain produced large microcolonies in a flow cell biofilm model, while the abpA mutant strains grew much more poorly and produced relatively small microcolonies. Taken together, these results suggest that AbpA of S. gordonii functions as an adhesin to amylase-coated hydroxyapatite, in salivary-amylase-mediated catabolism of dietary starches and in human saliva-supported biofilm formation by S. gordonii.

* Corresponding author. Mailing address: 109 Foster Hall, Department of Oral Biology, School of Dental Medicine, University at Buffalo, The State University of New York, Buffalo, NY 14214. Phone: (716) 829-3373. Fax: (716) 829-0642. E-mail: fas1{at}acsu.buffalo.edu.

dagger Present address: Department of Periodontics, School of Dentistry, Virginia Commonwealth University, Richmond, VA 23298-0566.

Infection and Immunity, November 2001, p. 7046-7056, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.7046-7056.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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