This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hamada, T. Articles by Senpuku, H. Search for Related Content PubMed PubMed Citation Articles by Hamada, T. Articles by Senpuku, H.

 Previous Article  |  Next Article 

Infection and Immunity, August 2004, p. 4819-4826, Vol. 72, No. 8
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.8.4819-4826.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Molecular Interactions of Surface Protein Peptides of Streptococcus gordonii with Human Salivary Components

Department of Cariology and Operative Dentistry, Tokyo Medical and Dental University, Tokyo 113-8519,¹ Department of Oral Health, National Institute of Public Health,² Department of Bacteriology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan³

Received 17 October 2003/ Returned for modification 12 January 2004/ Accepted 12 April 2004

Oral streptococci play a large role in dental biofilm formation, and several types interact as early colonizers with the enamel salivary pellicle to form the primary biofilm, as well as to incorporate other bacteria on tooth surfaces. Interactions of surface molecules of individual streptococci with the salivary pellicle on the tooth surface have an influence on the etiological properties of an oral biofilm. To elucidate the molecular interactions of streptococci with salivary components, binding between surface protein (SspB and PAg) peptides of Streptococcus gordonii and Streptococcus sobrinus were investigated by utilizing BIAcore biosensor technology. The analogous peptide [change of T at position 400 to K in SspB(390-402), resulting in the SspB(390-T400K-402) peptide] from S. gordonii showed the greatest response for binding to salivary components and inhibited the binding of Streptococcus sanguis by more than 50% in a competitive inhibition assay in a comparison with other SspB and PAg peptides. This peptide also bound to the high-molecular-weight protein complex of salivary components and the agglutinin (gp340/DMBT1) peptide (scavenger receptor cysteine-rich domain peptide 2 [SRCRP 2]). In addition, the SspB(390-T400K-402) peptide was visualized by two surface positive charges in connection with the positively charged residues, in which lysine was a key residue for binding. Therefore, the region containing lysine may have binding activity in S. gordonii and S. sanguis, and the SRCRP 2 region may function as a receptor for the binding. These findings may provide useful information regarding the molecular mechanism of early biofilm formation by streptococci on tooth surfaces.

Editor: V. J. DiRita

This article has been cited by other articles:

• Nobbs, A. H., Zhang, Y., Khammanivong, A., Herzberg, M. C. (2007). Streptococcus gordonii Hsa Environmentally Constrains Competitive Binding by Streptococcus sanguinis to Saliva-Coated Hydroxyapatite. J. Bacteriol. 189: 3106-3114 [Abstract] [Full Text]  
• Stratmann, J., Dohmann, K., Heinzmann, J., Gerlach, G.-F. (2006). Peptide aMptD-Mediated Capture PCR for Detection of Mycobacterium avium subsp. paratuberculosis in Bulk Milk Samples. Appl. Environ. Microbiol. 72: 5150-5158 [Abstract] [Full Text]  
• Kreikemeyer, B., Nakata, M., Oehmcke, S., Gschwendtner, C., Normann, J., Podbielski, A. (2005). Streptococcus pyogenes Collagen Type I-binding Cpa Surface Protein: EXPRESSION PROFILE, BINDING CHARACTERISTICS, BIOLOGICAL FUNCTIONS, AND POTENTIAL CLINICAL IMPACT. J. Biol. Chem. 280: 33228-33239 [Abstract] [Full Text]