This Article Full Text (PDF) References Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Add to Saved Citations Download to citation manager Request Permissions Request Reprints Add to My Marked Citations Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Citing Articles via Scopus Google Scholar Articles by Carlén, A. Articles by Strömberg, N. Search for Related Content PubMed PubMed Citation Articles by Carlén, A. Articles by Strömberg, N. Social Bookmarking                         What's this?

Agglutinin and Acidic Proline-rich Protein Receptor Patterns May Modulate Bacterial Adherence and Colonization on Tooth Surfaces

Department of Cariology, Faculty of Odontology, Göteborg University, Medicinaregatan 12, S-413 90 Göteborg

P. Bratt

Department of Cariology, Faculty of Odontology, UmeÅ University, S-901 87 UmeÅ, Sweden

C. Stenudd

Department of Cariology, Faculty of Odontology, UmeÅ University, S-901 87 UmeÅ, Sweden

J. Olsson

Department of Cariology, Faculty of Odontology, Göteborg University, Medicinaregatan 12, S-413 90 Göteborg

N. Strömberg

Department of Cariology, Faculty of Odontology, UmeÅ University, S-901 87 UmeÅ, Sweden

Bacterial binding to salivary proteins may in part account for individual differences in the colonization of tooth surface. High-motecular-weight glycoproteins, agglutinins, mediate S. mutans adherence, whereas acidic proline-rich proteins mediate adherence of other early-colonizing streptococci and Actinemyces. The aim of the present study was to examine the composition of adherence-related salivary proteins and dental plaque micro-organisms in three individuals with a low, moderate, and high capacity to mediate S. mutans adherence. The S. mutans (strain Ingbritt) binding activity resided with 300-kDa agglutinin which was six-fold more prevalent in the high S. mutans binding saliva compared with the low one. Binding to all three salivas was completely by a monoclonal anti-agglutinin antibody. The moderate S. mutans binding saliva was found to contain adherence-inhibiting components. Furthermore, the low and moderate S. mutant binding salivas mediated binding of A. naeslundii strain LY7 to a greater extent the saliva with high S. mutans binding. The A. naeslundii binding activity resided with the acidic proline-rich proteins (APRPS) and paralleled the relative content of 106- and 150-residue A-PRPS. Low A. naeslundii binding coincided with an almost two-fold higher ratio of 106/150 APRPs compared the high A. naestundii binding saliva. During conventional gel filtration, a degradation of the acidic, basic, and glycosylated proline-rich proteins was evident in the saliva with high S. mutatis and low A. naeslundii binding. This saliva donor had a comparably high rate of dental plaque formation, high counts of S. mutans, and low counts of other streptococci and Actinomyces.

Key Words: saliva • adherence • acidic proline-rich proteins • agglutinins • S. mutant, A. naeslundii.

Journal of Dental Research, Vol. 77, No. 1, 81-90 (1998)
DOI: 10.1177/00220345980770011301


CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				M.-R. Sarrias, S. Rosello, F. Sanchez-Barbero, J. M. Sierra, J. Vila, J. Yelamos, J. Vives, C. Casals, and F. Lozano A Role for Human SP{alpha} as a Pattern Recognition Receptor J. Biol. Chem., October 21, 2005; 280(42): 35391 - 35398. [Abstract] [Full Text] [PDF]

				F. J. Bikker, A. J. M. Ligtenberg, C. End, M. Renner, S. Blaich, S. Lyer, R. Wittig, W. van't Hof, E. C. I. Veerman, K. Nazmi, et al. Bacteria Binding by DMBT1/SAG/gp-340 Is Confined to the VEVLXXXXW Motif in Its Scavenger Receptor Cysteine-rich Domains J. Biol. Chem., November 12, 2004; 279(46): 47699 - 47703. [Abstract] [Full Text] [PDF]

				T. Oho, F. J. Bikker, A. V. Nieuw Amerongen, and J. Groenink A Peptide Domain of Bovine Milk Lactoferrin Inhibits the Interaction between Streptococcal Surface Protein Antigen and a Salivary Agglutinin Peptide Domain Infect. Immun., October 1, 2004; 72(10): 6181 - 6184. [Abstract] [Full Text] [PDF]

				T. Li, M. K. Khah, S. Slavnic, I. Johansson, and N. Stromberg Different Type 1 Fimbrial Genes and Tropisms of Commensal and Potentially Pathogenic Actinomyces spp. with Different Salivary Acidic Proline-Rich Protein and Statherin Ligand Specificities Infect. Immun., December 1, 2001; 69(12): 7224 - 7233. [Abstract] [Full Text] [PDF]

				R. L. Gregory Modified Immunogenicity of a Mucosally Administered Antigen Clin. Vaccine Immunol., May 1, 2001; 8(3): 540 - 544. [Abstract] [Full Text] [PDF]

				J.D. Rudney Saliva and Dental Plaque Advances in Dental Research, December 1, 2000; 14(1): 29 - 39. [Abstract] [PDF]

				T. Li, P. Bratt, A. P. Jonsson, M. Ryberg, I. Johansson, W. J. Griffiths, T. Bergman, and N. Stromberg Possible Release of an ArgGlyArgProGln Pentapeptide with Innate Immunity Properties from Acidic Proline-Rich Proteins by Proteolytic Activity in Commensal Streptococcus and Actinomyces Species Infect. Immun., September 1, 2000; 68(9): 5425 - 5429. [Abstract] [Full Text] [PDF]

				P. Bratt, D. Boren, T. Boren, and N. Stromberg Secretory Immunoglobulin A Heavy Chain Presents Gal{beta}1-3GalNAc Binding Structures for Actinomyces naeslundii genospecies 1 Journal of Dental Research, June 1, 1999; 78(6): 1238 - 1244. [Abstract] [PDF]

				A. Prakobphol, F. Xu, V. M. Hoang, T. Larsson, J. Bergstrom, I. Johansson, L. Frangsmyr, U. Holmskov, H. Leffler, C. Nilsson, et al. Salivary Agglutinin, Which Binds Streptococcus mutans and Helicobacter pylori, Is the Lung Scavenger Receptor Cysteine-rich Protein gp-340 J. Biol. Chem., December 15, 2000; 275(51): 39860 - 39866. [Abstract] [Full Text] [PDF]