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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


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