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

Abstract

Bacterial binding to salivary proteins may in part account for individual differences in the colonization of tooth surfaces. High-molecular-weight glycoproteins, agglutinins, mediate S. mutans adherence, whereas acidic proline-rich proteins mediate adherence of other early-colonizing streptococci and Actinomyces. 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 a 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 blocked 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. mutans binding salivas mediated binding of A. naeslundii strain LY7 to a greater extent than 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 APRPs. Low A. naeslundii binding coincided with an almost two-fold higher ratio of 106/150 APRPs compared with the high A. naeslundii 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. mutans 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.

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

“…supplemented with a human erythrocyte suspension (30 ml/l) at 37°C in a nitrogen atmosphere with 5% CO 2 and 10% H 2 or in an atmosphere with 5% CO 2 cells/ml) to salivary protein PRP-1 and coating of hydroxyapatite beads (5 mg) (Fluka, Chemie AG, Buchs, Switzerland) with saliva were done as previously described (7,14). Inhibition experiments with ArgGlyArgProGln and lactose were performed with 10 8 bacterial cells/ml and 4 mg of hydroxyapatite beads.…”

“…Acidic PRPs, but not statherin, are also present in rats (2,33) and hamsters (31). Acidic PRPs are highly polymorphic and multifunctional proteins that may determine host susceptibility and resistance to dental caries (3,7,26,44,53). While acidic PRPs promote avid adhesion of commensal species, such as A. naeslundii (14) and Streptococcus gordonii (15), statherin promotes the adhesion of potentially invasive species, such as Porphyromonas gingivalis (1) and Candida albicans (6,21).…”

Salivary microbial and nonmicrobial parameters in children with fixed orthodontic appliances

“…8 Although numerous studies of salivary function have used different methods to measure salivary function and corresponding microbial interactions, a relationship between salivary functions and outcomes related to bacterial counts in saliva or plaque or caries has been shown but not explained. [9][10][11] This may be attributable to a lack of data on a person's salivary function in healthy state, so that it is difficult to determine how the salivary function adjusts to new intraoral circumstances, such as placement of fixed orthodontic appliances.…”

Nanoscale Adhesion Forces between Enamel Pellicle Proteins and Hydroxyapatite

“…These results confirm that proteins with high affinity to HA, such as histatins, show strong molecular adhesive forces. Conversely, albumin is a salivary protein that does not exhibit high affinity for HA (Carlen et al, 1998), and thus does not demonstrate adhesion forces to HA as largely as those found for H5.…”