title: 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.
authors.affiliation: Department of Cariology, Faculty of Odontology, Göteborg University, Sweden.
authors.forename: A
authors.initials: A
authors.lastname: Carlén
authors.forename: P
authors.initials: P
authors.lastname: Bratt
authors.forename: C
authors.initials: C
authors.lastname: Stenudd
authors.forename: J
authors.initials: J
authors.lastname: Olsson
authors.forename: N
authors.initials: N
authors.lastname: Strömberg
mesh_terms: D000190:Actinomyces / Q000254:growth & development / Q000502:physiology; D000328:Adult; D000373:Agglutinins / Q000032:analysis* / Q000502:physiology; D001422:Bacterial Adhesion; D002648:Child; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D015169:Colony Count, Microbial; D003773:Dental Plaque / Q000382:microbiology; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006023:Glycoproteins / Q000032:analysis / Q000502:physiology; D006801:Humans; D010455:Peptides / Q000032:analysis* / Q000502:physiology; D010750:Phosphoproteins / Q000032:analysis* / Q000502:physiology; D011392:Proline / Q000032:analysis* / Q000502:physiology; D055232:Proline-Rich Protein Domains; D012471:Salivary Proteins and Peptides / Q000032:analysis* / Q000502:physiology; D013291:Streptococcus / Q000254:growth & development / Q000502:physiology; D013295:Streptococcus mutans / Q000254:growth & development / Q000502:physiology*; D014070:Tooth / Q000382:microbiology*
chemical_list: D000373:Agglutinins; D006023:Glycoproteins; D010455:Peptides; D010750:Phosphoproteins; D012471:Salivary Proteins and Peptides; D011392:Proline