Characterization of preparations enriched for Streptococcus mutans fimbriae: salivary immunoglobulin A antibodies in caries-free and caries-active subjects.

The ability of bacteria to adhere to salivary pellicle-coated enamel tooth surfaces is a critical step in oral bacterial colonization. Oral bacteria adhere to receptors of host origin in salivary pellicle. Streptococcus mutans has been identified as the major etiological agent of human dental caries and composes a significant proportion of the oral streptococci in carious lesions. Bacterial fimbriae are small (100 to 300 nm) hairlike appendages emanating from the cell surface. Preparations enriched for S. mutans fimbriae were isolated by a shearing technique and alternating high- and low-speed centrifugations. A representative fimbrial preparation had two distinct double bands comprising four proteins of approximately 100 to 200 kDa and one faint band at 40 kDa on reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis/immunoblots and had demonstrable glucosyltransferase activity. Rabbit antisera raised against the preparation specifically stained the fuzzy coat of S. mutans, demonstrating short fimbria-like structures protruding 100 to 200 nm from the cell surface. Controls without antifimbria antibody did not exhibit this staining. There were significantly higher (P < or = 0.05) levels of salivary immunoglobulin A, but not serum immunoglobulin G, antibodies to the enriched S. mutans fimbria preparation by enzyme-linked immunosorbent assay from caries-free subjects than from caries-active subjects. The results suggest that S. mutans fimbriae may be an important adherence factor to which caries-free subjects mount a protective salivary immune response.