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Clinical and Diagnostic Laboratory Immunology, Nov 1995, 719-725, Vol 2, No. 6
M Fontana, LE Gfell and RL Gregory
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.
Copyright © 1995 by the American Society for Microbiology. All rights reserved.
Characterization of preparations enriched for Streptococcus mutans fimbriae: salivary immunoglobulin A antibodies in caries-free and caries-active subjects
Department of Oral Biology, Indiana University, Indianapolis 46202, USA.
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