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Infect Immun. 1984 February; 43(2): 656-663

Adherence of Streptococcus sanguis to saliva-coated hydroxyapatite: evidence for two binding sites.

E J Morris and B C McBride

ABSTRACT

The characteristics of bacterial adherence to saliva-coated hydroxyapatite were examined for a salivary aggregating strain of Streptococcus sanguis, strain 12, and for its nonaggregating variant, strain 12na. Both strains were found to adhere in similar numbers to saliva-coated hydroxyapatite that had been preincubated at 4 degrees C overnight. Preincubation of saliva-coated hydroxyapatite overnight at 37 degrees C reduced subsequent adherence of S. sanguis 12 by approximately 10%, whereas adherence of S. sanguis 12na was reduced by over 80%. Preincubation at 37 degrees C in the presence of neuraminidase reduced adherence of S. sanguis 12 by over 90% and caused some additional reduction in adherence of S. sanguis 12na. The data were analyzed with Langmuir isotherms, Scatchard plots, and Hill plots. Some evidence of cooperativity was seen. A peak in the Scatchard plot for S. sanguis 12 binding to saliva-coated hydroxyapatite preincubated at 4 degrees C disappeared after preincubation at 37 degrees C, suggesting the loss of a salivary receptor. Many more organisms were found to bind when adherence was measured by assays counting the number of organisms remaining in suspension after the beads had settled. These weakly binding organisms, which were removed by washing, demonstrated adherence characteristics similar to those of the firmly bound organisms. Both strains were strongly hydrophobic. It is proposed that the binding of S. sanguis 12 and 12na involves two types of receptor on the salivary pellicle. One type of receptor is stable at 37 degrees C, but sensitive to neuraminidase; the second type is inactivated by prolonged incubation at 37 degrees C. S. sanguis 12 may bind to both types of receptor, whereas S. sanguis 12na binds only to the second type. The neuraminidase-sensitive receptor might be involved in saliva-mediated aggregation.

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Infect Immun. 1984 February; 43(2): 656-663

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