Hydrophobic interactions and the adherence of Streptococcus sanguis to hydroxylapatite.

Streptococcus sanguis demonstrated a high affinity for hydrocarbon solvents. When aqueous suspensions of the organism were mixed with either hexadecane or toluene, the cells tended to bind to the nonaqueous solvent. Increases in temperature resulted in a greater affinity of cells for hexadecane. Interaction between the cells and hexadecane was also enhanced by dilute aqueous sodium chloride and by low pH (pH less than 5). The results suggest that the cell surface of S. sanguis has hydrophobic properties. Isolated cell walls also tended to partition into the nonaqueous solvent. Amino acid analyses of the walls revealed the presence of several amino acids which possess hydrophobic side chains. It is likely that the hydrophobic amino acids associated with the cell wall contribute to the hydrophobicity of intact S. sanguis. When the adherence of S. sanguis to saliva-coated hydroxylapatite was measured, it was found that hydrophobic bond-disrupting agents, such as the Li+ cation, the SCN- anion, and sodium dodecyl sulfate, were capable of inhibiting the cell-hydroxylapatite union. In addition, it was observed that both urea and tetramethylurea were inhibitors of the adherence, although the latter reagent was the superior inhibitor. The results suggest that the adherence of S. sanguis to saliva-coated smooth surfaces is at least partially dependent on the formation of hydrophobic bonds between the cell and adsorbed salivary proteins. Hydrophobic bonding may contribute to cooperative interactions involving S. sanguis and saliva-coated hydroxylapatite (Nesbitt et al., Infect. Immun. 35:157-165, 1982).