Adhesion of oral streptococci to experimental bracket pellicles from glandular saliva.

The aim of this study was to evaluate the functions of bracket pellicles as the binding receptors for Streptococcus mutans and Streptococcus gordonii. Four different types of orthodontic brackets were used: stainless steel, monocrystalline sapphire, polycrystalline alumina, and plastic. The bracket pellicles were formed by incubating orthodontic brackets with fresh submandibular-sublingual saliva or parotid saliva for 2 hours. The pellicles were extracted, and their components were confirmed by gel electrophoresis, immunodetection, and amino acid composition analysis. The roles of the bracket pellicles in the adhesion of oral streptococci were evaluated by incubating tritium-labeled streptococci with pellicle-transfer blots. The results showed that the salivary components adhered selectively according to type of bracket and glandular saliva. The selective adsorption was also proven by the amino acid composition profiles. Among the several salivary proteins, MG2, alpha-amylase, and the acidic proline-rich proteins provided the binding sites for S gordonii. However, none of these proteins in the bracket pellicles contributed to the adhesion of S mutans. These findings suggest that numerous salivary proteins can adhere selectively to the orthodontic brackets, and some of them contribute to the binding of S gordonii.