Interaction between surface protein antigens of Streptococcus mutans and human salivary components.

The potential involvement of surface antigens (Ags) I/II and III of Streptococcus mutans in its adherence to salivary pellicle-coated tooth surfaces was investigated. The binding of radiolabelled Ag I/II to hydroxyapatite was increased by pretreating the mineral with human parotid saliva, and binding was maintained in the continuous presence of saliva. Binding of Ag III to hydroxyapatite was inhibited by pretreatment with, or in the presence of, saliva. Various aminohexoses, and also tris, inhibited the binding of Ag I/II. When Ags I/II and III were tested for their ability to bind to salivary components separated by SDS gel electrophoresis, several proteins capable of binding Ag I/II were identified, notably 2 proteins of apparent relative molecular mass 28,000 and 38,000. Analysis of these proteins, isolated by micro-preparative electrophoresis, indicated high proportions of proline, glycine, and glutamic acid, and overall compositions similar to basic proline-rich salivary proteins.