Monoclonal antibodies against a high-molecular-weight agglutinin block adherence to experimental pellicles on hydroxyapatite and aggregation of Streptococcus mutans.

High-molecular-weight (HMW) glycoproteins, agglutinins, in parotid saliva induce the aggregation of S. mutans and mediate binding of the bacteria to saliva-coated hydroxyapatite (SHA). Two types of monoclonal antibodies (mAb) directed against, respectively, protein and carbohydrate epitopes on the agglutinin have been reported to inhibit the aggregation of S. mutans. In this study, the mAbs were tested for their ability to block aggregation and adherence to SHA of S. mutans serotype c mediated by parotid, submaxillary, and whole saliva from three subjects. Both types of antibody inhibited the adherence and aggregation in a dose-dependent manner. However, individual variations were noted for the effects of the antibodies. Sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) and subsequent immunoblotting with the antibodies revealed a > 300 kDa agglutinin component in all types of saliva and in the proteins desorbed from SHA. The degree of staining of this component in immunoblots of the salivas and the desorbates seemed to be paralleled by the rates of aggregation and adherence, respectively. Thus, our results indicate that the adherence to SHA as well as the aggregation of S. mutans serotype c is primarily mediated by structurally related, HMW glycoproteins in parotid, submaxillary, and whole saliva.