Calcium-dependent salivary agglutinin with reactivity to various oral bacterial species.

Human parotid agglutinins from three individuals were isolated by adsorption to and desorption from strains of Streptococcus mutans belonging to serotypes a, b, c, d, and e and strains of Lactobacillus casei, Actinomyces viscosus, and Streptococcus sanguis. The desorption was achieved by suspending centrifuged saliva-coated microorganisms in 10 mM phosphate buffer (pH 6.8) containing 0.154 M sodium chloride. After another centrifugation, agglutinin activity was recovered in the supernatants. The L. casei strain was not agglutinated by any of the agglutinin extracts or by saliva, but all the other strains were agglutinated to a variable extent. However, all strains, including the nonagglutinating L. casei strain, adsorbed and desorbed agglutinins active for other strains. The agglutinin extracts from S. mutans serotype c, S. sanguis, and A. viscosus were purified and characterized by electrophoretic and immunological techniques. The purified preparations were positively stained for protein and carbohydrate, and the molecular weights were estimated to be 440,000. All agglutinin extracts needed calcium in the range of 0.1 to 0.5 mM to be active, and for a single strain, all agglutinins gave the same degree of agglutination, indicating that the isolated agglutinins may be of the same molecular species, a hypothesis that was also confirmed by the preliminary characterization of the purified agglutinins. This type of agglutinin, which seems to exert its activity among various bacterial species, could be important in mediating bacterial coaggregation and thus may add to the effect of specific agglutinins in the clearance of bacteria from the human mouth.