Stabilization of the glucan-binding lectin of Streptococcus sobrinus by specific ligand

Cell suspensions of Streptococcus sobrinus can be aggregated by high molecular-weight alpha-1,6 glucans. The aggregation depends on the fidelity of a cell wall-bound, glucan-binding lectin (GBL). It is thought that the lectin may play a part in the sucrose-dependent accretion of streptococci in dental plaques. Results showed that the anionic detergent, sodium dodecyl sulphate (SDS) was a potent inhibitor of the lectin. When cells were incubated in SDS and washed to remove the detergent, lectin activity was diminished. Following incubation of the cells with SDS in the presence of glucan T-10, a low molecular-weight alpha-1,6 glucan, the loss of activity was less pronounced, suggesting that the glucan afforded partial protection against denaturation. Urea and guanidine hydrochloride were good inhibitors of the lectin, but, unlike SDS, were not able to inhibit it irreversibly, except at very high concentrations. Cationic detergents, such as cetylpyridinium bromide (and chloride), also irreversibly denatured the streptococcal lectin, but were not as effective as SDS in abolishing its activity. The results suggest that alpha-1,6 glucan stabilizes the GBL of S. sobrinus, rendering it more resistant to the effect of chaotropes. This may be one reason why dental plaques tend to resist detergents in dentrifices.