Further characteristics of beta2-microglobulin binding to oral streptococci.

A total of 85 strains of oral bacteria representing Streptococcus mutans, S. sanguis, S. Mitior, S. salivarious, S. milleri, S. infrequens, S. durans, S. lactis, S. faecalis, S. faecium, S. equinus, Streptococcus species group E, Actinomyces, and one group A Streptococcus were tested for binding of aggregated human beta 2-microglobulin. Positive affinity between bacteria and aggregated human beta 2-microglobulin was detected in 36% of the strains. No apparent correlation with bacterial species, serotype, or group was noted. No positive strains were detected among seven group I:A S. sanguis strains (P < 0.01). Binding constants for one S. mutans strain indicated heterogeneous binding structures on the bacterial surface. The number of binding sites for aggregates of human beta 2-microglobulin involving multipoint attachment varied from 70 to 1,700 per bacterial cell. With whole saliva as buffer, a general increase in affinity was seen. Variations in salt concentrations of the buffers revealed different salt-dependent species-associated uptake patterns. Oral bacteria tended to have an uptake maximum at a salt concentration similar to that seen in saliva. Binding structures for aggregated beta 2-microglobulin on oral streptococci were sensitive to pepsin, heat, and formaldehyde treatment. Bacterial binding structures for aggregated beta 2-microglobulin might represent one of several factors of importance for bacterial attachment in the oral cavity. Experimental conditions reflecting the salivary milieu increased the degree of interaction, emphasizing the importance of physiological test systems for such studies.