SALIVA PROTEIN-BINDING TO LAYERS OF ORAL STREPTOCOCCI IN-VITRO AND IN-VIVO

This paper reports a system for measuring saliva protein binding to oral streptococci. Enamel chips with layers of Streptococcus gordonii Blackburn or Streptococcus oralis 10557 were incubated in vitro with whole saliva from eight persons. Blackburn bound significantly more amylase than 10557; no strain differences were seen for lysozyme or lactoferrin. There were significant correlations between saliva and bound amylase and lactoferrin. Blackburn and 10557 chips were then placed in ten subjects. Sites included the buccal left and right upper premolars and molars (UL, UR), labial upper central incisors (UC), and lingual lower central incisors (LL). That study was repeated three months later; chips with Streptococcus sanguis 13379 were also placed then. Blackburn bound significantly more amylase than the other strains. Blackburn and 10557 both bound the most amylase at UL and UR, and the least amylase at UC. However, strain 13379 bound less amylase at UL. That strain also bound significantly less sIgA at UL. All three strains bound the least sIgA at UC. Lysozyme and lactoferrin binding showed few differences among sites or strains. Bound protein concentrations were significantly correlated across sites and strains within subjects, but not correlated with whole saliva. Strain differences may reflect species differences in amylase binding, or differences in species-specific sIgA titers. Site differences may indicate local variation in protein availability. Differences between chip correlations with whole saliva in vitro and in vivo suggest that the salivary film may be modified as it flows over tooth surfaces.