Affiliation:
1. Department of Oral Science, School of Dentistry, University of Minnesota, 17-252 Moos Tower, 515 Delaware St., SE, Minneapolis, Minnesota 55455, USA
Abstract
Redundancy refers to the observation that many salivary proteins exhibit similar properties in vitro. It is possible that bacterial adherence to salivary pellicle occurs as a cumulative effect of multiple proteins. This study determined the joint and individual contributions of salivary amylase, S-IgA, lysozyme, salivary peroxidase, lactoferrin, and total protein concentrations to adherence by oral viridans streptococci in microplates coated with whole saliva from 123 persons. Strains used were: Streptococcus gordonii Blackburn, 10558, Streptococcus mitis 10712, 903, Streptococcus oralis 10557, 9811, and Streptococcus sanguis 10556, 13379. Rabbit antibody against 13379 was used for the detection of adherence. This antibody cross-reacted with all strains. Absorbance was standardized against saliva pooled from five donors. All saliva samples had been previously assayed for amylase, lactoferrin, lysozyme, secretory IgA, peroxidase, and total protein. Adherence scores for all strains except 13379 were significantly and positively correlated. Salivas binding high or low levels of one strain tended to bind others correspondingly. Multiple regression indicated significant contributions to 10558 adherence from total protein and lactoferrin (positive), and peroxidase and lysozyme (negative). Similar results were obtained for Blackburn and 903. Significant individual correlations were seen for 9811 and total protein (positive), 10557 and peroxidase (negative), and 13379 and lactoferrin (negative). Salivas with high adherence scores contained significantly more protein and lactoferrin, and significantly less peroxidase, than salivas with low adherence scores. These findings support the hypothesis that multiple proteins contribute to the adherence of streptococcal strains in vivo.