title: Salivary proteins promote proteolytic activity in Streptococcus mitis biovar 2 and Streptococcus mutans.
abstract: A major function of the salivary pellicle on oral surfaces is to promote colonization of the commensal microbiota by providing binding sites for adherence. Streptococcus mitis is an early colonizer of the oral cavity whereas Streptococcus mutans represents a later colonizer. To survive and grow, oral bacteria produce enzymes, proteases and glycosidases, which allow them to exploit salivary proteins as a nutrient source. In this study, adherence and proteolytic activity of S. mitis biovar 2 and S. mutans were investigated in a flow-cell model in the presence of different populations of surface-associated salivary proteins. Streptococcus mitis biovar 2 adhered well to surfaces coated with both a MUC5B-enriched fraction and a pool of low-density proteins containing MUC7, amylase, cystatin, gp340, immunoglobulin A, lactoferrin, lysozyme and statherin, whereas adherence of S. mutans to these proteins was poor. In environments of MUC5B or the low-density proteins, both S. mitis biovar 2 and S. mutans showed high levels of proteolytic activity. For S. mitis in the MUC5B environment, most of this activity may be attributable to contact with the molecules in the fluid phase although activity was also enhanced by adherence to surface-associated MUC5B. These data suggest that although they differ in their capacity to adhere to surface-associated salivary proteins, in the natural environment exploitation of saliva as a nutrient source can contribute to survival and colonization of the oral cavity by both S. mitis biovar 2 and S. mutans.
authors.affiliation: Department of Oral Biology, Faculty of Odontology, Malmö University, Malmö, Sweden.
authors.forename: C
authors.initials: C
authors.lastname: Kindblom
authors.forename: J R
authors.initials: JR
authors.lastname: Davies
authors.forename: M C
authors.initials: MC
authors.lastname: Herzberg
authors.forename: G
authors.initials: G
authors.lastname: Svensäter
authors.forename: C
authors.initials: C
authors.lastname: Wickström
mesh_terms: D000681:Amylases / Q000378:metabolism; D001422:Bacterial Adhesion / Q000502:physiology*; D002135:Calcium-Binding Proteins; D004268:DNA-Binding Proteins; D044622:Dental Pellicle / Q000378:metabolism* / Q000382:microbiology; D006801:Humans; D007071:Immunoglobulin A, Secretory / Q000378:metabolism; D007781:Lactoferrin / Q000378:metabolism; D018613:Microscopy, Confocal; D055257:Mucin-5B / Q000378:metabolism; D009077:Mucins / Q000378:metabolism; D009113:Muramidase / Q000378:metabolism; D059748:Proteolysis; D011956:Receptors, Cell Surface / Q000378:metabolism; D055333:Salivary Cystatins / Q000378:metabolism; D012471:Salivary Proteins and Peptides / Q000378:metabolism*; D034361:Streptococcus mitis / Q000378:metabolism*; D013295:Streptococcus mutans / Q000378:metabolism*; D025521:Tumor Suppressor Proteins
chemical_list: D002135:Calcium-Binding Proteins; C108174:DMBT1 protein, human; D004268:DNA-Binding Proteins; D007071:Immunoglobulin A, Secretory; C524578:MUC5B protein, human; C083238:MUC7 protein, human; D055257:Mucin-5B; D009077:Mucins; D011956:Receptors, Cell Surface; C018149:STATH protein, human; D055333:Salivary Cystatins; D012471:Salivary Proteins and Peptides; D025521:Tumor Suppressor Proteins; D000681:Amylases; D009113:Muramidase; D007781:Lactoferrin