title: Human milk compounds inhibiting adhesion of mutans streptococci to host ligand-coated hydroxyapatite in vitro.
abstract: Acquisition of mutans streptococci at an early age is a risk factor for later caries development. Following our recent finding that human milk may inhibit adhesion of Streptococcus mutans the aim of the present study was to identify compounds in human milk preventing adhesion of mutans streptococci to saliva- or gp340-coated hydroxyapatite (s-HA and gp340-HA) using an in vitro model system. Superdex 200 fractions of human milk and purified proteins were screened for binding inhibition of the S. mutans strain Ingbritt. Avid inhibition was seen to both s-HA and gp340-HA for caseins, lactoferrin, IgA and IgG, and moderate inhibition for alpha-lactalbumin and bile salt-stimulated lipase, whereas albumin and lysozyme had no effect. The inhibitory epitope in beta-casein was delineated to its C-terminal LLNQELLNPTHQIYPVTQPLAPVHNPISV stretch by use of synthetic peptides. Similarly, a peptide (SCKFDEYFSQSCA) corresponding to the human lactoferrin stretch that is highly homologous to the previously shown inhibitory stretch of bovine lactoferrin was found to inhibit S. mutans Ingbritt binding. Inhibition by human milk, IgA, and the inhibitory beta-casein peptide was universal among 4 strains of S. mutans (Ingbritt, NG8, LT11, JBP) and 2 strains of S. sobrinus (6715 and OMZ176). IgG inhibited 4, alpha-lactalbumin 3 and lactoferrin 2 of these 6 strains. It was also confirmed that none of the milk components coated on HA mediated S. mutans Ingbritt adhesion, which was consistent with the finding that no milk protein was recognized on Western blots by gp340/DMBT1 monoclonal antibodies.
authors.affiliation: Department of Odontology/Cariology, Umeå University, Umeå, Sweden.
authors.forename: L
authors.initials: L
authors.lastname: Danielsson Niemi
authors.forename: O
authors.initials: O
authors.lastname: Hernell
authors.forename: I
authors.initials: I
authors.lastname: Johansson
mesh_terms: D000328:Adult; D000418:Albumins / Q000494:pharmacology; D001422:Bacterial Adhesion / Q000187:drug effects*; D002135:Calcium-Binding Proteins; D002364:Caseins / Q000494:pharmacology; D002614:Chelating Agents / Q000494:pharmacology; D020099:Coated Materials, Biocompatible / Q000737:chemistry; D004268:DNA-Binding Proteins; D044622:Dental Pellicle / Q000737:chemistry; D017886:Durapatite / Q000737:chemistry; D000939:Epitopes; D005260:Female; D006801:Humans; D007071:Immunoglobulin A, Secretory / Q000494:pharmacology; D007074:Immunoglobulin G / Q000494:pharmacology; D007768:Lactalbumin / Q000494:pharmacology; D007781:Lactoferrin / Q000494:pharmacology; D008024:Ligands; D008894:Milk Proteins / Q000494:pharmacology*; D008895:Milk, Human / Q000737:chemistry* / Q000502:physiology; D009113:Muramidase / Q000494:pharmacology; D011956:Receptors, Cell Surface / Q000737:chemistry; D002787:Sterol Esterase / Q000494:pharmacology; D013295:Streptococcus mutans / Q000145:classification / Q000187:drug effects*; D016986:Streptococcus sobrinus / Q000145:classification / Q000187:drug effects*; D025521:Tumor Suppressor Proteins
chemical_list: D000418:Albumins; D002135:Calcium-Binding Proteins; D002364:Caseins; D002614:Chelating Agents; D020099:Coated Materials, Biocompatible; C108174:DMBT1 protein, human; D004268:DNA-Binding Proteins; D000939:Epitopes; D007071:Immunoglobulin A, Secretory; D007074:Immunoglobulin G; D008024:Ligands; D008894:Milk Proteins; D011956:Receptors, Cell Surface; D025521:Tumor Suppressor Proteins; D007768:Lactalbumin; D017886:Durapatite; C054784:bile salt-stimulated lipase; D002787:Sterol Esterase; D009113:Muramidase; D007781:Lactoferrin