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Human milk compounds inhibiting adhesion of mutans streptococci to host ligand-coated hydroxyapatite in vitro
Umeå University, Faculty of Medicine, Department of Odontology, Cariology.
Umeå University, Faculty of Medicine, Department of Clinical Sciences, Paediatrics.
Umeå University, Faculty of Medicine, Department of Odontology, Cariology.
2009 (English)In: Caries Research, ISSN 0008-6568, E-ISSN 1421-976X, Vol. 43, no 3, 171-178 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2009. Vol. 43, no 3, 171-178 p.
Keyword [en]
Adhesion of mutans streptococci, casein, human milk, saliva, Streptococcus mutans
National Category
Dentistry
Research subject
Cariology
Identifiers
URN: urn:nbn:se:umu:diva-31698DOI: 10.1159/000213888PubMedID: 19390191OAI: oai:DiVA.org:umu-31698DiVA: diva2:293889
Available from: 2010-02-15 Created: 2010-02-15 Last updated: 2017-12-12Bibliographically approved
In thesis
1. Host ligands and oral bacterial adhesion: studies on phosphorylated polypeptides and gp-340 in saliva and milk
Open this publication in new window or tab >>Host ligands and oral bacterial adhesion: studies on phosphorylated polypeptides and gp-340 in saliva and milk
2010 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Infectious diseases e.g. gastric ulcer, caries and perodontitis, are caused by bacteria in a biofilm. Adhesion of bacteria to host ligands e.g. proteins, polypeptides and glycoproteins, is a key event in biofilm formation and colonization of surfaces such as mucosa and tooth tissues. Thus, host ligands could contribute to the susceptibility to infectious diseases. The general aim of this doctoral thesis was to study the effect of phosphorylated polypeptides and gp-340 in saliva and milk on oral bacterial adhesion and aggregation.

Statherin is a non-glycosylated, phosphorylated polypeptide in saliva. The polypeptide inhibits precipitation and crystal growth of calcium phosphate and mediates adhesion of microorganisms. By using a hybrid peptide construct, the domain for adhesion of Actinomyces isolated from human infections and from rodents was found to reside in the C-terminal end, and the adhesion was inhibitable. With alanine substitution the peptide recognition epitope in the C-terminal end was delineated to Q and TF, where QAATF was an optimal inhibitory peptide. In contrast, human commensal Actinomyces bound to the middle region in a non-inhibitable fashion. Gp-340 is another protein in saliva, and it is a large, multifunctional glycoprotein. Four novel size variants (I-IV) of salivary gp-340 were distinguished within individuals, and their glycoforms were characterized. All four size variants were identical in the N-terminal amino acid sequence and shared core carbohydrates. Low-glyco lung gp-340, high-glyco saliva gp-340, and size variants I-III aggregated bacteria differently. Human milk, which shares many traits with saliva, could inhibit adhesion of Streptococcus mutans to saliva-coated hydroxyapatite (s-HA), a model for teeth, in an individually varying fashion. Human milk caseins, lactoferrin, secretory IgA, and IgG inhibited the binding avidly. By using synthetic peptides the inhibitory epitope in b-casein was mapped to a C-terminal stretch of 30 amino acids. Inhibition by human milk, secretory IgA and the b-casein-derived inhibitory peptide was universal among a panel of mutans streptococci.

The main conclusions are: (i) statherin mediates differential binding of commensal versus infectious Actinomyces strains with small conformation-dependent binding epitopes, (ii) salivary gp-340 has individual polymorphisms that at least affect binding of bacteria, (iii) human milk inhibits S. mutans adhesion to s-HA in an individually varying fashion, and the C-terminal end of human milk β-casein is one inhibitory component. Together these results suggest that the studied host ligands can influence the composition of the oral biofilm. Statherin may protect the host from colonization of bacteria associated with infections. Gp-340 size variants may affect functions related to host innate immune defences such as interactions with a wide array of bacteria, and human milk may have a protective effect in infants from colonization of mutans streptococci.

Place, publisher, year, edition, pages
Umeå: Umeå university, 2010. 66 p.
Series
Umeå University odontological dissertations, ISSN 0345-7532 ; 112
Keyword
Adhesion, statherin, gp-340, caseins, human milk, saliva, Streptococcus mutans, Actinomyces
National Category
Dentistry
Research subject
Cariology
Identifiers
urn:nbn:se:umu:diva-32894 (URN)978-91-7264-969-9 (ISBN)
Public defence
2010-04-22, Sal D Tandläkarhögskolan, Umeå Universitet, Umeå, 09:00 (Swedish)
Opponent
Supervisors
Available from: 2010-03-31 Created: 2010-03-30 Last updated: 2010-03-31Bibliographically approved

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