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Salivary statherin peptide-binding epitopes of commensal and potentially infectious Actinomyces spp. delineated by a hybrid peptide construct
Umeå universitet, Medicinsk fakultet, Odontologi, Kariologi.
Umeå universitet, Medicinsk fakultet, Odontologi, Kariologi.
2004 (engelsk)Inngår i: Infection and Immunity, ISSN 0019-9567, E-ISSN 1098-5522, Vol. 72, nr 2, s. 782-787Artikkel, forskningsoversikt (Fagfellevurdert) Published
Abstract [en]

Adhesion of microorganisms to host receptor molecules such as salivary statherin molecules is a common event in oral microbial colonization. Here we used a hybrid peptide construct (with both a hydroxyapatite-binding portion and a test peptide portion) to map the interaction of Actinomyces species (and Candida albicans) with statherin. Adhesion to hybrid peptides and truncated statherin variants revealed three binding types, types I to III. (i) Type I strains of rat, hamster, and human infection origins bound C-terminal-derived QQYTF and PYQPQY peptides. The QQYTF peptide inhibited statherin binding for some strains but not for others. (ii) Type II strains of human and monkey tooth origins bound middle-region-derived YQPVPE and QPLYPQ peptides. Neither strain was inhibited by soluble peptides. (iii) Type III strains of human infection origins (and C. albicans) did not bind to either statherin-derived peptides or truncated statherin. Moreover, the type I strains inhibited by QQYTF were also inhibited by TF and QAATF peptides and were detached from statherin by the same peptides. In conclusion, it is suggested that commensal and potentially infectious microorganisms bind middle or C-terminal statherin differently and that other microbes might require discontinuous epitopes.

sted, utgiver, år, opplag, sider
2004. Vol. 72, nr 2, s. 782-787
HSV kategori
Forskningsprogram
kariologi
Identifikatorer
URN: urn:nbn:se:umu:diva-16969DOI: 10.1128/IAI.72.2.782-787.2004PubMedID: 14742521OAI: oai:DiVA.org:umu-16969DiVA, id: diva2:156642
Tilgjengelig fra: 2007-10-25 Laget: 2007-10-25 Sist oppdatert: 2018-06-09bibliografisk kontrollert
Inngår i avhandling
1. Host ligands and oral bacterial adhesion: studies on phosphorylated polypeptides and gp-340 in saliva and milk
Åpne denne publikasjonen i ny fane eller vindu >>Host ligands and oral bacterial adhesion: studies on phosphorylated polypeptides and gp-340 in saliva and milk
2010 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
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.

sted, utgiver, år, opplag, sider
Umeå: Umeå university, 2010. s. 66
Serie
Umeå University odontological dissertations, ISSN 0345-7532 ; 112
Emneord
Adhesion, statherin, gp-340, caseins, human milk, saliva, Streptococcus mutans, Actinomyces
HSV kategori
Forskningsprogram
kariologi
Identifikatorer
urn:nbn:se:umu:diva-32894 (URN)978-91-7264-969-9 (ISBN)
Disputas
2010-04-22, Sal D Tandläkarhögskolan, Umeå Universitet, Umeå, 09:00 (svensk)
Opponent
Veileder
Tilgjengelig fra: 2010-03-31 Laget: 2010-03-30 Sist oppdatert: 2010-03-31bibliografisk kontrollert

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