Salivary statherin peptide-binding epitopes of commensal and potentially infectious Actinomyces spp. delineated by a hybrid peptide construct.
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.
Niemi
Liza Danielsson
LD
Department of Odontology/Cariology, Umeå University, Umeå, Sweden.
Johansson
Ingegerd
I
D000190:Actinomyces / Q000502:physiology*; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D001665:Binding Sites; D000939:Epitopes; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012471:Salivary Proteins and Peptides / Q000737:chemistry* / Q000276:immunology; D013329:Structure-Activity Relationship
D000939:Epitopes; D011993:Recombinant Fusion Proteins; C018149:STATH protein, human; D012471:Salivary Proteins and Peptides