title: Different type 1 fimbrial genes and tropisms of commensal and potentially pathogenic Actinomyces spp. with different salivary acidic proline-rich protein and statherin ligand specificities.
abstract: Actinomyces spp. exhibit type 1 fimbria-mediated adhesion to salivary acidic proline-rich proteins (PRPs) and statherin ligands. Actinomyces spp. with different animal and tissue origins belong to three major adhesion types as relates to ligand specificity and type 1 fimbria genes. (i) In preferential acidic-PRP binding, strains of Actinomyces naeslundii genospecies 1 and 2 from human and monkey mouths displayed at least three ligand specificities characterized by preferential acidic-PRP binding. Slot blot DNA hybridization showed seven highly conserved type 1 fimbria genes (orf1- to -6 and fimP) in genospecies 1 and 2 strains, except that orf5 and orf3 were divergent in genospecies 1. (ii) In preferential statherin binding, oral Actinomyces viscosus strains of rat and hamster origin (and strain 19246 from a human case of actinomycosis) bound statherin preferentially. DNA hybridization and characterization of the type 1 fimbria genes from strain 19246 revealed a homologous gene cluster of four open reading frames (orfA to -C and fimP). Bioinformatics suggested sortase (orfB, orf4, and part of orf5), prepilin peptidase (orfC and orf6), fimbria subunit (fimP), and usher- and autotransporter-like (orfA and orf1 to -3) functions. Those gene regions corresponding to orf3 and orf5 were divergent, those corresponding to orf2, orf1, and fimP were moderately conserved, and those corresponding to orf4 and orf6 were highly conserved. Restriction fragment length polymorphism analyses using a fimP probe separated human and monkey and rat and hamster strains into phylogenetically different groups. (iii) In statherin-specific binding, strains of A. naeslundii genospecies 1 from septic and other human infections displayed a low-avidity binding to statherin. Only the orf4 and orf6 gene regions were highly conserved. Finally, rat saliva devoid of statherin bound bacterial strains avidly irrespective of ligand specificity, and specific antisera detected either type 1, type 2, or both types of fimbria on the investigated Actinomyces strains.
authors.affiliation: Department of Odontology/Cariology, Umeå University, SE-901 87 Umeå, Sweden.
authors.forename: T
authors.initials: T
authors.lastname: Li
authors.forename: M K
authors.initials: MK
authors.lastname: Khah
authors.forename: S
authors.initials: S
authors.lastname: Slavnic
authors.forename: I
authors.initials: I
authors.lastname: Johansson
authors.forename: N
authors.initials: N
authors.lastname: Strömberg
mesh_terms: D000190:Actinomyces / Q000235:genetics* / Q000472:pathogenicity*; D016924:Actinomyces viscosus / Q000235:genetics / Q000472:pathogenicity; D000818:Animals; D001422:Bacterial Adhesion / Q000235:genetics*; D006224:Cricetinae; D019143:Evolution, Molecular; D010861:Fimbriae, Bacterial / Q000145:classification / Q000235:genetics*; D005798:Genes, Bacterial; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010455:Peptides / Q000378:metabolism; D011110:Polymorphism, Genetic; D055232:Proline-Rich Protein Domains; D051381:Rats; D055273:Salivary Proline-Rich Proteins; D012471:Salivary Proteins and Peptides / Q000378:metabolism*; D017422:Sequence Analysis, DNA; D013045:Species Specificity
chemical_list: D008024:Ligands; C524536:PRH1 protein, human; D010455:Peptides; C018149:STATH protein, human; D055273:Salivary Proline-Rich Proteins; D012471:Salivary Proteins and Peptides