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
T. Li et al., 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, INFEC IMMUN, 69(12), 2001, pp. 7224-7233
Actinomyces spp. exhibit type 1 fimbria-mediated adhesion to salivary acidi
c proline-rich proteins (PRPs) and statherin ligands. Actinomyces spp. with
different animal and tissue origins belong to three major adhesion types a
s relates to ligand specificity and type 1 fimbria genes. (i) In preferenti
al acidic-PRP binding, strains of Actinomyces naeslundii genospecies 1 and
2 from human and monkey mouths displayed at least three ligand specificitie
s characterized by preferential acidic-PRP binding. Slot blot DNA hybridiza
tion showed seven highly conserved type 1 fimbria genes (orf1- to -6 and fi
mP) in genospecies 1 and 2 strains, except that orf5 and orf3 were divergen
t in genospecies 1. (ii) In preferential statherin binding, oral Actinomyce
s viscosus strains of rat and hamster origin (and strain 19246 from a human
case of actinomycosis) bound statherin preferentially. DNA hybridization a
nd 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 autotran
sporter-like (orfA and orf1 to -3) functions. Those gene regions correspond
ing to orf3 and orf5 were divergent, those corresponding to orf2, orf1, and
fimP were moderately conserved, and those corresponding to orf4 and orf6 w
ere highly conserved. Restriction fragment length polymorphism analyses usi
ng a fimP probe separated human and monkey and rat and hamster strains into
phylogenetically different groups. (iii) In statherin-specific binding, st
rains 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 boun
d bacterial strains avidly irrespective of ligand specificity, and specific
antisera detected either type 1, type 2, or both types of fimbria on the i
nvestigated Actinomyces strains.