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PubMed1994

Initial catabolism of sorbitol in Actinomyces naeslundii and Actinomyces viscosus.

The initial steps of sorbitol catabolism were studied in 4 strains of Actinomyces naeslundii and Actinomyces viscosus that had been isolated from human dental plaque. Cell-free extracts were prepared from cells grown in the presence of either sorbitol, xylitol or glucose. The extracts from all strains grown on sorbitol had nicotinamide adenine dinucleotide-linked dehydrogenase activities for sorbitol and xylitol and reduced nicotinamide adenine dinucleotide-linked reductase activities for fructose and xylulose. Two of the strains also exhibited these activities when grown in the presence of xylitol, and all glucose-grown cells lacked them. The results indicate that sorbitol metabolism in oral actinomyces involve oxidation of sorbitol to fructose by an inducible enzyme, nicotinamide adenine dinucleotide-linked sorbitol dehydrogenase. This step is followed by the phosphorylation of fructose with guanosine triphosphate as a main phosphoryl donor. Thus, the initial catabolic pathway of sorbitol in A. naeslundii and A. viscosus is different from those described for other oral bacteria.

Actinomyces↗
PubMed1998

Characterization of Actinomyces turicensis and Actinomyces radingae strains from human clinical samples.

Whole-organism protein electrophoresis was used to compare and group unidentified coryneform bacteria resembling Gardnerella vaginalis and various Actinomyces and Arcanobacterium species. The obtained clusters of strains were further characterized by whole-cell fatty acid analysis and a variety of biochemical tests. Species-specific oligonucleotide probes based on 16S rRNA gene sequences were designed. The results demonstrate that the majority of the isolates belonged to Actinomyces turicensis; the other strains belonged to Actinomyces radingae. The descriptions of both species are emended.

Actinomyces↗
PubMed1982

Reclassification of Corynebacterium pyogenes (Glage) in the genus Actinomyces, as Actinomyces pyogenes comb.nov.

Corynebacterium pyogenes (Glage) differs to such an extent from the type species of Corynebacterium, Corynebacterium diphtheriae (Lehmann and Neumann), that it cannot be retained in this genus. Numerical phenetic and chemical data indicate a close relationship between Corynebacterium pyogenes and the species Actinomyces bovis (Harz). It is proposed that Corynebacterium pyogenes be reclassified in the genus Actinomyces, as Actinomyces pyogenes (Glage) comb.nov.

Actinomyces↗
PubMed1998

Actinomyces naeslundii genospecies 1 and 2 express different binding specificities to N-acetyl-beta-D-galactosamine, whereas Actinomyces odontolyticus expresses a different binding specificity in colonizing the human mouth.

A total of 102 strains of Actinomyces were isolated from teeth, buccal mucosa and tongue in eight individuals. The isolates were characterized by multivariate statistical analyses of phenotypic characteristics, serotyping and binding to beta-linked galactosamine (N-acetyl-beta-D-galactosamine) and acidic proline-rich protein structures. Based on these characteristics, isolates were classified into three major groups: (i) Isolates of Actinomyces naeslundii genospecies 2 were the dominant species on teeth and buccal mucosa and bound commonly to N-acetyl-beta-D-galactosamine (63 of 63 isolates) and acidic proline-rich proteins (63 of 63 isolates), regardless of tissue origin. They all exhibited a N-acetyl-beta-D-galactosamine binding specificity signified by N-acetyl-beta-D-galactosamine-inhibitable coaggregation with the streptococcal strains LVG1, GVE1, 24892 and MPB1; (ii) Isolates of A. naeslundii genospecies 1 were prevalent on teeth in certain individuals and bound commonly to N-acetyl-beta-D-galactosamine (20 of 20 isolates), but less commonly to acidic proline-rich proteins (5 of 20 isolates). They all possessed another N-acetyl-beta-D-galactosamine specificity, i.e. N-acetyl-beta-D-galactosamine-inhibitable coaggregation with the same streptococcal strains except for strain MPB1; (iii) Isolates of Actinomyces odontolyticus, the dominant species on the tongue (17 of 19 isolates), bound commonly to unknown structures on streptococci (17 of 19 isolates) but rarely to N-acetyl-beta-D-galactosamine (2 of 19 isolates) or acidic proline-rich proteins (3 of 19 isolates). In conclusion, A. naeslundii genospecies 1 and 2 exhibit different patterns of N-acetyl-beta-D-galactosamine and acidic proline-rich protein specificities to colonize dental and buccal mucosa surfaces, whereas A. odontolyticus utilizes another specificity to colonize the tongue.

Acetylgalactosamine↗
PubMed1983

Actinomyces viscosus and Actinomyces naeslundii agglutinins in human saliva.

The objectives were to determine the degree of Actinomyces agglutinating activity in human saliva and to begin characterizing the agglutination mechanism. Agglutination titres of whole saliva collected from adults and 6-yr-old children were compared. Titres for A. naeslundii were always higher than for A. viscosus. The mean A. naeslundii titre for the adults' and children's samples were equivalent. The children had a slightly lower mean titre than the adults for A. viscosus. No correlation was found between IgA concentrations and agglutination titre. Agglutinating activity was partially impaired by incubation with anti-IgA serum. Activity in submandibular/sublingual saliva was resistant to heat at 56 degrees C but sensitive to boiling. Boiling the bacteria had no effect. In sugar inhibition tests, only galactosides (beta-Gal) and glucosamine (for A. viscosus) affected Actinomyces agglutination but impairment was only temporary. Agglutinating activity was diminished by incubating saliva with hydroxyapatite. Thus, Actinomyces agglutinins 1) are probably distinct from IgA but may complex with it; 2) may include both beta-Gal and higher affinity sites; and 3) may contribute to salivary pellicle.

Actinomyces↗
PubMed1979

Mannose-contaminating agglutinin for Actinomyces viscosus and Actinomyces naeslundii.

Rapid agglutination of Actinomyces viscosus and Actinomyces naeslundii cells by D-mannose solutions was observed during studies of their attachment to mammalian cells in vitro. The specificity of the agglutination reaction was studied by slide agglutination tests and by measuring the rate of decrease in optical density of bacterial phosphate buffer suspensions caused by the setting of bacterial aggregates. Actinomyces cells were agglutinated by protein-containing mannose solutions of several chemical suppliers. Solutions of sugars other than D-mannose and solutions of mannitol and mannan all failed to agglutinate A. viscsus and A. naeslundii. "Mannose-enhanced" agglutination was impaired by boiling or autoclaving the mannose but was not affected by heating the bacteria, the presence of chloramphenicol, running the assay in the cold, or incorporating any of several commercially purchased sugars in the reaction mixture. During these hapten inhibition experiments, only 6-deoxy-L-talcose-containing extracts of an A. viscosus strain retarded the rate of mannose-enhanced agglutination. Protein-containing fractions of D-mannose mother liquors also agglutinated cells of A. viscosus and A. naeslundii. Other species of oral gram-positive rods were not agglutinated by mannose solutions. Together the data indicate that plant seed-derived D-mannose contains a protein-associated agglutinin for A. viscosus and A. naeslundii which may function via a "lectin-like" selective affinity for the unique cell wall sugar 6-deoxy-L-talose.

Actinomyces↗
PubMed1983

Chemical and immunological comparison of surface fibrils of strains representing six taxonomic groups of Actinomyces viscosus and Actinomyces naeslundii.

Human isolates of Actinomyces viscosus and Actinomyces naeslundii have been divided into six clusters in a numerical taxonomy study. Surface fibrils of strains representing these clusters were isolated and purified. Chemical analyses revealed that the major component of all fibrils was protein and that although differences in percentages of specific amino acid residues were found, the relative proportions of basic, acidic, polar uncharged, and nonpolar amino acids were rather similar among clusters. All of the fibrils except those from strain B236 (cluster 2) either failed to migrate or penetrated only slightly into gels during sodium dodecyl sulfate-polyacrylamide gel electrophoresis, even after boiling, reduction, or alkylation. Immunological studies by electron microscopic examination of fibril-antibody immunocomplexes, whole bacterial cell agglutination, inhibition of hemagglutination, and immunofluorescence by using antifibril antisera and antibodies demonstrated that strains of typical A. naeslundii (cluster 5) have a specific fibril-associated antigen(s) distinct from those of strains of other clusters. Cross-reactions for atypical A. naeslundii (cluster 3) were few. The fibrils from A. viscosus clusters 1, 2, 4, and 6 demonstrated several cross-reactions. By absorbing antifibril antibodies with cross-reactive strains it was possible to obtain cluster-specific antibodies, as determined by whole cell agglutination, only for cluster 5. Absorbed antifibril antisera for both A. naeslundii clusters 3 and 5 were specific by indirect immunofluorescence, whereas anti-cluster 1 fibril antisera cross-reacted only with other A. viscosus cluster representatives. Purification of Actinomyces fibrils by methods used for appendages of other species yields preparations containing common antigens among taxonomic groups. However, absorbing antifibril antisera, gamma globulin, or both has promise for producing cluster-specific reagents useful in identification.

Actinomyces↗
PubMed1992

Conservation of an Actinomyces viscosus T14V type 1 fimbrial subunit homolog among divergent groups of Actinomyces spp.

The type 1 fimbrial subunit gene of the human Actinomyces viscosus T14V was used as a DNA probe in Southern analyses to detect related DNA sequences in 16 of 30 strains of Actinomyces spp. under conditions of high stringency. The organisms with homology to the DNA probe included two human and six nonhuman A. viscosus, three human and three nonhuman A. naeslundii, and two A. bovis isolates. Homologous DNA sequences were not detected in strains of A. odontolyticus and A. israelii examined in this study. Northern (RNA) blot analysis revealed expression of a transcript from each of the A. viscosus and A. naeslundii strains and from one A. bovis strain that was comparable in size to that detected from A. viscosus T14V. Cell surface fimbriae were observed on a majority of the strains that expressed the transcript. Various degrees of cross-immunoreactivities between these strains and antibodies specific for type 1 fimbriae of A. viscosus T14V were also observed by colony immunoassay. Thus, the data clearly demonstrate the existence in, and expression by, divergent Actinomyces groups of genomic sequences that are closely related to the type 1 fimbriae of A. viscosus T14V.

Actinomyces↗
PubMed1999

Strains of Actinomyces naeslundii and Actinomyces viscosus exhibit structurally variant fimbrial subunit proteins and bind to different peptide motifs in salivary proteins.

Oral strains of Actinomyces spp. express type 1 fimbriae, which are composed of major FimP subunits, and bind preferentially to salivary acidic proline-rich proteins (APRPs) or to statherin. We have mapped genetic differences in the fimP subunit genes and the peptide recognition motifs within the host proteins associated with these differential binding specificities. The fimP genes were amplified by PCR from Actinomyces viscosus ATCC 19246, with preferential binding to statherin, and from Actinomyces naeslundii LY7, P-1-K, and B-1-K, with preferential binding to APRPs. The fimP gene from the statherin-binding strain 19246 is novel and has about 80% nucleotide and amino acid sequence identity to the highly conserved fimP genes of the APRP-binding strains (about 98 to 99% sequence identity). The novel FimP protein contains an amino-terminal signal peptide, randomly distributed single-amino-acid substitutions, and structurally different segments and ends with a cell wall-anchoring and a membrane-spanning region. When agarose beads with CNBr-linked host determinant-specific decapeptides were used, A. viscosus 19246 bound to the Thr42Phe43 terminus of statherin and A. naeslundii LY7 bound to the Pro149Gln150 termini of APRPs. Furthermore, while the APRP-binding A. naeslundii strains originate from the human mouth, A. viscosus strains isolated from the oral cavity of rat and hamster hosts showed preferential binding to statherin and contained the novel fimP gene. Thus, A. viscosus and A. naeslundii display structurally variant fimP genes whose protein products are likely to interact with different peptide motifs and to determine animal host tropism.

Actinomyces↗
PubMed1988

Glycogen synthetic and degradative activities by Actinomyces viscosus and Actinomyces naeslundii of root surface caries and noncaries sites.

The relative glycogen synthetic and degradative activities of Actinomyces viscosus and Actinomyces naeslundii, freshly isolated from root surface caries and noncaries sites, were compared. The glycogen synthetic activity was measured by incubating glucose-(or sucrose-)grown resting cells with 100 mM glucose (or sucrose) and U-[14C]-glucose (or U-[14C]-sucrose) on a pH-stat maintained at 5.0, 6.0, and 7.0 for 1 h under anaerobic conditions. For the glycogen degradation assays, after the 1-hour incubation period, the cells were reincubated under similar conditions, but in the absence of external carbon sources. Carbohydrate utilization and total acid formation were also monitored. Both the glucose- and sucrose-grown cells of A. viscosus and A. naeslundii strains originating from root surface caries lesions synthesized approximately twice as much glycogen as the strains of noncaries origin. Although there were significant differences in the rates of glycogen synthesis, the rates of glycogen degradation were essentially the same for the Actinomyces strains from both caries and noncaries sites. However, the time required for glycogen degradation by the strains from caries sites was much longer. This study suggests that the abilities of A. viscosus and A. naeslundii originating from root surface caries lesions to synthesize large amounts of glycogen and to degrade this stored polymer slowly under conditions of starvation, particularly in an acidic environment, may be one of the factors contributing to the cariogenic potential of these organisms in root surface caries.

Actinomyces↗
PubMed2006

Sequence analyses of fimbriae subunit FimA proteins on Actinomyces naeslundii genospecies 1 and 2 and Actinomyces odontolyticus with variant carbohydrate binding specificities.

BACKGROUND: Actinomyces naeslundii genospecies 1 and 2 express type-2 fimbriae (FimA subunit polymers) with variant Galbeta binding specificities and Actinomyces odontolyticus a sialic acid specificity to colonize different oral surfaces. However, the fimbrial nature of the sialic acid binding property and sequence information about FimA proteins from multiple strains are lacking. RESULTS: Here we have sequenced fimA genes from strains of A.naeslundii genospecies 1 (n = 4) and genospecies 2 (n = 4), both of which harboured variant Galbeta-dependent hemagglutination (HA) types, and from A.odontolyticus PK984 with a sialic acid-dependent HA pattern. Three unique subtypes of FimA proteins with 63.8-66.4% sequence identity were present in strains of A. naeslundii genospecies 1 and 2 and A. odontolyticus. The generally high FimA sequence identity (> 97.2%) within a genospecies revealed species specific sequences or segments that coincided with binding specificity. All three FimA protein variants contained a signal peptide, pilin motif, E box, proline-rich segment and an LPXTG sorting motif among other conserved segments for secretion, assembly and sorting of fimbrial proteins. The highly conserved pilin, E box and LPXTG motifs are present in fimbriae proteins from other Gram-positive bacteria. Moreover, only strains of genospecies 1 were agglutinated with type-2 fimbriae antisera derived from A. naeslundii genospecies 1 strain 12104, emphasizing that the overall folding of FimA may generate different functionalities. Western blot analyses with FimA antisera revealed monomers and oligomers of FimA in whole cell protein extracts and a purified recombinant FimA preparation, indicating a sortase-independent oligomerization of FimA. CONCLUSION: The genus Actinomyces involves a diversity of unique FimA proteins with conserved pilin, E box and LPXTG motifs, depending on subspecies and associated binding specificity. In addition, a sortase independent oligomerization of FimA subunit proteins in solution was indicated.

Actinomyces↗
PubMed2000

Actinomyces and actinobacillus actinomycetemcomitans-Actinomyces-associated lymphadenopathy mimicking lymphoma.

We present 2 unusual cases of long-standing, extensive reactive lymphadenopathy secondary to Actinomyces infection, 1 of which was also accompanied by Actinobacillus actinomycetemcomitans-Actinomyces complex infection. To our knowledge, histologic features of lymph node involvement by these organisms have not been previously reported in the literature. One patient had extensive cervical, posterior mediastinal, and abdominal lymphadenopathy. The second patient presented with a submandibular mass and cervical lymphadenopathy. Clinical features strongly suggested lymphoma. The histologic examination of the lymph nodes from both patients revealed reactive follicular hyperplasia, marked interfollicular and capsular fibrosis, and multiple interfollicular microabscesses. Characteristic Actinomyces colonies were identified at the center of the microabscesses in deep sections. Cultures were obtained from the lymph nodes of 1 patient, and were positive for A actinomycetemcomitans. Both patients had poor dental hygiene. Lymphadenopathy subsided with antibiotic therapy and appropriate dental care.

Actinobacillus↗
PubMed1993

Complete nucleotide sequence of the Actinomyces viscosus T14V sialidase gene: presence of a conserved repeating sequence among strains of Actinomyces spp.

The nucleotide sequence of the Actinomyces viscosus T14V sialidase gene (nanH) and flanking regions was determined. An open reading frame of 2,703 nucleotides that encodes a predominately hydrophobic protein of 901 amino acids (M(r), 92,871) was identified. The amino acid sequence at the amino terminus of the predicted protein exhibited properties characteristic of a typical leader peptide. Five 12-amino-acid units that shared between 33 and 67% sequence identity were noted within the central domain of the protein. Each unit contained the sequence Ser-X-Asp-X-Gly-X-Thr-Trp, which is conserved among other bacterial and trypanosoma sp. sialidases. Thus, the A. viscosus T14V nanH gene and the other prokaryotic and eukaryotic sialidase genes evolved from a common ancestor. Southern hybridization analyses under conditions of high stringency revealed the existence of DNA sequences homologous to A. viscosus T14V nanH in the genomes of 18 strains of five Actinomyces species that expressed various levels of sialidase activity. The data demonstrate that the sialidase genes from divergent groups of Actinomyces spp. are highly conserved.

Actinomycetaceae↗
PubMed1988

Distribution of antigenic determinants between Actinomyces viscosus and Actinomyces naeslundii.

A total of 18 monoclonal antibodies was raised against whole cells of Actinomyces viscosus and Actinomyces naeslundii. The monoclonal antibodies were used to determine the cross-reacting patterns among 26 strains of these species. Eleven different antigenic determinants were found. The specificity profiles of the antibodies indicated that the antigenic determinants of A. viscosus and A. naeslundii were arranged in a complicated mosaic. Extensive cross-reactions occurred between A. viscosus strains and strains of "typical" and "atypical" A. naeslundii. However, cross-reactions were rare between the two groups of A. naeslundii. A. viscosus appears to occupy a "middle position" between the two A. naeslundii groups. In addition to their value in seroclassification, some of the monoclonal antibodies were found to be useful in the identification of these species. One monoclonal antibody appeared to be selective for the "typical" A. naeslundii group. A. viscosus and "atypical" A. naeslundii-specific antibodies were also found, though they did not label every strain in their respective clusters. A. viscosus detection might be improved if mixtures of monoclonal antibodies were used.

Actinomyces↗
PubMed1993

Synergistic, growth-inhibitory effects of chlorhexidine and copper combinations on Streptococcus mutans, Actinomyces viscosus, and Actinomyces naeslundii.

The purpose of this investigation was to determine whether chlorhexidine combined with copper would exert a synergistic, growth-inhibitory effect against selected oral bacteria. Actinomyces viscosus, Actinomyces naeslundii, and Streptococcus mutans were all susceptible to chlorhexidine individually, with S. mutans displaying the highest sensitivity. Much higher concentrations of copper were needed to achieve growth inhibition of the micro-organisms tested. Determination of minimum inhibitory concentrations (MICs) of chlorhexidine and Cu2+ combinations suggested synergistic activity. Bactericidal kinetics assays confirmed synergism of chlorhexidine and Cu2+ combinations with 1 to 2 log greater decreases in viable cell numbers compared with chlorhexidine alone. Under the constraints of the conditions employed, these data demonstrate the efficacy of chlorhexidine and Cu2+ combinations against the oral bacteria tested. These studies suggest that a chlorhexidine and copper formulation could be useful as a mouthrinse in helping control cariogenic micro-organisms and/or in the treatment of gingivitis.

Actinomyces↗
PubMed1985

Establishment and distribution of the bacteria Actinomyces viscosus and Actinomyces naeslundii in the mouths of monkeys (Macaca fascicularis).

The colonization of the mouth by the two Actinomyces species, postulated to be members of a basic plaque flora, was studied in 27 consecutively-born neonatal monkeys. Bacteria adherent to the tongue and cheek surfaces were sampled from each monkey soon after birth (mean age = 3.2 days). The tongue and cheek surfaces and the labial surfaces of the incisor teeth were sampled at 4, 8 and 12 weeks of age. From only one neonatal sample were Actinomyces species isolated. By 4 weeks of age, the incisor teeth are partially erupted and, from teeth erupted more than 1 mm, A. naeslundii was frequently isolated and its proportion increased between 4 and 8 weeks on all surfaces sampled. At 4, 8 and 12 weeks, the proportion of A. naeslundii on the incisor teeth was greater than on the mucosal surfaces. The isolation rate of A. viscosus was low in these neonates, but it was isolated from each of 6 juvenile monkeys fed a starch diet. In the 6 juvenile monkeys, the proportion of A. viscosus decreased following the introduction of a sucrose-containing diet, whereas the proportion of A. naeslundii on the teeth increased. The early establishment of A. naeslundii and, to a lesser extent, A. viscosus in the dental plaque of neonatal monkeys fed exclusively by their mothers suggests that members of a basic plaque flora may be those bacteria establishing in the plaque during the period of breast-feeding.

Actinomyces↗
PubMed2003

Actinomyces hongkongensis sp. nov. a novel Actinomyces species isolated from a patient with pelvic actinomycosis.

A bacterium was isolated from the pus of a patient with pelvic actinomycosis. The cells were strictly anaerobic, straight, non-sporulating, Gram-positive rods. It grows on sheep blood agar as non-haemolytic, pinpoint colonies after 24 hours of incubation at 37 degrees C in anaerobic environment. It is non-motile and does not produce catalase. 16S ribosomal RNA (rRNA) gene sequencing showed that there were 6.6% difference between the 16S rRNA gene sequence of the bacterium that of Actinomyces marimammalium (GenBank Accession no. AJ276405), a new species described in 2001, isolated from two seals and a porpoise. For these reasons a new species, Actinomyces hongkongensis sp. nov., is proposed, for which HKU8(T) is the type strain. Further studies should be performed to ascertain the potential of this bacterium to become an important cause of actinomycosis.

Actinomyces↗
PubMed2002

Tricuspid valve endocarditis caused by a new species of actinomyces: Actinomyces funkei.

We present a case of tricuspid valve endocarditis in a 40-y-old woman with a history of heroin abuse. Blood cultures yielded a Gram-positive rod, preliminarily identified as "Actinomyces turicensis-like", but subsequently formally described as Actinomyces funkei sp. nov. The patient was cured by prolonged treatment with 10 weeks of i.v. antibiotics followed by oral antibiotic treatment for 12 weeks.

Actinomyces↗