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Infection and Immunity Apr 1978A lytic phage which produces clear plaques on a human isolate of Actinomyces viscosus was isolated from a sample of raw domestic sewage.
A lytic phage which produces clear plaques on a human isolate of Actinomyces viscosus was isolated from a sample of raw domestic sewage.
Topics: Actinomyces; Bacteriophages; Viral Plaque Assay
PubMed: 669798
DOI: 10.1128/iai.20.1.303-306.1978 -
Oral Diseases Jul 2006To determine whether oral tolerance with the oral bacterium Actinomyces viscosus was inducible in mice.
OBJECTIVES
To determine whether oral tolerance with the oral bacterium Actinomyces viscosus was inducible in mice.
MATERIALS AND METHODS
Mice were intragastrically (i.g.) and then intraperitoneally (i.p.) immunized with heat-killed A. viscosus. A control group of mice received only saline. A delayed type hypersensitivity (DTH) response and the levels of isotype specific antibodies were assessed. Spleen cells from mice that were i.g. immunized with A. viscosus were transferred to A. viscosus-primed mice in vivo and in vitro. Furthermore, mice were i.g. immunized with saline or A. viscosus and then challenged i.p. with saline, A. viscosus, or Porphyromonas gingivalis.
RESULTS
Intragastric immunization with A. viscosus suppressed both DTH and serum specific antibodies to A. viscosus. DTH suppression lasted until week 4, while serum immunoglobulin (Ig)A and both IgG and IgM specific antibody levels remained suppressed up to week 8 and 12 respectively. IgG specific antibody suppression was transferable. The DTH response and serum antibodies specific to A. viscosus were suppressed in mice after i.g. challenged with A. viscosus but not P. gingivalis.
CONCLUSION
Mucosal presentation of A. viscosus in mice led to the suppression of immune response to this bacterium in an antigen-specific fashion. Tolerance of DTH response was short lived, while suppression of antigen-specific IgG antibodies in mucosally tolerized mice was long-lasting.
Topics: Actinomyces viscosus; Adoptive Transfer; Analysis of Variance; Animals; Antibodies, Bacterial; Antibody Formation; Epitopes; Female; Hypersensitivity, Delayed; Immune Tolerance; Immunization; Mice; Mice, Inbred DBA; Mouth Mucosa
PubMed: 16792724
DOI: 10.1111/j.1601-0825.2005.01210.x -
Microbiology and Immunology 1985A cell-free extract of Actinomyces viscosus T14Av catalyzed the synthesis of extracellular N-acetylglucosamine-rich slime polysaccharide. The activity was localized in...
A cell-free extract of Actinomyces viscosus T14Av catalyzed the synthesis of extracellular N-acetylglucosamine-rich slime polysaccharide. The activity was localized in the cytoplasmic membrane fraction and required the presence of ADP-glucose and UDP-N-acetylglucosamine. Maximal activity was demonstrated at pH 7.5 and also required the presence of divalent cations such as Mg2+ or Mn2+. Extracellular slime appeared to serve as a primer for slime biosynthesis. The antibiotic tunicamycin acted as an inhibitor of slime formation. However, another glucosamine analogue, amphomycin, as well as the antibiotic bacitracin produced moderate stimulatory effects on slime biosynthesis.
Topics: Actinomyces; Anti-Bacterial Agents; Magnesium; Polysaccharides, Bacterial; Uridine Diphosphate N-Acetylglucosamine
PubMed: 4046889
DOI: 10.1111/j.1348-0421.1985.tb00850.x -
Caries Research 1976
Topics: Actinomyces; Animals; Cells, Cultured; Chemical Phenomena; Chemistry; Culture Media; Dental Plaque; Glucosyltransferases; Hexosyltransferases; Polysaccharides; Rats; Sucrose
PubMed: 1058740
DOI: 10.1159/000260187 -
American Journal of Clinical Pathology Jan 1981Two cases of Actinomyces viscosus infection of the lungs were seen in nonimmunosuppressed patients. One patient had a peripheral actinomycotic lung mass resembling a...
Two cases of Actinomyces viscosus infection of the lungs were seen in nonimmunosuppressed patients. One patient had a peripheral actinomycotic lung mass resembling a tumor. Both patients responded to a long course of penicillin therapy. Reports of A. viscosus infections are rare, although the organism colonizes the mouths of most adult humans. Only ten cases have previously been described. There is no characteristic of A. viscosus infection that can distinguish it from Actinomyces israelii or Actinomyces bovis infections. The illness usually manifests as a chronic disease weeks to months before the diagnosis, which can only be made by identification of the organism from a clinical specimen uncontaminated by sputum or mouth flora. Ignorance of the biochemical reactions and growth characteristics of this organism have in the past hindered its isolation and identification. At least three weeks of antibiotic therapy using agents to which A. viscosus is sensitive in vitro are required for cure.
Topics: Actinomyces; Actinomycosis; Adult; Humans; Lung Diseases; Male
PubMed: 7457420
DOI: 10.1093/ajcp/75.1.113 -
Infection and Immunity Nov 1979Rapid agglutination of Actinomyces viscosus and Actinomyces naeslundii cells by D-mannose solutions was observed during studies of their attachment to mammalian cells in...
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.
Topics: Actinomyces; Agglutination Tests; Agglutinins; Glucose; Hot Temperature; Mannose; Solutions; Stereoisomerism
PubMed: 546781
DOI: 10.1128/iai.26.2.427-434.1979 -
Infection and Immunity Apr 1989Strains representing taxonomic clusters of Actinomyces viscosus and Actinomyces naeslundii were studied by indirect immunogold electron microscopy with either...
Strains representing taxonomic clusters of Actinomyces viscosus and Actinomyces naeslundii were studied by indirect immunogold electron microscopy with either monospecific anti-type 1 and anti-type 2 rabbit antibodies or species-specific monoclonal antibodies. The monoclonal and anti-type 2 antibodies localized on long fibrils, whereas the anti-type 1 antibodies mostly localized close to the cell body or on shorter appendages.
Topics: Actinomyces; Animals; Antibodies, Bacterial; Antibodies, Monoclonal; Antigens, Bacterial; Fimbriae, Bacterial; Humans; Immunohistochemistry; Microscopy, Electron; Rabbits
PubMed: 2564376
DOI: 10.1128/iai.57.4.1327-1331.1989 -
Scandinavian Journal of Dental Research Aug 1983The objectives were to determine the degree of Actinomyces agglutinating activity in human saliva and to begin characterizing the agglutination mechanism. Agglutination... (Comparative Study)
Comparative Study
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.
Topics: Actinomyces; Adult; Agglutination; Agglutinins; Child; Dental Pellicle; Humans; Immunoglobulin A; Saliva
PubMed: 6579605
DOI: 10.1111/j.1600-0722.1983.tb00815.x -
Journal of Dental Research Jan 1988A total of 18 monoclonal antibodies was raised against whole cells of Actinomyces viscosus and Actinomyces naeslundii. The monoclonal antibodies were used to determine... (Comparative Study)
Comparative Study
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.
Topics: Actinomyces; Actinomyces viscosus; Antibodies, Monoclonal; Antibody Specificity; Cross Reactions; Epitopes; Fluorescent Antibody Technique, Indirect; Humans; Serotyping; Species Specificity
PubMed: 11039037
DOI: 10.1177/00220345880670010101 -
Infection and Immunity May 1999Oral strains of Actinomyces spp. express type 1 fimbriae, which are composed of major FimP subunits, and bind preferentially to salivary acidic proline-rich proteins... (Comparative Study)
Comparative Study
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.
Topics: Actinomyces; Amino Acid Sequence; Animals; Bacterial Proteins; Base Sequence; Binding Sites; Cricetinae; DNA Primers; Fimbriae, Bacterial; Genes, Bacterial; Humans; Molecular Sequence Data; Mouth; Protein Binding; Rats; Salivary Proteins and Peptides; Sequence Homology, Amino Acid; Species Specificity
PubMed: 10225854
DOI: 10.1128/IAI.67.5.2053-2059.1999