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PubMed1986

Modulation of Actinomyces viscosus colonization of mouse teeth in vivo by immunization with fimbrial adhesins.

Experiments were performed to determine whether immunization of mice with fimbrial adhesins isolated from Actinomyces viscosus T14V could modulate infection of tooth surfaces in animals challenged with the homologous strain. Saliva and sera from animals immunized in the submandibular gland region contained elevated levels of fimbria-specific immunoglobulin A (IgA) and IgG, whereas saliva and sera from sham-immunized animals did not. There was a statistically significant inverse correlation between the presence of fimbria-specific antibodies in saliva and serum and the levels of bacterial colonization on molar tooth surfaces. These results suggest that fimbrial adhesins may effectively modulate infection of tooth surfaces by periodontopathic bacteria.

Actinomyces↗
PubMed1987

Purification and characterization of levanase from Actinomyces viscosus ATCC 19246.

The extracellular levanase of Actinomyces viscosus ATCC 19246 was purified about 3,701-fold in 11% yield from the bacterial culture supernatant by means of ammonium sulfate precipitation, followed by DE52 column chromatography, Sephadex G-100 gel filtration, hydroxylapatite column chromatography, and Bio-Gel A 1.5m gel filtration. The molecular weight of the enzyme was estimated to be 89,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme was optimally reactive at pH 6.0 and at 45 degrees C. The activity was inhibited by MnCl2, BaCl2, FeCl3, ZnCl2, HgCl2, and EDTA at a final concentration of 1 mM. The inhibition by EDTA was recovered by adding CaCl2 or MgCl2. The enzyme specifically hydrolyzed levan, but not sucrose, raffinose, melezitose, inulin, and dextran. These results indicate that the purified enzyme is specific for fructan (i.e., levan), which mainly consists of beta-(2,6) linkages.

Actinomyces↗
PubMed1988

Mutants of Actinomyces viscosus T14V lacking type 1, type 2, or both types of fimbriae.

Mutants of Actinomyces viscosus T14V lacking type 1 or type 2 fimbriae or both were selected by their failure to react with rabbit antibodies against either or both fimbrial antigens. Immunospecific double labeling with iron dextran and ferritin-conjugated antibodies showed two types of fimbriae on individual cells of the parent organism, a single type on mutant strains with type 1+2- and type 1-2+ fimbriae and no labeled or unlabeled fimbriae on a type 1-2- fimbria-deficient strain. The mutational loss of one fimbrial antigen did not appear to affect expression of the other, since bacteria with one or two types of fimbriae bound similar amounts of a monoclonal antibody directed against the fimbrial antigen present on both bacterial phenotypes. The strong adsorption of strains with type 1+2+ or 1+2- fimbriae to saliva-treated hydroxyapatite and weak adsorption of those with type 1-2+ or no fimbriae was consistent with the known involvement of type 1 fimbriae in this attachment process. Similarly, the A. viscosus lectin was clearly associated with the expression of type 2 fimbriae, since only the strains with type 1+2+ or 1-2+ fimbriae participated in lactose-sensitive coaggregations with Streptococcus sanguis 34. Further studies using the fimbria-deficient mutant strains showed that aggregation of A. viscosus T14V in the presence of sialidase-treated human saliva involved both types of fimbriae, whereas neither type was required for the lactose-resistant coaggregation of the organism with certain streptococcal strains.

Actinomyces↗
PubMed1990

Binding of colloidal gold-labeled salivary proline-rich proteins to Actinomyces viscosus type 1 fimbriae.

Salivary proline-rich proteins (PRPs), which were purified from parotid saliva, were adsorbed onto 15-nm-diameter gold particles to visualize specific binding of the salivary molecules to Actinomyces viscosus type 1 fimbriae. Negatively stained preparations incubated with PRP-gold conjugates but not bovine serum albumin-gold complexes bound specifically to bacteria possessing type 1 fimbriae, A. viscosus T14V-J1 and 5519. Binding of the PRP-gold probes to strains deficient in type 1 fimbriae, i.e., strains 5951 (type 2 fimbriae only) and 147 (no fimbriae), was negligible.

Actinomyces↗
PubMed1991

Genetic control of serum antibody responses of inbred mice to type 1 and type 2 fimbriae from Actinomyces viscosus T14V.

Antibodies reactive with type 1 and type 2 fimbriae from Actinomyces viscosus T14V specifically inhibit the adherence of A. viscosus T14V to salivary pellicle-coated tooth surfaces and other bacteria, and these antibodies are thought to modulate colonization by this microorganism. These studies were done to determine whether previously noted differences in the antibody responses of inbred mice to type 1 and type 2 fimbriae might be under genetic control. The serum immunoglobulin G (IgG) and IgM antibody responses of inbred, F1 hybrid, and H-2 congenic mice, immunized with A. viscosus T14V cells, were analyzed by enzyme-linked immunosorbent assays for antibodies reactive with A. viscosus T14V whole-cell type 1 and type 2 fimbriae. The results confirmed earlier findings and indicated striking variations in the amounts of IgG anti-type 1 (23-fold) and anti-type 2 (48-fold) fimbria antibodies elicited. The responses of the 17 inbred strains tested showed a relatively continuous distribution from high to low, as well as marked differences in the responses of H-2 and Igh-C identical strain pairs. An analysis of the responses of F1 hybrid and H-2 congenic mice indicated dominance of the low-responder gene(s) and control by H-2-linked genes. Antisera from two high-responder strains inhibited in vitro bacterial adherence to a much greater degree than antisera from a low-responding strain. These data suggest polygenic control of the magnitude of the IgG anti-type 1 and anti-type 2 fimbria antibody responses by H-2-linked genes as well as background genes not associated with H-2 or Igh-C loci.

Actinomyces↗
PubMed1992

Isolation and characterization of Actinomyces viscosus mutants defective in binding salivary proline-rich proteins.

Recent studies have provided evidence for human salivary proline-rich proteins (PRPs) serving as potential receptors in the acquired pellicle for Actinomyces viscosus type 1 fimbriae. We report here the isolation of mutants derived from A. viscosus T14V-J1 which are defective in binding to PRPs partially purified from parotid gland saliva. Mutagenesis with ethyl methanesulfonate preceded enrichment for cells nonreactive with PRPs by successive adsorptions with PRP-treated latex beads. Screening was accomplished by random selection of 250 isolated colonies from each of four enrichment cycles and reaction with PRP-treated latex beads in microtiter plates. Two mutants of independent origin were examined for adherence to hydroxyapatite treated with either PRPs, proline-rich glycoproteins, deglycosylated proline-rich glycoproteins, or whole saliva. Additional surface properties that were examined included agglutination with polyclonal antisera to type 1 and type 2 fimbriae, agglutination by a monoclonal antibody to type 1 fimbriae that inhibits adherence of the parent strain to saliva-treated hydroxyapatite, the ability to bind monoclonal antibody to the type 1 fimbrial subunit, and lactose-reversible coaggregation with Streptococcus sanguis 34. Both mutants exhibited reduced binding to hydroxyapatite treated with whole saliva or salivary protein preparations but were still capable of reaction with antiserum to type 1 and type 2 fimbriae. In addition, these mutants possessed the ability to bind monoclonal antibody to the type 1 fimbrial subunit in amounts comparable to the amount bound by the parent strain but were not agglutinated by the adherence-inhibiting monoclonal antibody. When considered with previously published data, these results suggest that an adhesive molecule is probably associated with type 1 fimbriae and allows for the interaction of A. viscosus with constituents in the salivary pellicle.

Actinomyces viscosus↗
PubMed1993

Inactivation of the gene encoding surface protein SspA in Streptococcus gordonii DL1 affects cell interactions with human salivary agglutinin and oral actinomyces.

Cell surface protein SSP-5 in the oral bacterium Streptococcus gordonii M5 binds human salivary agglutinin in a Ca(2+)-dependent reaction (D.R. Demuth, E.E. Golub, and D. Malamud, J. Biol. Chem. 265:7120-7126, 1990). The region of the gene encoding an N-terminal segment of a related polypeptide (SspA) in S. gordonii DL1 (Challis) was isolated following polymerase chain reaction amplification of genomic DNA. The sspA gene in S. gordonii DL1 was insertionally inactivated by homologous recombination of the erythromycin resistance (Emr) determinant ermAM onto the streptococcal chromosome. The SspA polypeptide (apparent molecular mass, 210 kDa) was detected on Western blots (immunoblots) of spheroplast extracts and extracellular culture medium proteins from wild-type strain DL1 but was absent from Emr mutants. One SspA- mutant (designated OB220) was not altered in rate or extent of aggregation by whole saliva or parotid saliva but showed reduced aggregation in the presence of purified salivary agglutinin. Mutant bacteria were unaffected in their ability to adhere to hydroxylapatite beads coated with whole or parotid saliva and were unaltered in cell surface hydrophobicity. However, the SspA- strain OB220 was deficient in binding salivary agglutinin and in binding to six strains of Actinomyces naeslundii. Therefore, expression of SspA polypeptide in S. gordonii is associated with both agglutinin-dependent and agglutinin-independent aggregation and adherence reactions of streptococcal cells.

Actinomyces↗
PubMed1996

Recognition of immunoglobulin A1 by oral actinomyces and streptococcal lectins.

Actinomyces naeslundii and Streptococcus gordonii, oral bacteria that possess Gal/GalNAc- and sialic acid-reactive lectins, respectively, were adherent to immobilized secretory immunoglobulin A (IgA) and two IgA1 myeloma proteins but not to two IgA2 myeloma proteins. Apparently, O-linked oligosaccharides at the hinge region of the IgA1 heavy chain are receptors for lectin-mediated adhesion of these bacteria.

Actinomyces↗
PubMed1998

Identification of a gene involved in assembly of Actinomyces naeslundii T14V type 2 fimbriae.

The nucleotide sequence of the Actinomyces naeslundii T14V type 2 fimbrial structural subunit gene, fimA, and the 3' flanking DNA region was determined. The fimA gene encoded a 535-amino-acid precursor subunit protein (FimA) which included both N-terminal leader and C-terminal cell wall sorting sequences. A second gene, designated orf365, that encoded a 365-amino-acid protein which contained a putative transmembrane segment was identified immediately 3' to fimA. Mutants in which either fimA or orf365 was replaced with a kanamycin resistance gene did not participate in type 2 fimbriae-mediated coaggregation with Streptococcus oralis 34. Type 2 fimbrial antigen was not detected in cell extracts of the fimA mutant by Western blotting with anti-A. naeslundii type 2 fimbrial antibody, but the subunit protein was detected in extracts of the orf365 mutant. The subunit protein detected in this mutant also was immunostained by an antibody raised against a synthetic peptide representing the C-terminal 20 amino acid residues of the predicted FimA. The antipeptide antibody reacted with FimA isolated from the recombinant Escherichia coli clone containing fimA but did not react with purified type 2 fimbriae in extracts of the wild-type strain. These results indicate that synthesis of type 2 fimbriae in A. naeslundii T14V may involve posttranslational cleavage of both the N-terminal and C-terminal peptides of the precursor subunit and also the expression of orf365.

Actinomyces↗
PubMed1999

Genetic and physiologic characterization of urease of Actinomyces naeslundii.

Ammonia production from urea by ureolytic oral bacteria is believed to have a significant impact on oral health and the ecological balance of oral microbial populations. In this study we cloned and characterized the urease gene cluster of Actinomyces naeslundii, which is one of the pioneer organisms in the oral cavity and a significant constituent of supragingival and subgingival dental plaque in children and adults. An internal fragment of the ureC gene of A. naeslundii WVU45 was initially amplified by PCR with degenerate primers derived from conserved amino acid sequences of the large catalytic subunit of urease in bacteria and plants. The PCR product was then used as a probe to identify recombinant bacteriophages carrying the A. naeslundii urease gene cluster and roughly 30 kbp of flanking DNA. Nucleotide sequence analysis demonstrated that the gene cluster was comprised of seven contiguously arranged open reading frames with significant homologies at the protein and nucleotide sequence levels to the ureABCEFGD genes from other organisms. By using primer extension, a putative transcription initiation site was mapped at 66 bases 5' to the start codon of ureA. A urease-deficient strain was constructed by insertion of a kanamycin resistance determinant within the ureC gene via allelic replacement. In contrast to the wild-type organism, the isogenic mutant was unable to grow in a semidefined medium supplemented with urea as the nitrogen source and was not protected by the addition of urea against killing in moderately acidic environments. These data indicated that urea can be effectively utilized as a nitrogen source by A. naeslundii via a urease-dependent pathway and that ureolysis can protect A. naeslundii against environmental acidification at physiologically relevant pH values. Therefore, urease could confer to A. naeslundii critical selective advantages over nonureolytic organisms in dental plaque, constituting an important determinant of plaque ecology.

Actinomyces↗
PubMed1999

An Arcanobacterium (Actinomyces) pyogenes mutant deficient in production of the pore-forming cytolysin pyolysin has reduced virulence.

Pyolysin (PLO), the hemolytic exotoxin expressed by Arcanobacterium (Actinomyces) pyogenes, is a member of the thiol-activated cytolysin family of bacterial toxins. Insertional inactivation of the plo gene results in loss of expression of PLO with a concomitant loss in hemolytic activity. The plo mutant, PLO-1, has an approximately 1. 8-log10 reduction in the 50% infectious dose compared to that for wild-type A. pyogenes in a mouse intraperitoneal infection model. Studies involving cochallenge of wild-type and PLO-1 bacteria resulted in recovery of similar numbers of both strains, suggesting that PLO production is required for survival in vivo. Recombinant, His-tagged PLO (His-PLO) is cytotoxic for mouse peritoneal macrophages and J774 cells in a dose-dependent manner. Protection against challenge with A. pyogenes could be afforded by vaccination with formalin-inactivated His-PLO, suggesting that PLO is a host-protective antigen, as well as a virulence determinant.

Actinomyces↗
PubMed2000

Analysis of urease expression in Actinomyces naeslundii WVU45.

The hydrolysis of urea by ureases of oral bacteria in dental plaque can cause a considerable increase in plaque pH, which can inhibit the development of dental caries. There is also indirect evidence that urea metabolism may promote the formation of calculus and that ammonia release from urea could exacerbate periodontal diseases. Actinomyces naeslundii, an early colonizer of the oral cavity and a numerically significant plaque constituent, demonstrates comparatively low levels of urease activity on isolation, so this organism has not been considered a major contributor to total oral urease activity. In this study it was observed that urease activity and urease-specific mRNA levels in A. naeslundii WVU45 can increase up to 50-fold during growth under nitrogen-limiting conditions. Using primer extension analysis, a putative, proximal, nitrogen-regulated promoter of the A. naeslundii urease gene cluster was identified. The functionality and nitrogen responsiveness of this promoter were confirmed using reporter gene fusions and 5' deletion analysis. The data indicated that regulation of urease expression by nitrogen availability in A. naeslundii may require a positive transcriptional activator. Plaque bacteria may experience nitrogen limitation when carbohydrates are present in excess. Therefore, based on the results of this study and in contrast to previous beliefs, strains of A. naeslundii may have the potential to be significant contributors to total plaque ureolysis, particularly during periods when there is an increased risk for caries development.

Actinomyces↗
PubMed2000

Possible release of an ArgGlyArgProGln pentapeptide with innate immunity properties from acidic proline-rich proteins by proteolytic activity in commensal streptococcus and actinomyces species.

This study suggests degradation of salivary acidic proline-rich proteins (PRPs) into potential innate-immunity-like peptides by oral Streptococcus and Actinomyces species. PRP degradation paralleled cleavage of Pro-containing substrates. PRP degradation by S. gordonii strain SK12 instantly released a Pyr(1)-Pro(104)Pro(105) and a Gly(111)-Pro(149)Gln(150) peptide together with a presumed Arg(106)Gly(107)Arg(108)Pro(109)Gln(110) pentapeptide. The synthetic Arg(106)Gly(107)Arg(108)Pro(109)Gln(110) peptide desorbed bound bacteria and counteracted sucrose-induced decrease of dental plaque pH in vitro.

Actinomyces↗
PubMed2001

Identification of independent Streptococcus gordonii SspA and SspB functions in coaggregation with Actinomyces naeslundii.

The initial stages of dental plaque formation involve the adherence of early colonizing organisms such as Streptococcus gordonii and Actinomyces naeslundii to the saliva-coated tooth surface and to each other. The S. gordonii surface proteins SspA and SspB are known to play a role in adherence to salivary proteins and mediate coaggregation with other bacteria. Coaggregation is the adhesin receptor-mediated interaction between genetically distinct cell types and appears to be ubiquitous among oral isolates. To define the function of SspA and SspB separately on the surface of their natural host, we constructed and analyzed the coaggregation properties of an isogenic sspB mutant of S. gordonii DL1, an sspAB double mutant, and a previously described sspA mutant. A. naeslundii strains have been previously classified into six coaggregation groups based on the nature of their coaggregations with S. gordonii DL1 and other oral streptococci. Coaggregation assays with the sspA and sspB mutants showed that SspA and SspB are the streptococcal proteins primarily responsible for defining these coaggregation groups and, thus, are highly significant in the establishment of early dental plaque. SspA exhibited two coaggregation-specific functions. It participated in lactose-inhibitable and -noninhibitable interactions, while SspB mediated only lactose-noninhibitable coaggregations. Accordingly, the sspAB double mutant lacked these functions and allowed us to detect a third coaggregation interaction with one of these organisms. These proteins may play an important role in development of S. gordonii-A. naeslundii communities in early dental plaque. Understanding these adhesin proteins will aid investigations of complex microbial communities that characterize periodontal diseases.

Actinomyces↗
PubMed2004

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.

Actinomyces↗
PubMed1975

Purification, characterization, and regulation of a nicotinamide adenine dinucleotide-dependent lactate dehydrogenase from Actinomyces viscosus.

A nicotinamide adenine dinucleotide-specific L-(+)-lactate dehydrogenase (LDH) (EC 1.11.27) from Actinomyces viscosus T-6-1600 was purified approximately 110-fold by a combination of diethylaminoethyl-cellulose and 0.5 M Agarose A column chromatography. The ldh was stable at 26 C, but was quite labile at temperatures below 5 C. The enzyme had a molecular weight of 100,000 +/- 10,000 as determined by 0.5 M Agarose molecular exclusion chromatography and showed optimum activity between pH 5.5 and 6.2. The A. viscosus LDH exhibited homotropic interactions with its substrate, pyruvate, and its coenzyme, reduced nicotinamide adenine dinucleotide, indicating multiple binding sites on the enzyme for these ligands with some degree of cooperative interaction between them. The enzyme was under negative control by adenosine 5'-triphosphate, and its kinetic response to the negative effector was sigmoidal in nature. Inorganic phosphate reversed the inhibition exerted on the A. viscosus LDH by adenosine. The 5'-triphosphate thermal stability at 65 C of the LDH from A. viscosus was increased in the presence of its negative effector, adenosine 5'-triphosphate, but was markedly decreased in the presence of its coenzyme, reduced nicotinamide adenine dinucleotide. The glycolytic intermediate, fructose-1,6-diphosphate, had no effect on the catalytic activity of the A. viscosus LDH at saturating pyruvate concentrations. However, fructose-1,6-diphosphate was a potent positive effector at low substrate concentrations. Thus the A. viscosus LDH is under positive control by fructose-1,6-diphosphate and inorganic phosphate, but under negative control by adenosine 5'-triphosphate.

Actinomyces↗