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PubMed1979

Resolution of the glycosyltransferase activities from two strains of Streptococcus mutans by polyacrylamide gel electrophoresis in the presence of Tween 80.

The glycosyltransferase complex from Streptococcus mutans can be resolved by polyacrylamide gel electrophoresis following treatment with Tween 80. The enzyme complex was treated with Tween 80 and electrophoresis was performed in the presence of Tween 80. Discrete bands of glycosyltransferase activity were observed when the gels were incubated in buffered sucrose. The enzyme aggregation that occurs with the exocellular glycosyltransferase may involve lipophilic interactions that are disrupted by the Tween 80.

Electrophoresis, Polyacrylamide Gel↗
PubMed2001

Characterization of two operons that encode components of fructose-specific enzyme II of the sugar:phosphotransferase system of Streptococcus mutans.

Three genes, designated as fruC, fruD and fruI, were predicted to encode polypeptides homologous to fructose-specific enzyme II (II(Fru)) of the phosphoenolpyruvate-dependent sugar:phosphotransferase system, and were cloned from Streptococcus mutans, the primary etiological agent of human dental caries. The fruC and fruD genes encoded domains BC and domain A of II(Fru), respectively. The fruI gene encoded IICBA(Fru). Northern hybridization and slot blot analysis showed that expression of fruI was inducible by sucrose and fructose, while fruCD were expressed constitutively and at much lower levels. Inactivation of either fruI or fruCD alone, or of both fruCD and fruI, had no major impact on growth on fructose at a concentration of 0.5% (w/v). However, when the strains were grown with 0.2% fructose as the sole carbohydrate source, a significant decrease in the growth rate was seen with the fruCD/fruI double mutants. Assays of sugar:phosphotransferase activity showed that the fruCD/fruI double mutants had roughly 30% of the capacity of the wild-type strain to transport fructose via the phosphoenolpyruvate-dependent sugar:phosphotransferase system. Xylitol toxicity assays indicated that the inducible fructose permease was responsible for xylitol transport.

Blotting, Northern↗
PubMed2001

In vitro antimicrobial activity of a chitooligosaccharide mixture against Actinobacillus actinomycetemcomitans and Streptococcus mutans.

The purpose of this study was to evaluate the in vitro antibacterial activity of a chitooligosaccharide mixture (MW 2000-30000 Da) with a deacetylation degree of 91.5% against two representative oral pathogens, Actinobacillus actinomycetemcomitans and Streptococcus mutans. A 0.1% concentration of the chitooligosaccharides (derived from the exoskeletons of marine crustaceans) was used to estimate antibacterial activity. Approximately 2 logcolony forming units (CFU)/ml of A. actinomycetemcomitans were inactivated by 0.1% chitosan after 30 min, while 120 min exposure inactivated about 4.5 logCFU/ml of this organism. In contrast, the level of inactivation against S. mutans was less than 0.5 logCFU/ml after an exposure of up to 120 min. Electron microscopy showed that the exposure of A. actinomycetemcomitans to the chitooligosaccharides resulted in the disruption of cell membranes and that it could be considered for the treatment of periodontal diseases associated with A. actinomycetemcomitans.

Aggregatibacter actinomycetemcomitans↗
PubMed2006

Influence of cranberry juice on glucan-mediated processes involved in Streptococcus mutans biofilm development.

Cranberry juice (CJ) has biological properties that may provide health benefits. In this study, we investigated the influence of CJ (pH 5.5) on several activities in vitro associated with the development of Streptococcus mutans UA159 biofilms. The ability of CJ to influence the adherence of S. mutans to either saliva- (sHA) or glucan-coated hydroxyapatite (gsHA), and to inhibit the glucan production by purified glucosyltransferases adsorbed to sHA was determined. For the adherence assays, we used both uncoated and saliva-coated bacterial cells. Furthermore, we examined whether CJ interferes with the viability, development, polysaccharide composition and acidogenicity of S. mutans biofilms. A solution containing equivalent amounts of glucose, fructose and organic acids at pH 5.5 was used as negative control. The adherence of S. mutans (uncoated and saliva-coated) to either sHA or gsHA treated with 25% CJ (v/v) was remarkably reduced (40-85% inhibition compared to control: p < 0.05), indicating that CJ effectively blocked the bacterial adherence to binding sites in salivary pellicle and in glucans. In contrast, when the bacterial cells alone were treated with CJ they adhered to the similar untreated surfaces. Cranberry juice (25%, v/v) also inhibited the activities of surface-adsorbed GTF B and C (70-80% inhibition compared to control, p < 0.05). The effect of CJ on the viability of microorganisms in biofilms was not significant. Biofilm formation and accumulation were significantly reduced by topical applications of 25% CJ (v/v) twice daily with 1-min exposures (p < 0.05). The biomass and insoluble glucan content of the biofilms in addition to its acidogenicity were significantly reduced by cranberry treatments (p < 0.05). Our data show that cranberry juice inhibited glucan-mediated biofilm development and acid production, and holds promise as a natural product to prevent biofilm-related oral diseases.

Analysis of Variance↗
PubMed1977

Ultrastructural localization of sucrases in Streptococcus mutans GS-5 and an extracellular polysaccharide mutant: a comparative cytochemical and immunocytochemical study.

Electron microscopy and cytochemical and immunocytochemical procedures were used to study the ultrastructural distribution of sucrase enzymes in two strains of Streptococcus mutans. In a strongly adherent and virulent parent strain, GS-5, most of the invertase and fructosyltransferase activities were demonstrated extracellularly or bound to the cell surfaces. Intracellularly, enzymatic sites were detected near the plasma membrane on the periphery of the nucleoid and central mesosome. In GS-511, a mutant of diminished virulence and adherence, most of the enzymatic activity was not located on the cell surfaces, but was found away from the cell walls and associated with extracellular polysaccharides. Intracellularly, GS-511 manifested the same distribution of invertase and fructosyltransferase as did GS-5; however, the close association of these enzymes with the plasma membrane was not shown in GS-511. In both strains, extracellular areas near regions associated with cross wall formation appeared to show localized concentrations of these sucrases. Antibodies against partially purified glucosyltransferase (GTF) enzymes from GS-5 were used to localize GTF by immunocytochemical techniques. Indirect ferritin localization procedures showed that the extracellular and cell-bound GTF enzymes were distributed in similar locations as the fructosyltransferase and invertase enzymes. By absorption of the antiserum with whole GS-511 cells, the location of extracellular GTF and surface antigens unique to GS-5 was demonstrated. The dramatically reduced levels of cell-bound sucrase activity in GS-511 indicates the significant role of these enzymes in adherence and cariogenicity.

Cell Membrane↗
PubMed1986

Origin and function of the multiple extracellular glucosyltransferase species from cultures of a serotype c strain of Streptococcus mutans.

Two methods were used to purify the bifunctional extracellular enzyme sucrose: (1-6)- and (1-3)-alpha-D-glucan-6-alpha-D-glucosyltransferase (EC 2.4.1.5; dextransucrase) from continuous cultures of a serotype c strain of Streptococcus mutans. The first method, based on a previously published report, involved Sepharose 6B gel filtration and DEAE cellulose anion exchange chromatography. This resulted in a dextransucrase preparation with an apparent molecular mass of 162 kDa and a specific activity of 125 mg of glucan formed from sucrose h-1 (mg of protein)-1, at 37 degrees C. It was almost homogeneous as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The ratio of carbohydrate to protein was 0.14 and the recovery was 14% relative to the total glucosyltransferase activity in the original culture fluid. In the subsequently preferred method, hydroxyapatite-Ultrogel was used to purify dextransucrase with a 24% yield. The specific activity, 197 mg of glucan formed h-1 (mg of protein)-1, was the highest yet reported and this preparation contained less than 0.5 glucose-equivalent per subunit of molecular mass 162 kDa. Dextransucrase is therefore not a glycoprotein. Exogenous dextran stimulated activity, but was not essential for activity. The purified protein slowly degraded to multiple lower molecular mass forms during storage at 4 degrees C and 87% of the activity was lost after 20 days. The molecular mass of the most prominent, active degradation product was 140 kDa, similar to that of one of the multiple forms of dextransucrase detected in other laboratories. Preparations in which either the 140-kDa or the 162-kDa species predominated catalyzed the synthesis of a water-soluble glucan with sucrose alone, but catalyzed that of an insoluble glucan with sucrose and a high concentration of either (NH4)2SO4 or polyethylene glycol. The water-insoluble glucan was shown to lack sequences of 1,3-alpha-linked glycosyl residues typical of the insoluble glucan, mutan, which has been implicated in dental caries. We conclude that mutan is synthesized by the concerted action of two independent glucosyltransferases rather than by interconvertible forms of a single enzyme, as was proposed previously.

Electrophoresis, Polyacrylamide Gel↗
PubMed1978

Antigens of Streptococcus mutans: isolation of a serotype-specific and a cross-reactive antigen from walls of strain V-100 (serotype e).

Two cell wall-associated polysaccharide antigens were extracted from purified cell walls of Streptococcus mutans serotype e strain V-100. One of these purified antigens (I) is specific for serotype e, whereas the other (II) has antigenic determinants reactive with both heterologous anti-serotype c serum (GS-5) and the homologous (e) serum. When crude formamide extracts of V-100 cell walls were loaded onto a Cellex-D column and eluted with a linear gradient of ammonium carbonate (0.02 to 0.40 M), the two products mentioned above could be recovered. The purified, antigenically reactive products (I and II) were each composed only of rhamnose and glucose in approximately a 2:1 molar ratio. Immunoelectrophoresis of the crude formamide extract, peak I, and peak II showed the purified fractions to have opposite mobilities and the crude extract to have a mobility that encompassed both purified peaks when reacted with homologous antiserum (V-100). When these three fractions were immunoelectrophoresed and reacted with heterologous anti-serotype c serum (GS-5), only the anodic portion of the crude V-100 formamide extract and purified peak II formed precipitates. Ouchterlony analysis with homologous antiserum produced precipitin patterns between the crude formamide extract and both purified peaks, indicating complete identity. However, only crude extracts of V-100 and the purified peak II material reacted with heterologous (c) antiserum; peak I did not cross-react in these Ouchterlony assays. Hapten inhibition studies revealed that a beta-glucosyl moiety is the immunodeterminant for serotype e and is present on each purified fraction. The basis of the cross-reaction between anti-c sera and the purified antigen II of e is discussed.

Cell Wall↗
PubMed1984

Characterization of polysaccharide antigens of Streptococcus mutans B13 grown under various conditions.

Bacteria may respond to changes in their environment by varying the synthesis of surface components. This study examined the effects of various culture conditions on two wall polysaccharides of Streptococcus mutans B13 (serotype d): serotype d antigen, a galactose-glucose polymer, and RGP antigen, a rhamnose-glucose polymer. Cells were grown in a chemostat at various dilution rates (D) and pH values, including D = 0.05, 0.1, and 0.5 h-1 at pH 6.0 and D = 0.1 h-1 at pH 5.5, 6.0, 6.5, and 7.5. The cells were examined for protein and carbohydrate content by colorimetric assays and gas-liquid chromatography. Rantz-Randall extracts (120 degrees C, 30 min) and M-1 N-acetylmuramidase digests were prepared and examined for the presence of specific antigens by agar gel diffusion and quantitative precipitation assays. Cell preparations did not vary significantly with respect to total protein or carbohydrate content; however, cells grown at D = 0.1 h-1 and pH 7.5 had a significantly higher rhamnose content than did the other preparations. Rapidly growing cultures appeared to be more resistant to M-1 N-acetylmuramidase digestion than did slower-growing cultures. Agar gel diffusion studies demonstrated that both serotype d and RGP antigens were present in all samples, although significantly less RGP antigen was noted in the pH 7.5 culture. These observations were confirmed by quantitative precipitation assays. M-1 N-acetylmuramidase digests of the pH 7.5 culture were lacking in RGP precipitation activity although RGP inhibition activity was demonstrated. The data suggest that the cell content of serotype d antigen was relatively constant under the growth conditions tested, whereas the synthesis of RGP antigen was modified under conditions of high pH.

Antigens, Bacterial↗
PubMed2000

Identification of the operon for the sorbitol (Glucitol) Phosphoenolpyruvate:Sugar phosphotransferase system in Streptococcus mutans.

Transposon mutagenesis and marker rescue were used to isolate and identify an 8.5-kb contiguous region containing six open reading frames constituting the operon for the sorbitol P-enolpyruvate phosphotransferase transport system (PTS) of Streptococcus mutans LT11. The first gene, srlD, codes for sorbitol-6-phosphate dehydrogenase, followed downstream by srlR, coding for a transcriptional regulator; srlM, coding for a putative activator; and the srlA, srlE, and srlB genes, coding for the EIIC, EIIBC, and EIIA components of the sorbitol PTS, respectively. Among all sorbitol PTS operons characterized to date, the srlD gene is found after the genes coding for the EII components; thus, the location of the gene in S. mutans is unique. The SrlR protein is similar to several transcriptional regulators found in Bacillus spp. that contain PTS regulator domains (J. Stülke, M. Arnaud, G. Rapoport, and I. Martin-Verstraete, Mol. Microbiol. 28:865-874, 1998), and its gene overlaps the srlM gene by 1 bp. The arrangement of these two regulatory genes is unique, having not been reported for other bacteria.

Amino Acid Sequence↗
PubMed1974

Acceleration of dextransucrase activity of Streptococcus mutans by secretory immunoglobulin A.

The effect of immunoglobulins on the activity of dextransucrase purified from Streptococcus mutans strain HS-6 is described. When human salivary immunoglobulin A (IgA) or colostral IgA, either natured or denatured, was incubated with dextransucrase, the rate of the dextran synthesis was markedly accelerated, whereas human serum IgA or IgG neither accelerated nor inhibited the enzyme activity. The results suggest that a portion unique for secretory IgA, the secretory component, might be related to the enzyme acceleration. On the other hand, specific rabbit antiserum against the dextransucrase inhibited completely dextran synthesis by the enzyme.

Animals↗
PubMed2005

A whole cell BIAcore assay to evaluate P1-mediated adherence of Streptococcus mutans to human salivary agglutinin and inhibition by specific antibodies.

Researchers now recognize the utility of surface plasmon resonance technology to evaluate interactions of microbial pathogens with host components. The surface adhesin and candidate vaccine antigen P1 of Streptococcus mutans, the main causative agent of dental caries, interacts with a high molecular weight glycoprotein called salivary agglutinin, or gp340, in the salivary pellicle. We optimized a BIAcore assay to measure P1-mediated Ca(2+) dependent binding of S. mutans whole cells to this physiological ligand immobilized on a Pioneer F1 sensor chip. Regeneration conditions allowed cells to be eluted from the sensor chip permitting multiple reuse of the agglutinin-coated surface. An isogenic P1-deficient S. mutans mutant did not bind to immobilized agglutinin demonstrating specificity of the detected interaction. Glutaraldehyde-fixation of bacterial cells showed the assay measured a whole cell-ligand interaction and was not an artifact of solubilized or leached proteins. Adherence inhibition assays demonstrated varying degrees of disruption of the S. mutans-agglutinin interaction by anti-P1 monoclonal antibodies recognizing different epitopes, whereas a polyclonal reagent demonstrated more complete inhibition. This report describes an improved method to assess salivary agglutinin-mediated adherence of S. mutans in vitro under physiological-like conditions and to evaluate the effectiveness of antibodies of differing specificities to inhibit binding.

Agglutinins↗
PubMed2000

Characterization of recombinant, ureolytic Streptococcus mutans demonstrates an inverse relationship between dental plaque ureolytic capacity and cariogenicity.

Dental caries results from prolonged plaque acidification that leads to the establishment of a cariogenic microflora and demineralization of the tooth. Urease enzymes of oral bacteria hydrolyze urea to ammonia, which can neutralize plaque acids. To begin to examine the relationship between plaque ureolytic activity and the incidence of dental caries, recombinant, ureolytic strains of Streptococcus mutans were constructed. Specifically, the ureABCEFGD operon from Streptococcus salivarius 57.I was integrated into the S. mutans chromosome in such a way that the operon was transcribed from a weak, cognate promoter in S. mutans ACUS4 or a stronger promoter in S. mutans ACUS6. Both strains expressed NiCl(2)-dependent urease activity, but the maximal urease levels in ACUS6 were threefold higher than those in ACUS4. In vitro pH drop experiments demonstrated that the ability of the recombinant S. mutans strains to moderate a decrease in pH during the simultaneous metabolism of glucose and urea increased proportionately with the level of urease activity expressed. Specific-pathogen-free rats that were infected with ACUS6 and fed a cariogenic diet with drinking water containing 25 mM urea and 50 microM NiCl(2) had relatively high levels of oral urease activity, as well as dramatic decreases in the prevalence of smooth-surface caries and the severity of sulcal caries, relative to controls. Urease activity appears to influence plaque biochemistry and metabolism in a manner that reduces cariogenicity, suggesting that recombinant, ureolytic bacteria may be useful to promote dental health.

Animals↗
PubMed2001

[Effects of immune bovine whey on sucrose-dependent adherence of Streptococcus mutans].

OBJECTIVE: The aim of this experiment is to explore the possible anti-carious mechanisms of immune bovine whey. METHODS: The immune milk was collected from cows immunized with cell associated glucosyltransferase(GFT) over-expression strain B-29-33 of Streptococcus mutans(S. mutans) MT8148. The control milk was obtained from non-immunized cows. The immune and control bovine whey were prepared by removing fat and casein. The effects of two kinds of bovine whey on sucrose-dependent adherence of S. mutans MT8148 were examined by using TTY media with five different volumes of the immune and the control milk, 100, 300, 500, 700 and 900 microliters respectively. The adherent rates were determined by reading the optical density. The adherent morphology was observed by using a scanning electron microscope(SEM). RESULTS: There was no significant difference in adherence of S. mutans MT8148 cells to the smooth glass surface among five doses with those of the control whey. The immune bovine whey inhibited the adherence of S. mutans. The adherent percentage was 84.37% at 100 microliters and decreased by 58.59% at 900 microliters. The inhibition was does-dependent. The difference of adherent morphology between the immune and control whey was noticeable at 900 microliters. The SEM revealed that cells of S. mutans MT8148 with the control whey were covered by large quantities of gelatinous material, but cells with the immune whey were clearly distinguished. CONCLUSION: The immune whey has inhibitory potential against the sucrose-dependent adherence of S. mutans.

Animals↗
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↗
PubMed2000

Characterization of the Streptococcus mutans pyruvate formate-lyase (PFL)-activating enzyme gene by complementary reconstitution of the In vitro PFL-reactivating system.

The act gene was identified and an act mutant as well as the pfl mutant was constructed in Streptococcus mutans. Pyruvate formate-lyase (PFL) activity was regenerated with the mixture of the respective cell extracts from these mutants by complementary reconstitution of the in vitro reactivating system. The S. mutans act gene encoded the sole enzyme able to activate the PFL protein in this organism.

Acetyltransferases↗
PubMed1974

Streptococcus mutans dextransucrase: requirement for primer dextran.

Dextran stimulation (priming) of the dextransucrase (EC 2.4.1.5) from Streptococcus mutans strain 6715 was studied. The dextransucrase activity in supernatant fluids from glucose-grown cultures was shown to be partially primer dependent. During extended storage at 4 C the enzyme retained its activity. However, the ability to make dextran became increasingly primer dependent. Hydroxylapatite-chromatographed enzyme preparations were completely dependent upon added dextran for rapid synthesis of methanol-insoluble glucan from sucrose. Half-maximal stimulation of new dextran synthesis occurred with dextran at a concentration of 2 to 3 muM and with a molecular weight of about 2,600. Neither glycogen, amylose, inulin, nor isomaltose functioned as primer. Studies with the dextransucrase activities detectable by in situ assay in polyacrylamide gels subjected to electrophoresis under nondenaturing conditions revealed that the major activity was detectable in the presence of sucrose alone and was stimulated by addition of primer dextran. The minor activity was only detected when primer dextran was present. Homogeneous preparations of both enzymes contained 30 to 40% carbohydrate.

Autoradiography↗
PubMed2004

Biofilm growth of Lactobacillus species is promoted by Actinomyces species and Streptococcus mutans.

The ability of oral bacteria to integrate within a biofilm is pivotal to their survival. A dependence on the amount of biofilm growth by noncoaggregating Lactobacillus rhamnosus and Lactobacillus plantarum on coculture with Actinomyces naeslundii, Actinomyces gerencseriae, Streptococcus mutans and Veillonella parvula was investigated using an artificial-mouth culture system. Biofilm formation by the lactobacilli in mono-culture was poor. In coculture with Actinomyces species the amount of L. rhamnosus increased 7-20 times and L. plantarum 4-7 times compared to its mono-culture biofilm. S. mutans also promoted substantial biofilm growth of lactobacilli but V. parvula had no effect. We conclude that these Actinomyces species promoted growth of key Lactobacillus species in a biofilm, as did S. mutans to a smaller extent, and that the ability of individual bacteria to form mono-culture biofilms is not necessarily an indicator of their survival and pathogenic potential in a complex multispecies biofilm community.

Actinomyces↗