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PubMed2005

[MGB probes detect Streptococcus mutans and Streptococcus sobrinus in real time].

OBJECTIVE: To detect and distinguish Streptococcus mutans (S. mutans) and Streptococcus sobrinus (S. sobrinus) quickly in epidemiology and investigate the distribution of S. mutans in the oral of children with rampant caries. METHODS: Designed minor groove binder (MGB) probes according to the gtf gene of S. mutans and S. sobrinus. Detected 9 reference strains of Streptococcus mutans group by MGB probes in real time and after cultivation. Evaluated the results of these two methods. 92 dental plaques from pre-school children with rampant caries were detected in real time with MGB probes. RESULTS: The primers could amplify the target sequences specificity and distinguished S. mutans and S. sobrinus from each other using MGB probes. Though the fluorescence occurred earlier in S. mutans than in S. sobrinus, they had the same results in nature. In 92 children with rampant caries, the detective ratio of S. mutans was 96.7% and that of S. sobrinus was 32.6%. All the samples which could detect S. sobrinus were positive for S. mutans. CONCLUSION: The primers and probe designed from gtf genes of S. mutans and S. sobrinus can amplify the target sequence and distinguish them from each other in real time.

Child↗
PubMed1992

DNA probes for detection of cariogenic Streptococcus mutans.

Streptococcus mutans has been identified as the principal etiological agent in human dental caries. Therefore, the specificity and sensitivity of 3 potential gene probes derived from S. mutans GS5 have been examined as potential reagents for detecting the cariogenic bacteria. The gene probes derived from the cloned gtfB, gtfD and ftf genes were examined in Southern blots with a panel of representative oral bacteria. The gtfB and ftf genes were apparently specific for S. mutans under high-stringency hybridization conditions. However, the gtfD gene fragment did cross-hybridize with the DNA from other mutans streptococci. These results suggest that gtfB and ftf gene fragments may be used as specific probes for S. mutans.

Blotting, Southern↗
PubMed2004

Activation of plasminogen by Streptococcus mutans.

Streptococcus mutans, a member of the viridans streptococci, is the etiologic agent of dental caries and is also a causative agent of subacute infective endocarditis. The generation of proteolytic molecules, such as plasmin, may be important in the pathogenesis of endocarditis caused by S. mutans. In this study, we demonstrate that S. mutans cells have the ability to bind and activate plasminogen to plasmin. Incubation of S. mutans cells with plasminogen was found to be sufficient for the activation of plasminogen, which suggests the presence of an endogenously produced plasminogen activator. The plasmin activity generated by S. mutans cells was shown to be inhibited by epsilon-aminocaproic acid, lysine, aprotinin, and alpha(2)-macroglobulin. We also show that S. mutans cells have the ability to bind and activate plasminogen from human plasma as well as human serum. The plasmin activity generated on the surface of S. mutans cells could degrade the extracellular matrix molecule, fibronectin.

Enzyme Activation↗
PubMed2004

Virulence properties of Streptococcus mutans.

Streptococcus mutans is considered one of the primary causative agents of dental caries and can also be a source of infective endocarditis. The main virulence factors associated with cariogenicity include adhesion, acidogenicity, and acid tolerance. Each of these properties works coordinately to alter dental plaque ecology. The ecological changes are characterized by increased proportions of S. mutans and other species that are similarly acidogenic and aciduric. The selection for a cariogenic flora increases the magnitude of the drop in pH following the fermentation of available carbohydrate and increases the probability of enamel demineralization. This review focuses on the bacterial components that contribute to each of the major virulence properties. Further understanding of how these components work together in the development of dental caries will be aided by the recent completion of the sequence of the S. mutans genome and experimental designs that model the dental plaque biofilm.

Bacterial Adhesion↗
PubMed2004

Both lactoferrin and iron influence aggregation and biofilm formation in Streptococcus mutans.

Streptococcus mutans, a gram-positive immobile bacterium, is an oral pathogen considered to be the principal etiologic agent of dental caries. Although some researches suggest that trace metals, including iron, can be associated with dental caries, the function of salivary iron and lactoferrin in the human oral cavity remains unclear. The data reported in this study indicates that iron-deprived saliva (Fe3+ < 0.1 microM) increases S. mutans aggregation and biofilm formation in the fluid and adherent phases as compared with saliva (Fe3+ from 0.1 to 1 microM), while iron-loaded saliva (Fe3+ > 1 microM) inhibits both phenomena. Our findings are consistent with the hypothesis that S. mutans aggregation and biofilm formation are negatively iron-modulated as confirmed by the different effect of bovine lactoferrin (bLf), added to saliva at physiological concentration (20 microg/ml) in the apo- or iron-saturated form. Even if saliva itself induces bacterial aggregation, iron binding capability of apo-bLf is responsible for the noticeable increase of bacterial aggregation and biofilm development in the fluid and adherent phases. On the contrary, iron-saturated bLf decreases aggregation and biofilm development by supplying iron to S. mutans. Therefore, the iron-withholding capability of apo-Lf or native Lf is an important signal to which S. mutans counteracts by leaving the planktonic state and entering into a new lifestyle, biofilm, to colonize and persist in the human oral cavity. In addition, another function of bLf, unrelated to its iron binding capability, is responsible for the inhibition of the adhesion of S. mutans free, aggregated or biofilm on abiotic surfaces. Both these activities of lactoferrin, related and unrelated to the iron binding capability, could have a key role in protecting the human oral cavity from S. mutans pathogenicity.

Animals↗
PubMed2003

The role of glucan-binding proteins in the cariogenicity of Streptococcus mutans.

Streptococcus mutans produces glucan-binding proteins (Gbps), which appear to contribute to the virulence of S. mutans. GbpA and GbpC genes were inactivated by the insertion of antibiotic-resistant genes into each gbp gene of S. mutans MT8148 to generate Gbp-defective mutants. Sucrose dependent adherences of the GbpA- and GbpC-defective mutants were found to be significantly lower than those of their parent strains MT8148. Caries inducing activity of the mutants in rats was significantly lower than that of strain MT8148R (streptomycin-resistant strain of MT8148). These results suggest that GbpA and GbpC participate in cellular adherence to tooth surfaces and contribute to the cariogenicity of S. mutans.

Adhesins, Bacterial↗
PubMed1983

Binding of Todd-Hewitt broth antigens by Streptococcus mutans.

Streptococcus mutans 10449, grown in chemically defined culture medium, was tested for its ability to bind 3H-labeled Todd-Hewitt broth components (greater than 12,000 Mr). Maximum adsorption of radioactivity occurred within 5 min at room temperature, and cell-bound material was not completely removed by extended washing with buffer. Heat-killed, arsenate-inhibited, and viable bacteria bound similar quantities. Only 0.09% of the radioactivity in the preparation of high Mr Todd-Hewitt broth components was removed by absorption with excess numbers of S. mutans 10449 cells. Binding followed saturation kinetics and was competitively inhibited by unlabeled medium components, both the dialyzable and nondialyzable fractions. Other oral streptococci were also found to bind these complex medium components. Rabbit antiserum elicited to the high-molecular-weight Todd-Hewitt broth components reacted with monkey cardiac muscle and with S. mutans coated with medium components. Absorption of the anti-Todd-Hewitt broth serum with homogenized heart removed antibodies that reacted with Todd-Hewitt broth-coated S. mutans. Therefore, the tissue-specific antigens of this beef heart infusion medium that adsorb to S. mutans can interfere with the detection and characterization of antigens shared by these bacteria and animal tissues.

Adsorption↗
PubMed2002

Functional genomics approach to identifying genes required for biofilm development by Streptococcus mutans.

Streptococcus mutans, the primary etiological agent of human dental caries, is an obligate biofilm-forming bacterium. The goals of this study were to identify the gene(s) required for biofilm formation by this organism and to elucidate the role(s) that some of the known global regulators of gene expression play in controlling biofilm formation. In S. mutans UA159, the brpA gene (for biofilm regulatory protein) was found to encode a novel protein of 406 amino acid residues. A strain carrying an insertionally inactivated copy of brpA formed longer chains than did the parental strain, aggregated in liquid culture, and was unable to form biofilms as shown by an in vitro biofilm assay. A putative homologue of the enzyme responsible for synthesis of autoinducer II (AI-2) of the bacterial quorum-sensing system was also identified in S. mutans UA159, but insertional inactivation of the gene (luxS(Sm)) did not alter colony or cell morphology or diminish the capacity of S. mutans to form biofilms. We also examined the role of the homologue of the Bacillus subtilis catabolite control protein CcpA in S. mutans in biofilm formation, and the results showed that loss of CcpA resulted in about a 60% decrease in the ability to form biofilms on an abiotic surface. From these data, we conclude that CcpA and BrpA may regulate genes that are required for stable biofilm formation by S. mutans.

Amino Acid Sequence↗
PubMed1997

Identification and analysis of a collagenolytic activity in Streptococcus mutans.

Streptococcus mutans is an important pathogen in coronal caries and is implicated in dental root decay by its ability to bind collagen from various sources. In the present study, electron microscopic analysis demonstrated the ability of S. mutans to bind and to disrupt collagen fibrils of the amniotic membrane. The synthetic peptide FALGPA, which is similar in structure to collagen, was degraded by S. mutans, with a lower level of FALGPA hydrolytic activity observed in sucrose-grown cells compared with cells grown in the absence of sucrose. Inhibition studies of FALGPA hydrolytic activity showed a pattern characteristic of collagenase activity, with inhibition by 1,10-phenanthroline and EDTA, but not by phenylmethylsulfonyl fluoride (PMSF). Additionally, immunological cross-reactivity was observed between proteins from disrupted cells of S. mutans and antiserum to collagenase from Clostridium histolyticum. Gelatinolytic activity was demonstrated by gelatin zymogram analysis. These findings suggest that collagenolytic activity by S. mutans may be an important virulence factor in dental root decay.

Amnion↗
PubMed1982

Humoral and cell-mediated responses to a ribosomal preparation from Streptococcus mutans.

Streptococcus mutans 6715 ribosomes disrupted in a Braun homogenizer were isolated in sodium dodecyl sulfate by differential centrifugation. This preparation contained 80% RNA and 20% protein, and carbohydrate was not detected by phenol-sulfuric acid and methyl pentose assays. The sedimentation coefficient of the ribosomes was 70S. After dialysis in 0.01 M phosphate buffer containing 10(-4) M MgCl2, the ribosomes dissociated into 54S and 32S particles. Leukocytes from rabbits immunized intramuscularly with the ribosomal preparation showed transformation and migration indices of 13.0 and 0.71, which were significantly different (P less than 0.05) from the respective indices of 0.9 and 0.98 in nonimmunized animals. Hyperimmune serum from these rabbits agglutinated representative Formalin-killed strains of all seven serotypes of S. mutans, inhibited adherence of live S. mutans 6715 to glass, and agglutinated S. mutans 6715 ribosomes adsorbed upon erythrocytes. These findings suggested that animals immunized with S. mutans ribosomes may be protected from caries caused by any of the seven serotypes of this organism.

Agglutination Tests↗
PubMed1985

Colonization of the human oral cavity by a strain of Streptococcus mutans.

Streptococcus mutans strain JH1001 produces a bacteriocin that can kill virtually all other strains of this micro-organism. The ability of JH1001 to colonize the human oral cavity was tested in a study involving five subjects and three different infection regimens, all of which involved multiple exposures to large numbers of organisms. Two and one-half years after infection, JH1001 was found to have persistently colonized three of the subjects. The indigenous S. mutans in one subject were reduced below the level of detection. Levels of (total) S. mutans and S. sanguis were not affected in persistently colonized subjects. Mutants of indigenous S. mutans resistant to the bacteriocin were not observed. The results indicate the importance of host variability and infection regimen for superinfection by this strain of S. mutans. The efficient replacement of indigenous S. mutans by JH1001 in one subject lends support to the eventual application of replacement therapy to the prevention of dental caries.

Bacteriocins↗
PubMed2003

Biochemical and functional properties of a pyruvate formate-lyase (PFL)-activating system in Streptococcus mutans.

Streptococcus mutans has an oxygen-sensitive enzyme, pyruvate formate-lyase (PFL), which is a key enzyme in anaerobic sugar fermentation. We have shown that S. mutans has an activating system, including a PFL-activating enzyme (PFL-activase) and an electron transport system; the latter transfers an electron from NADPH to PFL-activase, as occurs in Escherichia coli. NADPH was a physiological electron donor for the electron transport system and as little as 0.02 mM NADPH activated over 80% of PFL of S. mutans. The optimum pH of the PFL-activating system was around 6.8, whereas the optimum of the E. coli system is at alkaline pH. In addition, small dialyzable molecules in cell-free extracts participated in keeping PFL active in S. mutans. These results suggest that, in dental plaque under anaerobic conditions where sugar supply is often limited or pH frequently falls below neutrality, S. mutans always keeps PFL active through the activating system.

Acetyltransferases↗
PubMed2005

Identification of nlmTE, the locus encoding the ABC transport system required for export of nonlantibiotic mutacins in Streptococcus mutans.

Streptococcus mutans UA159, the genome sequence reference strain, exhibits nonlantibiotic bacteriocin (mutacin) activity. In this study, we have combined bioinformatic and mutational analyses to identify the ABC transporter designated NlmTE, which is required for mutacin biogenesis in strain UA159 as well as in another mutacin producer, S. mutans N.

ATP-Binding Cassette Transporters↗
PubMed2005

Transport and metabolism of citrate by Streptococcus mutans.

Streptococcus mutans, a normal inhabitant of dental plaque, is considered a primary etiological agent of dental caries. Two virulence determinants of S. mutans are its acidogenicity and aciduricity (the ability to produce acid and the ability to survive and grow at low pH, respectively). Citric acid is ubiquitous in nature; it is a component of fruit juices, bones, and teeth. In lactic acid bacteria citrate transport has been linked to increased survival in acidic conditions. We identified putative citrate transport and metabolism genes in S. mutans, which led us to investigate citrate transport and metabolism. Our goals in this study were to determine the mechanisms of citrate transport and metabolism in S. mutans and to examine whether citrate modulates S. mutans aciduricity. Radiolabeled citrate was used during citrate transport to identify citrate metal ion cofactors, and thin-layer chromatography was used to identify metabolic end products of citrate metabolism. S. mutans was grown in medium MM4 with different citrate concentrations and pH values, and the effects on the growth rate and cell survival were monitored. Intracellular citrate inhibited the growth of the bacteria, especially at low pH. The most effective cofactor for citrate uptake by S. mutans was Fe(3+). The metabolic end product of citrate metabolism was aspartate, and a citrate transporter mutant was more citrate tolerant than the parent.

Biological Transport↗
PubMed1987

Relationship between growth rate and phagocytosis susceptibility in Streptococcus mutans.

Streptococcus mutans strain GS-5 was grown in a variety of carbon sources in order to achieve different balanced growth rates, ranging from 61 to 383 minutes. The influence of the S. mutans growth rate on mouse phagocyte activity against these bacteria has been evaluated. The percentages of bacteria phagocytized and intracellularly killed by macrophages rose to 60-80% and 85-95% respectively when the doubling time was longer, showing that S. mutans is particularly sensitive to nonspecific immune defence mechanisms when cultured under conditions similar to those of its natural ecosystem.

Animals↗
PubMed2005

Peptide pheromone induced cell death of Streptococcus mutans.

Streptococcus mutans is considered one of the main causative agents of human dental caries. Cell-cell communication through two-component signal transduction systems (TCSTS) plays an important role in the pathogenesis of S. mutans. One of the S. mutans TCSTS, ComDE, controls both competence development and biofilm formation. In this study, we showed that addition of exogenous competence-stimulating peptide (CSP) beyond the levels necessary for competence inhibited the growth of S. mutans in a ComDE-dependent manner. We also demonstrated that further increases of CSP stopped S. mutans cell division leading to cell death. Use of CSP as a possible therapeutic agent is discussed.

Bacterial Proteins↗
PubMed2002

Genes involved in bacitracin resistance in Streptococcus mutans.

Streptococcus mutans is resistant to bacitracin, which is a peptide antibiotic produced by certain species of Bacillus. The purpose of this study was to clarify the bacitracin resistance mechanism of S. mutans. We cloned and sequenced two S. mutans loci that are involved in bacitracin resistance. The rgp locus, which is located downstream from rmlD, contains six rgp genes (rgpA to rgpF) that are involved in rhamnose-glucose polysaccharide (RGP) synthesis in S. mutans. The inactivation of RGP synthesis in S. mutans resulted in an approximately fivefold-higher sensitivity to bacitracin relative to that observed for the wild-type strain Xc. The second bacitracin resistance locus comprised four mbr genes (mbrA, mbrB, mbrC, and mbrD) and was located immediately downstream from gtfC, which encodes the water-insoluble glucan-synthesizing enzyme. Although the bacitracin sensitivities of mutants that had defects in flanking genes were similar to that of the parental strain Xc, mutants that were defective in mbrA, mbrB, mbrC, or mbrD were about 100 to 120 times more sensitive to bacitracin than strain Xc. In addition, a mutant that was defective in all of the mbrABCD genes and rgpA was more sensitive to bacitracin than either the RGP or Mbr mutants. We conclude that RGP synthesis is related to bacitracin resistance in S. mutans and that the mbr genes modulate resistance to bacitracin via an unknown mechanism that is independent of RGP synthesis.

Anti-Bacterial Agents↗