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PubMed2005

Early acquisition of Streptococcus mutans for children.

Existing evidence reveals that in Early Oral Infection the main route of transmission of Streptococcus mutans is mother-child saliva contacts and that initial acquisition takes place during a specific period of time denominated "Window of Infectivity" that lapses between 6 and 30 months of the child's life, with a higher risk between 18 and 30 months of age. The aim of the present study was to analyze Early Oral Infection. The levels of Streptococcus mutans in saliva and bacterial plaque in the binomial mother-child 6 to 18 months after childbirth were evaluated. Twenty-four mother-child binomials that attended the University Hospital of Maternity and Neonatology of Córdoba participated in the study. Samples of saliva and dental plaque were taken from mother and child and seeded in selective Agar Mitis Salivarius Bacitracin medium (0.28 mg/ml) and cultured for 48 hours at 37 degrees C and in 5% CO2 to allow for the growth of Streptococcus mutans. The colonies were identified morphologically and biochemically. At 6 months after childbirth: 58.33% of the samples of the mother's saliva were positive, while the presence of the microorganism was not detected in 100% of the samples of the infants' saliva. At 18 months of after childbirth: 79.16% of the samples of saliva and 100% of the samples of the mothers' dental plaque were positive, whereas the samples of saliva and dental plaque of the infants were positive for Streptococcus mutans in 20.83% and 70.83% of the cases respectively. The initial acquisition of Streptococcus mutans would have occurred in 20.8% of the children at the age of 18 months. Eruption of primary molars occurs at this age.

Age Factors↗

PubMed1988

Immunological properties of the primer-independent glucosyltransferase of Streptococcus mutans serotypes d and g.

Streptococcus mutans serotype g secretes at least three kinds of glucosyltransferase with different enzymological and immunological properties. One of them is a primer-independent enzyme and seems to be the source of primer for the others, both of which are primer-dependent enzymes. Recently, we purified the primer-independent enzyme, the third glucosyltransferase in this group from S. mutans strain AHT-k serotype g. In the present study, we examined the specificity of the antiserum against the primer-independent glucosyltransferase using extracellular culture-conditioned fluids of many strains of the various serotypes of S. mutans. The antiserum cross-reacted with the extracellular culture fluids from strains of serotypes d and a, in addition to serotype g, but not with those of other serotypes, indicating that the primer-independent glucosyltransferase is secreted by the S. sobrinus and S. cricetus, but not by S. mutans and S. rattus. The antiserum did not completely inhibit the activity of the enzyme, even at more than twofold antibody excess, determined by indirect precipitation with immobilized staphylococcal protein A.

Animals↗

PubMed2006

Identification of genetic differences between two clinical isolates of Streptococcus mutans by suppression subtractive hybridization.

Streptococcus mutans is generally considered to be the principal aetiological agent for dental caries. Phenotypic variation in strains is often associated with differences in gene content, so the isolation of DNA fragments from these genes or associated regions is illuminating. The S. mutans strains 9-1 and 9-2, which both colonized the same oral cavity, were selected after screening for the possession of suspected virulence traits. Genomic DNA of strain 9-1 was used as the tester, and that of 9-2 was used as the driver. Suppression subtractive hybridization (SSH) was applied between the tester and the driver DNAs. The subtractive products were cloned into a pCR2.1 vector. Clone libraries representing sequence differences were obtained. The subtractive fragments that were found specifically in strain 9-1 but not in strain 9-2 were identified by dot blotting and then sequenced. BLASTn and BLASTx sequence homology analyses were subsequently performed. Twenty-seven sequences were found in the genome of strain 9-1 that were not in 9-2. Among them, three revealed no homology to published nucleotide sequences while the remaining sequences showed 81-100% homology to known genes of S. mutans strain UA159. These sequences are involved in competence development, signal transduction and transcriptional regulation, repairing stress damage, transport, carbohydrate catabolism, biochemical synthesis, or unknown functions. Differences exist in the genomes of different S. mutans isolates. SSH is effective in screening for S. mutans strain specific DNA sequences.

Adult↗

PubMed1980

Excretion of extracellular lipids by Streptococcus mutans BHT and FA-1.

Streptococcus mutans BHT and FA-1, when grown to log phase on chemically defined medium containing [14C]glycerol, excreted 15% of the total biosynthesized 14C-lipid into the medium. When grown to early stationary phase, 28 to 33% of the 14C-lipid was found in the medium. The radioactive lipids of these varieties of S. mutans were identified as diacylglycerol, diglucosyl diacylglycerol (DGD), monoglucosyl diacylglycerol, diphosphatidylglycerol, phosphatidylglycerol (PG), and smaller amounts of two other lipids tentatively were identified as amino acyl-PG and glycerol phosphoryl-DGD. All lipids were found as extracellular and intracellular components from cells grown to either log or stationary phase. However, there were some shifts in the relative percentage of these lipids as the cells changed from log to stationary phase. For example, the intracellular lipid content of log-phase S. mutans BHT was composed of 49% PG and 19% DGD, but these percents shifted to 18% PG and 57% DGD when the cells were grown to stationary phase. However, the extracellular lipids of this organism contained 50 to 60% PG and 20% DGD in both log and stationary phases.

Cardiolipins↗

PubMed2004

Streptococcus mutans fructosyltransferase interactions with glucans.

Streptococcus mutans utilizes sucrose to synthesize glucans by glucosyltransferase and fructans by fructosyltransferase (FTF). Antibodies raised against a recombinant FTF were used to study S. mutans FTF secretion. Low amounts of cell-free FTF were found in culture of S. mutans grown with sucrose, while an increase in bacteria displaying cell surface FTF was detected. FTF added to S. mutans cultures was adsorbed to bacteria grown with sucrose but not to bacteria grown with glucose or fructose or to a gtf inactivated mutant grown with sucrose. Recombinant FTF was found to have high affinity for glucans suggesting that fructans and glucans are an integral part of the polysaccharide matrix of oral biofilms.

Biofilms↗

PubMed1982

Involvement of oxygen-sensitive pyruvate formate-lyase in mixed-acid fermentation by Streptococcus mutans under strictly anaerobic conditions.

Streptococcus mutans JC2 produced formate, acetate, ethanol, and lactate when suspensions were incubated with an excess of galactose or mannitol under strictly anaerobic conditions. The galactose- or mannitol-grown cell suspensions produced more formate, acetate, and ethanol than the glucose-grown cells even when incubated with glucose. The levels of lactate dehydrogenase and fructose 1,6-bisphosphate were not significantly different in these cells, but the level of pyruvate formate-lyase was higher in the galactose- or mannitol-grown cells, and that of triose phosphate was lower in the galactose-grown cells. This suggests that the regulation of pyruvate formate-lyase may play a major role in the change of the fermentation patterns. The cells of S. mutans grown on glucose produced a significant amount of volatile products even in the presence of excess glucose under strictly anaerobic conditions. However, when the anaerobically grown cells were exposed to air, only lactate was produced from glucose. When cells were anaerobically grown on mannitol and then exposed to air for 2 min, only trace amounts of fermentation products were formed from mannitol under anaerobic conditions. It was found that the pyruvate formate-lyase in the cells was inactivated by exposure of the cells to air.

Acetates↗

PubMed1980

Effect of cultural conditions on trimethylsilyl-sugar profiles of Streptococcus mutans.

The cellular carbohydrates of Streptococcus mutans NCTC 10832 were converted to methyl glycoside trimethylsilyl ethers and analyzed by gas-liquid chromatography. The resulting profiles revealed the presence of glycerol, xylose, rhamnose, galactose, glucose, N-acetylglucosamine, and N-acetylmuramic acid. The proportions of monosaccharides in the profile were found to be stable with respect to changing growth temperature or duration of growth. However, the type of medium used, and its carbohydrate content, did significantly alter the profile, whereas gaseous atmosphere exerted a lesser effect on carbohydrate composition. By controlling growth parameters, we obtained reproducible profiles. Whole cells are probably a satisfactory alternative to highly purified cell walls.

Carbon Dioxide↗

PubMed1991

Metabolism of intracellular polysaccharide in the cells of Streptococcus mutans under strictly anaerobic conditions.

Streptococcus mutans, which had accumulated glycogen-like iodophilic intracellular polysaccharide (IPS), produced large amounts of formate, acetate and ethanol from the IPS by pyruvate formate-lyase (PFL) under strictly anaerobic conditions without exogenous sugar. Under aerobic conditions, the same S. mutans produced exclusively lactate and pyruvate from the IPS because of the inactivation of PFL by oxygen. The total amount of acid produced under anaerobic conditions was larger than that under aerobic conditions. The analysis of intracellular glycolytic intermediates revealed that levels of fructose 1,6-bisphosphate (lactate dehydrogenase (LDH) activator) and glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (PFL inhibitors) were low when IPS was used as a glycolytic substrate, implying that PFL functions more efficiently than LDH in IPS metabolism. These findings suggest that the PFL pathway contributes to the acid production from IPS, and may explain partially why the acids in starved dental plaque are mainly acetate and formate.

Acetates↗

PubMed1984

Transport of glucose and mannose by a common phosphoenolpyruvate-dependent phosphotransferase system in Streptococcus mutans GS5.

Decryptified cells of Streptococcus mutans GS5 transport glucose, mannose, and fructose by constitutive phosphoenolpyruvate-dependent phosphotransferase systems (PTSs). Although the non-metabolizable glucose analog 2-deoxyglucose is transported by a PTS, alpha-methylglucose is not taken up by strain GS5. The transport of [14C]mannose and [14C]glucose was almost totally blocked by the heterologous sugars, indicating that these substrates may share a common PTS permease. [14C]fructose transport, however, was not inhibited by large excesses of glucose, indicating the existence of a separate fructose PTS. All "tight" glucose PTS- mutant clones studied were also unable to transport mannose, whereas some "leaky" glucose PTS- clones also were leaky for mannose phosphorylation. Fructose transport in most of these mutant strains was unimpaired, indicating that genetic lesions did not involve soluble (cytoplasmic) PTS components.

Binding, Competitive↗

PubMed1984

Immunogenicity, biochemical and serological characterizations of ribosomal preparations from human oral strains of serotypes c and d of the bacterium Streptococcus mutans.

Crude ribosomal preparations of Streptococcus mutans C67-1 (serotype c) and 50B4 (serotype d) contain protein RNA and carbohydrate. Sepharose CL-2B column chromatography of preparations yielded two distinct peaks. Cell-wall carbohydrates were predominantly present in peak I; the serological activity resided mainly in peak II. The preparations contained antigens which cross-reacted with several streptococcal Lancefield antisera. Antisera prepared against the preparations cross-reacted with cell-wall proteins (NaCl extracts) and Ag I/II, but not with cell-wall carbohydrate antigens (Rantz-Randall extracts). Thus, cell-envelope protein antigens in the preparations appear to be responsible for the serological activity. The unique properties of ribosomal preparations may, apart from serological cross-reactivity, be useful in the immunological protection against dental caries.

Antibody Formation↗

PubMed2002

gbpC and pac gene mutations detected in Streptococcus mutans strain GS-5.

The Streptococcus mutans gbpC gene encoding cell wall-anchoring glucan-binding protein C is involved in the dextran(alpha-1,6 glucan)-dependent aggregation (ddag) of this organism. Unlike cells of other strains of S. mutans, strain GS-5 cells did not exhibit dextran(alpha-1,6 glucan)-dependent aggregation under any conditions. We therefore hypothesized that the gbpC gene may be mutated in strain GS-5. Sequencing analysis of the 1752-nucleotide GS-5 gbpC gene revealed a point mutation that switched codon 65 to a TAA termination codon. Strain GS-5 was previously reported also to have a mutation in the pac gene encoding the cell wall-anchored major protein antigen. The laboratory-maintained strain GS-5 is regarded as having lower cariogenicity than the original isolate. The decreased cariogenicity developed during the laboratory culture of strain GS-5 may have been caused by mutations in an environment lacking appropriate selective pressures.

Antigens, Bacterial↗

PubMed2005

Identification of genes associated with mutacin I production in Streptococcus mutans using random insertional mutagenesis.

Streptococcus mutans is a major pathogen implicated in dental caries. Its virulence is enhanced by its ability to produce bacteriocins, called mutacins, which inhibit the growth of other Gram-positive bacteria. The goal of this study is to use a random insertional mutagenesis approach to search for genes that are associated with mutacin I production in the virulent strain UA140. A random insertional mutagenesis library consisting of 11,000 clones was constructed and screened for a mutacin-defective phenotype. Mutacin-defective clones were isolated, and their insertion sites were determined by PCR amplification or plasmid rescue followed by sequencing. A total of twenty-five unique genes were identified. These genes can be categorized into the following functional classes: two-component sensory systems, stress responses, energy metabolism and central cellular processes. Several conserved hypothetical proteins with unknown functions were also identified. These results suggest that mutacin I production is stringently controlled by diverse and complex regulatory pathways.

Bacteriocins↗

PubMed2006

A novel signal transduction system and feedback loop regulate fructan hydrolase gene expression in Streptococcus mutans.

The fruA gene of Streptococcus mutans encodes for a secreted fructan hydrolase (fructanase), an established virulence determinant required for releasing D-fructose from levan- and inulin-type fructans. Expression of fruA is under the control of carbon catabolite repression and is induced by growth in fructans. In this report, we identified an operon in S. mutans UA159 encoding a two-component system flanked by two predicted carbohydrate-binding proteins that is absolutely required for the expression of fruA. All four genes were found to be required for optimal growth of S. mutans on inulin-containing medium and for transcriptional activation of fruA. Complementation assays using a plasmid expressing the response regulator suggested that the two-component system works in concert with the sugar-binding proteins. This operon was also shown to activate a four-gene cluster located immediately downstream and encoding an Enzyme II (EII(Lev)) for a fructose/mannose sugar : phosphotransferase enzyme, which was found to negatively regulate the expression of fruA. Using transcriptional fusions, it was found that fructose could signal induction of the fruA and levD operons through the two-component system/sugar-binding protein complex. A recombinant LevR protein was shown to bind to the promoter regions of fruA and levD in gel mobility shift assays. Thus, a 'four-component signal transduction system' activates fructan catabolism and the expression of an Enzyme II complex that functions in a feedback loop to sense the accumulation of the end-product of fructan degradation.

Bacterial Proteins↗

PubMed1983

Effect of adsorbed protein on hydroxyapatite zeta potential and Streptococcus mutans adherence.

The adherence of Streptococcus mutans PK1 to hydroxyapatite disks pretreated with various acidic and basic proteins in imidazole buffer was studied. Adsorption of a basic protein onto an hydroxyapatite disk enhanced or had no effect on bacterial adherence, whereas adsorption of an acidic protein reduced adherence. The effect of adsorbed protein on bacterial adherence was of both short and long range. The long-range effect of the acidic proteins in reducing the number of bacteria adhering to hydroxyapatite was related to protein adsorption causing an increase in surface net negative charge, as shown by zeta potential measurement. Basic protein produced a net positive surface charge which facilitated adherence. Within the acidic protein group, the acidic residue percentage of the adsorbed protein was negatively correlated with the number of bacteria adhering, whereas the nonpolar residue percentage was positively correlated with bacterial adherence. Within the basic protein group, the basic residue percentage was correlated with the number of cells adhering. These results indicate the involvement of short-range hydrophobic and ionic interactions in bacterial adherence to protein-coated hydroxyapatite.

Adhesiveness↗

PubMed1987

Expression, purification, and characterization of an exo-beta-D-fructosidase of Streptococcus mutans.

A genetic library of Streptococcus mutans GS-5, constructed in an Escherichia coli plasmid vector, was screened for cells which could utilize sucrose as the sole carbon and energy source. The recombinant plasmid pFRU1, containing a 4.2-kilobase pair insert of S. mutans DNA, was shown to confer this phenotype. Further characterization of the gene product encoded by pFRU1 revealed that the enzyme was a beta-D-fructosidase with the highest specificity for the beta (2----6)-linked fructan polymer levan. The enzyme could also hydrolyze inulin [beta (2----1)-linked fructan], sucrose, and raffinose with 34, 21, and 12%, respectively, of the activity observed for levan. The gene (designated fruA) appeared to be expressed under its own control in E. coli, as judged by the lack of influence on gene product activity of induction or repression of the beta-galactosidase promoter adjacent to the insertion site on the cloning vector. The protein was purified to homogeneity, as judged by silver staining of purified protein in denaturing and reducing conditions in polyacrylamide gels, from sonic lysate of E. coli, as well as from culture supernatants of S. mutans GS-5 grown in a chemostat at low dilution rate with fructose as the sole carbohydrate source. Both purified proteins had an apparent molecular mass of 140,000 daltons in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, were immunologically related and comigrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as determined by Western blotting with antisera raised against the cloned gene product, and were identical in all physical and biochemical properties tested. The pH optimum of the enzyme acting on fructan polymers was 5.5, with a significant amount of activity remaining at pH 4.0. The optimum pH for sucrose degradation was broader and lower, with a peak at approximately 4.5. Enzyme activity was inhibited almost completely by Hg2+ and Ag2+, inhibited partially by Cu2+, not inhibited by fluoride ion or Tris, and slightly stimulated by Mn2+ and Co2+. Fructan polymers were attacked exohydrolytically by the enzyme, fructose being the only product released. With sufficient time, both levan and inulin were degraded to completion, with no evidence of product inhibition.

Bacterial Proteins↗

PubMed1983

Mechanism of synthesis of D-glucans by D-glucosyltransferases from Streptococcus mutans 6715.

Two glucosyltransferases from Streptococcus mutans 6715 were purified and separated. One of the glucosyltransferases synthesized an insoluble glucan, and the other, a soluble glucan. The enzymes were immobilized on Bio-Gel P-2 beads, and the mechanism of glucan synthesis was studied by pulse and chase techniques with 14C-sucrose. Label was associated with the immobilized enzymes. The label could be quantitatively released by heating at pH 2. Analysis of the labeled products from the pulse experiment showed labeled glucose and labeled glucan; the chase experiment showed labeled glucan and a significant decrease in labeled glucose. The glucans from the pulse and the chase experiments were separated from glucose by chromatography on Bio-Gel P-6. They were reduced with sodium borohydride, and the products hydrolyzed with acid. Analysis of the labeled products from the reduced and hydrolyzed, pulsed glucans showed labeled glucose and labeled glucitol; label in the glucitol was greatly decreased in the chase experiment. These experiments showed that glucose and glucan were covalently attached to the active site of the enzymes during synthesis, and that the glucose was being transferred to the reducing end of the glucan chain. A mechanism for the synthesis of the glucans is proposed in which there are two catalytic groups on each enzyme that holds glucosyl and glucanosyl units. During synthesis, the glucosyl and glucanosyl units alternate between the two sites, giving elongation of the glucans from the reducing end. The addition of increasing amounts of B-512F dextran to the insoluble-glucan-forming glucosyltransferase produced a decrease in the proportion of insoluble glucan formed and a concomitant increase in a soluble glucan. The total amount of glucan synthesized (soluble plus insoluble) was increased 1.6 times over the amount of insoluble glucan formed when no exogenous dextran was added. It is shown that the addition of B-512F dextran affects the solubility of the synthesized alpha-(1 to 3)-glucan by accepting alpha-(1-3)-glucan chains at various positions along the dextran chain, to give a soluble, graft polymer.

Enzymes, Immobilized↗

PubMed2006

Streptococcus mutans glucan-binding protein-A affects Streptococcus gordonii biofilm architecture.

The glucan-binding protein-A (GbpA) of Streptococcus mutans has been shown to contribute to the architecture of glucan-dependent biofilms formed by this species and influence virulence in a rat model. As S. mutans synthesizes multiple glucosyltransferases and nonglucosyltransferase glucan-binding proteins (GBPs), it is possible that there is functional redundancy that overshadows the full extent of GbpA contributions to S. mutans biology. Glucan-associated properties such as adhesion, aggregation, and biofilm formation were examined independently of other S. mutans GBPs by cloning the gbpA gene into a heterologous host, Streptococcus gordonii, and derivatives with altered or diminished glucosyltransferase activity. The presence of GbpA did not alter dextran-dependent aggregation nor the initial sucrose-dependent adhesion of S. gordonii. However, expression of GbpA altered the biofilm formed by wild-type S. gordonii as well as the biofilm formed by strain CH107 that produced primarily alpha-1,6-linked glucan. Expression of gbpA did not alter the biofilm formed by strain DS512, which produced significantly lower quantities of parental glucan. These data are consistent with a role for GbpA in facilitating the development of biofilms that harbor taller microcolonies via binding to alpha-1,6-linkages within glucan. The magnitude of the GbpA effect appears to be dependent on the quantity and linkage of available glucan.

Bacterial Adhesion↗

PubMed1983

Effects of xylitol on the acid production activity from sorbitol by Streptococcus mutans and human dental plaque.

-A method for the determination of acid production from 20-25 mg (wet weight) of Streptococcus mutans and 12-33 mg (wet weight) of human dental plaque is described. After endogenous acid production had been followed, either sorbitol or xylitol or a mixture of sorbitol and xylitol (2:1) was added. After about ten minutes glucose, sucrose or Palatinose were added for a vitality test. Addition of xylitol to the bacterial suspension caused inhibition of acid production from sorbitol by Streptococcus mutans grown on sorbitol or a mixture of sorbitol and glucose. It was also observed that it had a similar effect on acid production from sorbitol in suspensions of dental plaque with few exceptions. On the other hand, Streptococcus mutans cells grown on glucose, sucrose and xylitol media, produced no or insignificant amounts of acid from sorbitol. Streptococcus mutans cells grown on media containing glucose, sucrose, sorbitol and a mixture of sorbitol and glucose generally formed a large amount of acid from glucose and sucrose after the addition of sorbitol and xylitol. However, Streptococcus mutans cells grown on a medium containing xylitol and the mixture of sorbitol and xylitol formed less acid from glucose. The acid production activity from sorbitol in suspensions of dental plaque after the xylitol addition was somewhat lower than the acid production from sorbitol alone (p less than 0.02).

Acids↗