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PubMed1983

Detection of antigens in enzymic lysates of cell wall from Streptococcus mutans strains.

Lysis of cell wall preparations from strains representing serotypes a - g of Streptococcus mutans has provided a convenient and efficient means of obtaining the typing antigens in a soluble undegraded form, and has demonstrated that, in each case, the antigen is a cell wall component in the strict sense of a component joined covalently to peptidoglycan. This influences the choice of extraction procedures.

Antigens, Bacterial↗

PubMed2006

Genomic variation in Streptococcus mutans: deletions affecting the multiple pathways of beta-glucoside metabolism.

The genome of Streptococcus mutans UA159 contains two phospho-beta-glucosidase genes, bglA and celA, which occur in operon-like arrangements along with genes for components of phosphotransferase transport systems and a third phospho-beta-glucosidase encoded by the arb gene, which does not have its own associated transport system but relies on uptake by the bgl or cel systems. Targeted inactivation of each of the phospho-beta-glucosidase genes revealed that bglA is involved in aesculin hydrolysis, celA is essential for utilisation of cellobiose, amygdalin, gentobiose and salicin, and arb is required for utilisation of arbutin. Inactivation of genes for the phosphotransferase systems revealed an overlap of specificity for transport of beta-glucosides and also indicated that further, unidentified transport systems exist. The cel and arb genes are subject to catabolite repression by glucose, but the regM gene is not essential for catabolite repression. Screening a collection of isolates of S. mutans revealed strains with deletions affecting the msm, bgl and/or cel operons. The phenotypes of these strains could largely be explained on the basis of the results obtained from the knockout mutants of S. mutans UA159 but also indicated the existence of other pathways apparently absent from UA159. The extensive genetic and phenotypic variation found in beta-glucoside metabolism indicates that there may be extensive heterogeneity in the species.

Amygdalin↗

PubMed1980

Laser light scattering measurement of dextran-induced Streptococcus mutans aggregation.

Intensity fluctuation spectroscopy was used to study dextran-induced aggregation of Streptococcus mutans bacteria. Smoluchowski's theory of colloidal flocculation provided a consistent model of the agglutination process. Our experiments indicated that aggregation was inhibited by the negatively charged surfaces of the cells, while dextran polymers effectively bound organisms together. Our experimental data were consistent with the quantitative predictions of a polymer bridge model of agglutination.

Biophysical Phenomena↗

PubMed1999

A novel gene required for rhamnose-glucose polysaccharide synthesis in Streptococcus mutans.

Gene rgpG is required for biosynthesis of rhamnose-glucose polysaccharide (RGP) in Streptococcus mutans. Its deduced amino acid sequence had similarity to WecA, which initiates syntheses of enterobacterial common antigen and some O antigens in Escherichia coli. Gene rgpG complemented a wecA mutation of E. coli, suggesting that rgpG may function similarly in RGP synthesis.

Cloning, Molecular↗

PubMed1974

Dissociation of plaque formation from glucan-induced agglutination in mutants of Streptococcus mutans.

The traits adhesion and cohesion are manifested in Streptococcus mutans by in vitro plaque formation and glucan-mediated agglutination and have been dissociated in mutants of this caries-associated microbe. In these mutants, which differ from each other in colonial morphology, we have observed a consistent loss of ability to form adhesive microbial deposits (plaque) on wires, but only a minimal alteration from the wild type in ability to agglutinate into macroscopic clumps in the presence of exogenous glucans or sucrose. Also, when these mutants were cultured in sucrose-containing medium, there was an increase in the synthesis of water-soluble, extracellular glucans and a decrease in the synthesis of alkali-soluble, cell-associated glucans. Based on these findings, it appears (i) that in vitro plaque formation and agglutination are distinct and dissociable traits, and (ii) that adhesion but not agglutination appears related to the synthesis of alkali-soluble, cell-associated glucans.

Agglutination↗

PubMed1978

Evaluation of a micromethod for determination of Streptococcus mutans and Lactobacillus infection.

A micromethod was developed for quantitative estimation in saliva of Streptococcus mutans and lactobacilli. With a semiautomatic pipette, 25 microliter of diluted saliva was spotted on the surface of an agar plate containing a selective medium. This volume gave a spot with a diameter of about 10 mm in which separate colonies could be counted. The results obtained with the spotting technique showed excellent agreement with those obtained with conventional agar plating. The method is convenient and results in a substantial saving of culture media.

Agar↗

PubMed2006

A lacticin 3147 enriched food ingredient reduces Streptococcus mutans isolated from the human oral cavity in saliva.

AIMS: To isolate and characterise Streptococcus mutans from Irish saliva samples and to assess their sensitivity to a food-grade preparation of the lantibiotic, lacticin 3147, produced by Lactococcus lactis DPC3147. METHODS AND RESULTS: Saliva samples collected from children with varying oral health status were screened on Mitis Salivarius agar for the presence of pathogenic streptococci. Following selective plating, 16S rDNA sequencing and Pulsed Field Gel Electrophoresis (PFGE), 15 distinct strains of Strep. mutans were identified. These were grouped according to their relative sensitivity to lacticin 3147 which ranged from 0.78 to 6.25%; relative to a sensitive indicator strain, Lactococcus lactis ssp. lactis HP. Inhibition of indicator Strep. mutans strains from sensitive, intermediate and tolerant groupings were assessed in microtitre plate assays with increasing concentrations of lacticin 3147. The concentration of lacticin 3147 required to give 50% growth inhibition correlated with their relative sensitivities (as assayed by well diffusion methodology) and ranged from 1280 to 5120 AU ml(-1). Concentrated preparations of lacticin 3147 caused a rapid killing of Strep. mutans strains in broth. Moreover, in human saliva deliberately spiked with Strep. mutans, the pathogen was eliminated (initial inoculum of 10(5)) in the presence of 40,000 AU ml(-1) of lacticin 3147. Furthermore, a food-grade lacticin 3147 spray dried powder ingredient was assessed for the inhibition of Strep. mutans in human saliva, spiked with a strain of intermediate sensitivity, resulting in up to a 4-log reduction in counts after 20 min. CONCLUSION: A food grade preparation of lacticin 3147 was effective in the inhibition of oral Strep. mutans. SIGNIFICANCE AND IMPACT OF THE STUDY: The inhibition of oral streptococci by food grade preparations of lacticin 3147 may offer novel opportunities for the development of lacticin 3147 as an anti-cariogenic agent particularly in the area of functional foods for the improvement of oral health.

Bacterial Proteins↗

PubMed2002

Analysis of a dextran-binding domain of the dextranase of Streptococcus mutans.

AIMS: To examine the dextran-binding domain of the dextranase (Dex) of Streptococcus mutans. METHODS AND RESULTS: Deletion mutants of the Dex gene of Strep. mutans were prepared by polymerase chain reaction and expressed in Escherichia coli cells. Binding of the truncated Dexs to dextran was measured with a Sephadex G-150 gel. Although the Dexs which lacked the N-terminal variable region lost enzyme activity, they still retained dextran-binding ability. In addition, further deletion into the conserved region from the N-terminal did not influence the dextran-binding ability. However, the Dex which carried a deletion in the C-terminus still possessed both enzyme activity and dextran-binding ability. Further deletion into the conserved region from the C-terminal resulted in complete disappearance of both enzyme and dextran-binding activities. CONCLUSIONS: Deletion analysis of the Dex gene of Strep. mutans showed that the C-terminal side (about 120 amino acid residues) of the conserved region of the Dex was essential for dextran-binding ability. SIGNIFICANCE AND IMPACT OF THE STUDY: The dextran-binding domain was present in a different area from the catalytic site in the conserved region of the Dex molecule. The amino acid sequence of the dextran-binding domain of the Dex differed from those of glucan-binding regions of other glucan-binding proteins reported.

Amino Acid Sequence↗

PubMed1992

Cloning of the phospho-beta-galactosidase gene in Escherichia coli from lactose-negative mutants of Streptococcus mutans isolated following random mutagenesis with plasmid pVA891 clone banks.

In order to mutagenize Streptococcus mutans a marker rescue plasmid, pVA891, was employed. The plasmid was ligated with Sau3AI digested chromosomal DNA fragments from S. mutans GS-5IS3 and the resultant plasmids were amplified in Escherichia coli. These plasmids were then randomly integrated into the chromosome of strain GS-5IS3 following transformation. Lactose-negative transformants were isolated as white colonies on lactose-BTR-Xgal agar plates containing erythromycin. Six lactose-negative mutants representing three different chromosomal sites of integration were isolated from about eight thousand transformants. Mutant chromosomal DNA fragments flanking the plasmids were recovered by a marker-rescue method in E. coli and exhibited phospho-beta-galactosidase activity.

Cloning, Molecular↗

PubMed2003

Characterization of a suppressor mutation complementing an acid-sensitive mutation in Streptococcus mutans.

We isolated a spontaneous suppressor mutant complementing the acid-sensitive phenotype of Streptococcus mutans strain Tn-1, a mutant previously generated in this laboratory, defective in the activity of the dgk-encoded putative undecaprenol kinase. A relatively simple genetic method was developed to identify the suppressor mutation, based on selection for transformants containing two closely linked markers: a selectable allele of the unknown suppressor gene and an antibiotic resistance gene introduced on a suicide plasmid at random sites into the chromosome via homologous recombination. While we have not actually identified the original suppressor mutation, another mutated gene restoring acid resistance has been isolated, which suggests a possible mechanism of suppression.

Acids↗

PubMed2000

Protein interactions of SGP, an essential Streptococcus mutans GTPase, revealed by biochemical and yeast two-hybrid system analyses.

SGP, a Streptococcus mutans essential GTPase, plays a role in the stress response of the organism. Recently, we proposed that one of the physiological functions of the SGP is the modulation of the GTP/GDP ratio under different growth conditions. In order to further determine the functions of SGP and its possible interactions with other molecules, we carried out immunoprecipitation, SGP binding, and the yeast two-hybrid system analyses. These approaches suggest that SGP may oligomerize and such interactions could be important for the function of this regulatory protein.

Bacterial Proteins↗

PubMed1989

Interactions of zinc with fluoride on growth, glycolysis and survival of Streptococcus mutans GS-5.

Effects of zinc and/or fluoride on growth, glycolysis and survival of Streptococcus mutans GS-5 were examined in vitro. Zinc inhibited growth and glycolysis, and enhanced the antimetabolic activity of fluoride. Zinc alone had little effect on cell survival. During cell growth without pH control a protection from cell death was mediated by fluoride, which appeared to be caused by a higher final pH in the culture medium. When cell death was observed under controlled pH conditions in a lactate-acetate buffer at pH 6.5, 5.0 or 4.0, fluoride was bactericidal only at pH 4.0. However, the combination of zinc plus fluoride was strongly bactericidal at all pH values that were tested.

Acids↗

PubMed1984

Effect of orthodontic treatment on prevalence of Streptococcus mutans in plaque and saliva.

The effect of orthodontic treatment on the prevalence of Streptococcus mutans was investigated in 14 subjects. Insertion of appliances tended to give a transient decrease in S.mutans levels, in both plaque and saliva, possibly due to elimination of S.mutans reservoirs by the banding procedure. After 3 months of extensive banding, the S.mutans proportions surpassed pretreatment levels in saliva and on banded teeth, whereas unbanded surfaces only showed a slight increase. It was thus concluded that creation of new retentive areas favors the local growth of S.mutans, which in turn increases the general infection level of this organism. Time was, however, needed before elevated levels were reached. Insertion of appliances tended to eliminate the characteristic gradient of S.mutans levels within the dental arches.

Adolescent↗

PubMed1988

The in vitro effect of lithium on growth and adherence of Streptococcus mutans 6715.

The in vitro effect of lithium (Li) on growth and adherence of Streptococcus mutans 6715 in the presence and absence of sucrose was examined by means of optical density and transmission electron microscopy. In the non-sucrose assay, bacterial growth was depressed and adherence was elevated between concentrations of 1.44-11.52 mmol/L Li. At 7.20 mmol/L Li extracellular material was present on the bacterial wall. Using 11.52-28.08 mmol/L Li resulted in a perfect negative correlation between the increasing concentrations of Li and bacterial growth and adherence (rs = -0.9 and rs = -1, respectively) in both assays. This paper addresses the dichotomy between the low and high Li concentrations regarding the two bacterial parameters studied, as well as their possibly related cariogenic and cariostatic clinical relevance.

Bacterial Adhesion↗

PubMed1989

Effects of Tween 80 and sodium fluoride on extracellular glucosyltransferase production and membrane lipids of Streptococcus mutans.

1. Both Tween 80 and sodium fluoride significantly enhanced total extracellular glucosyltransferase activities of Streptococcus mutans. 2. Water-insoluble and water-soluble glucan formation were uniformly increased by Tween 80, whereas fluoride stimulated only water-soluble glucan formation. 3. Elevated glucan formation was due to an increase in enzymes secreted from bacterial cells. 4. Fatty acid composition and phospholipid content in bacterial membrane were changed by Tween 80, although sodium fluoride scarcely showed these changes. 5. Comparative results suggest that modulation of membrane lipids participates in mutansucrase production but not in dextransucrase production of S. mutans.

Glucosyltransferases↗

PubMed1980

Virulence of Streptococcus mutans: revertants of mutant C4.

Mutant C4, a poor plaque-forming mutant of Streptococcus mutans 6715-HSR, was employed to obtain isolates resembling the parent strain (a plaque former). Seventeen presumptive revertants, as identified by colonial morphology, were isolated from mutant C4 after enrichment cycles in a sucrose-glass beads medium. These isolates displayed properties which resembled the parent in ability to produce plaque, patterns of fermentation, and resistance to streptomycin. In a detailed study, five selected isolates were found to be similar to the parent type 6715-HSR with respect to content of the serotype antigen, sucrose- or dextran-induced cell aggregation, glucosyltransferase and adherence activities, and cariogenicity. Thus, in selection for revertants to parental colonial morphology, the pleiotropic changes in plaque formation, adherence, glycosyltransferase activity, and virulence demonstrated by C4 all concomitantly reverted to their parental phenotypes.

Animals↗

PubMed1992

Molecular characterization and expression of the cell-associated glucosyltransferase gene from Streptococcus mutans.

A gene encoding cell-associated glucosyltransferase (CA-GTase) was cloned from Streptococcus mutans MT8148 into Escherichia coli DH5 alpha by using a low-copy-number plasmid, pMW119. After screening of a gene library with the oligonucleotide probe designed on the basis of a partial amino acid sequence of CA-GTase, a recombinant plasmid, pSK6, that had a 5.6 kb insert carrying the CA-GTase gene was selected. The gene product (recombinant CA-GTase) of pSK6 was expressed by using a lac promoter in pMW119. Western blotting revealed that rCA-GTase reacted with antibody to CA-GTase. rCA-GTase was found to synthesize water-insoluble glucans. Southern blotting indicated that the MT8148 chromosome contained another gene which was homologous to pSK6. A plasmid harboring this gene (pSK16) was also isolated from the gene library, the gene product of pSK16 exhibited GTase activity but ten times lower than that of pSK6.

Base Sequence↗

PubMed1977

Decreased oral colonization of Streptococcus mutans during aging of Sprague-Dawley rats.

The colonization by streptomycin-resistant Streptococcus mutans strains of the teeth of conventional and ex-germfree Sprague-Dawley rats of various ages fed either a high-sucrose or a high-glucose diet was studied. Bacterial colonization occurred with increasingly greater difficulty as the rats became older. This was observed in studies of the implantation of the test organism after oral inoculation with different cell numbers as well as its transmission between infected and uninfected rats. With rat fed sucrose diet, the effect of age could not be demonstrated until they were age 3 months or older; the results from rats fed a glucose diet suggest that changes may already have occurred early after weaning. Changes in susceptibility to colonization during aging manifested themselves as a decrease in the proportions of rats which became infected as well as lower population levels in infected rats. The possible mechanism(s) involved as well as the possible significance of the findings was discussed.

Aging↗