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PubMed1982

Purification and properties of pyruvate kinase from Streptococcus mutans.

Pyruvate kinase (EC 2.7.1.40) from Streptococcus mutans strain JC2 was purified, giving a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight of the native enzyme was 180,000 to 190,000, and the enzyme was considered to consist of four identical subunits. This enzyme was completely dependent on glucose 6-phosphate for activity, and the saturation curve for activation by glucose 6-phosphate was sigmoidal. In the presence of 0.5 mM glucose 6-phosphate, the saturation curves for the substrates phosphoenolpyruvate and ADP were hyperbolic, and the Km values were 0.22 and 0.39 mM, respectively. GDP, IDP, and UDP could replace ADP, and the Km for GDP (0.026 mM) was 0.067 of that for ADP. The enzyme required not only divalent cations, Mg2+ or Mn2+, but also monovalent cations, K+ or NH4+, for activity, and it was strongly inhibited by Pi. When the concentration of Pi was increased, the half-saturating concentration and Hill coefficient for glucose 6-phosphate increased. However, the enzyme was immediately inactivated in a solution without Pi. The intracellular concentration of glucose 6-phosphate, in cooperation with that of Pi, may regulate pyruvate kinase activity in S. mutans.

Adenosine Diphosphate↗

PubMed1986

Sucrose-dependent cell adherence and cariogenicity of serotype c Streptococcus mutans.

Four strains of serotype c Streptococcus mutans differing in glucosyltransferase (GTase) and fructosyltransferase (FTase) activities were examined. These strains had been made resistant to streptomycin. FTase activity of an S. mutans clinical variant, MT6801R, which forms large mucoid colonies on sucrose-containing agar, was considerably higher than that of a typical serotype c strain, MT8148R, which forms small, rough colonies on the same agar. Two mutants, NG14 and NG7183, were induced from strain MT6801R by N-methyl-N'-nitro-N-nitrosoguanidine, and were found to be streptomycin-resistant. GTase and FTase activities of mutant NG14 were similar to those of the typical serotype c strain, while in mutant NG7183 the two enzyme activities were very low. Growing cells of these strains (except NG7183) adhered firmly to a glass surface in sucrose broth. Resting cells of all strains attached in small numbers to saliva-coated hydroxyapatite in the absence of sucrose. On the other hand, the presence of sucrose markedly enhanced the attachment of cells of strains MT8148R, MT6801R and NG14, but not NG7183. Cell-surface hydrophobicity and acid production of all strains were similar. Both strain MT8148R and NG14 colonized tooth surfaces and produced significant dental caries in specific-pathogen-free rats. Strain MT6801R had lower colonization ability and cariogenicity when compared with strains MT8148R and NG14. Furthermore, mutant NG7183 was able to colonize the tooth surfaces in small numbers, but failed to cause dental caries. These results indicate that sucrose-dependent cell adherence mediated by de novo glucan synthesis is necessary for the accumulation of serotype c S. mutans cells on the tooth surface and the induction of dental caries.

Adsorption↗

PubMed1982

Fundus lesions after carotid injection of Streptococcus mutans in monkeys.

Carotid injection of Streptococcus mutans in pigtail monkeys caused fundus lesions clinically resembling those seen in humans with bacteremia. On histopathological examination microabscesses occurred in the retina, choroid, and optic nerve. Bacteria were observed in the histopathological sections of the microabscesses, and S. mutans was cultured from the retina and choroid.

Animals↗

PubMed1987

Acetoin production by wild-type strains and a lactate dehydrogenase-deficient mutant of Streptococcus mutans.

Eleven different laboratory strains of Streptococcus mutans representing the various serogroups were found to produce an average of 6.0 +/- 4.8 mM acetoin when grown in glucose-containing medium under aerobic conditions. None of the strains produced detectable acetoin when grown anaerobically. A lactate dehydrogenase-deficient mutant produced acetoin both aerobically and anaerobically and in substantially greater amounts than the wild-type strains did. Substitution of mannitol for glucose resulted in decreased acetoin production by wild-type strains and the lactate dehydrogenase-deficient mutant, indicating a role for NADH2 in the regulation of the acetoin pathway. Pyruvate incorporated into the growth medium of a wild-type strain caused acetoin to be produced anaerobically and stimulated acetoin production aerobically. Cell extracts of a wild-type S. mutans strain were capable of producing acetoin from pyruvate and were (partly) dependent on thiamine PPi. Extracts prepared from aerobically grown cells had approximately twice the acetoin-producing activity as did extracts prepared from anaerobically grown cells. The results indicate that acetoin production by S. mutans may represent an auxiliary reaction of pyruvate dehydrogenase in this organism.

Acetoin↗

PubMed1981

Effect of fructose and other carbohydrates on the surface properties, lipoteichoic acid production, and extracellular proteins of Streptococcus mutans Ingbritt grown in continuous culture.

Streptococcus mutans Ingbritt was grown in a chemostat at destined dilution rates in either 0.5% fructose or 0.5% sorbitol and at destined pH values in 0.5% fructose. The yield of cells was affected by the carbohydrate source, as well as by the pH, with the lowest yield being at pH 5.5 in 0.5% fructose. Fructose-grown cells showed greater susceptibility to lysis by a muramidase than the corresponding glucose-grown cells, but there were no marked differences in the lytic susceptibilities of the corresponding cell wall preparations or in the serological reactivities of wall lysates with antiserum to S. mutans Ingbritt. The greatest amounts of cellular lipoteichoic acid were obtained at high dilution rates in both fructose and sorbitol, as well as at high pH values in fructose. The greatest amounts of extracellular lipoteichoic acid were found at low dilution rates, as estimated by rocket immunoelectrophoresis and also by hemagglutination. Three major extracellular protein components were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the effects of growth conditions on these components were determined. Results for batch-grown cultures showed that there was genotypic variation in the susceptibility of cells to lysis by a muramidase. The enhancement of lipoteichoic acid production by fructose and sorbitol in batch cultures was not identical in representative strains of S. mutans serotype c, nor was the effect of fructose found uniformly in representative strains of the different S. mutans serotypes.

Bacterial Proteins↗

PubMed2004

Deletion in sortase gene of Streptococcus mutans Ingbritt.

Our previous studies on Streptococcus mutans have demonstrated that surface proteins containing a C-terminal sorting signal, such as surface protein antigen (PAc), glucan-binding protein C (GbpC) and dextranase (Dex), are anchored to the cell wall by a sortase (SrtA). In this study we found that, unlike other strains of S. mutans, strain Ingbritt did not exhibit cell wall-anchoring of PAc, GbpC and Dex. It is speculated that the SrtA of strain Ingbritt did not function in the cell wall-anchoring process of these surface proteins. Sequence analysis revealed a deletion of an 11-bp nucleotide sequence in the srtA gene of strain Ingbritt, resulting in the generation of a new termination codon, resulting in production of an incomplete SrtA enzyme protein. As a result, strain Ingbritt showed a localization change of PAc, GbpC and Dex in the cell, implying that strain Ingbritt loses the biological functions mediated by the cell surface-associated proteins of S. mutans. These results suggest that strain Ingbritt could be less cariogenic than other strains of S. mutans.

Aminoacyltransferases↗

PubMed1980

Interaction of Streptococcus mutans glucosyltransferases with teichoic acids.

The Streptococcus mutans GS5 glucosyltransferase activities (both water-soluble and -insoluble glucan-synthesizing fractions) were inhibited by purified lipoteichoic acid. In vitro sucrose-dependent colonization of smooth surfaces by strain GS5 was also markedly reduced in the presence of the amphipathic molecules. The inhibition of soluble glucan synthesis by lipoteichoic acid appeared to be competitive with respect to both sucrose and primer dextran T10. These inhibitory effects were dependent on the presence of the fatty acid components of lipoteichoic acid since deacylated lipoteichoic acids did not inhibit glucosyltransferase activity. However, the deacylated molecules did interact with the enzymes since deacylated lipoteichoic acid partially protected the enzyme activity against heat inactivation and also induced the formation of high-molecular-weight enzyme complexes from the soluble glucan-synthesizing fraction. The presence of teichoic acid in high-molecular-weight aggregates of glucosyltransferase isolated from the culture fluids of strain GS5 was suggested by the detection of polyglycerophosphate in these fractions. In addition to strain GS5, two other organisms containing polyglycerophosphate teichoic acids, Lactobacillus casei and Lactobacillus fermentum, were demonstrated to bind glucosyltransferase activity. These results are discussed relative to the potential role of teichoic acid-glucosyltransferase interactions in enzyme binding to the cell surface of S. mutans and the formation of high-molecular-weight enzyme aggregates in the culture fluids of the organism.

Acylation↗

PubMed2006

Serotype-specific polysaccharide of Streptococcus mutans contributes to infectivity in endocarditis.

Streptococcus mutans and other viridans streptococci have been implicated as major etiological agents of infective endocarditis. The serotype-specific rhamnose-glucose polysaccharide (RGP) of S. mutans has several biological functions that appear to be essential for the induction of infective endocarditis. The aim of this study was to examine the contribution of RGP to the infectivity of S. mutans in infective endocarditis using a rat model. The RGP-defective mutant of S. mutans showed reduced ability to induce infective endocarditis compared to the parental strain. The ability of S. mutans to induce infective endocarditis was not consistent with the binding capacity of the organism to extracellular matrix proteins. The results suggest that S. mutans containing whole RGP is more virulent than the RGP-defective mutant, and the RGP has an important role for the induction of infective endocarditis by S. mutans.

Animals↗

PubMed2003

A 100 kDa vanadate and lanzoprazole-sensitive ATPase from Streptococcus mutans membrane.

The cariogenic potential of Streptococcus mutans is due to the production of organic acids derived from energy metabolism, which implies the need of mechanisms for the organism to tolerate this acidic environment. The F(1)F(o)-ATPase is generally considered as the main enzyme responsible for cytoplasmic proton extrusion, but mutations that resulted in a 50% reduction in F(1)F(o)-ATPase activity in S. mutans still allowed the micro-organism to grow and extrude acid, keeping the intracellular pH one pH unit above the extracellular ambient. This finding suggests the existence of other enzymatic (or cellular) mechanisms that keep the cytosolic pH neutral during micro-organism growth. This paper describes a membrane protein in S. mutans, with a molecular weight of 100 kDa, which exhibits ATPase activity inhibited by classic inhibitors of P-type ATPases (orthovanadate) and H(+),K(+)-ATPase (lanzoprazole), has an optimum pH comparable to other H(+)-ATPases and undergoes phosphorylation during the catalytic reaction, like that of H(+)-ATPases described in yeast and plant plasma membrane. Together, these results strongly suggest that the enzyme we describe here is a P-type H(+)-ATPase or H(+),ion-ATPase that can act in association with F(1)F(o)-ATPase during the growth of the S. mutans.

2-Pyridinylmethylsulfinylbenzimidazoles↗

PubMed2006

Identification and molecular characterization of an N-Acetylmuraminidase, Aml, involved in Streptococcus mutans cell separation.

We previously demonstrated Streptococcus mutans produces two bacteriolytic enzymes of 100 kDa and 80 kDa (G. Yoshimura et al. Microbiol. Immunol. 48, 465-469, 2004). Here, we identified the protein sequence of these enzymes and found they come from a single gene product designated as automutanolysin (Aml). Aml has a modular design where the N-terminus contains five 13-amino-acid repeats and a C-terminal enzyme active domain. Aml selectively lyses S. mutans and S. sobrinus but no other oral streptococci. This suggests Aml possesses strong substrate specificity towards cariogenic bacteria present in the human oral cavity. Analysis of S. mutans peptidoglycan fragments released by Aml shows the enzyme is an N-acetylmuraminidase. We found Ca(2+) enhances the activity; and EGTA, EDTA and iodoacetic acid inhibit the activity. The optimum pH range for lytic activity was 6 to 7. Disruption of the aml gene in S. mutans results in the formation of a longer bacterial cell chain length that was dispersed by the addition of a low concentration of Aml. This suggests Aml is involved in S. mutans cell separation.

Amino Acid Sequence↗

PubMed1987

Effects of oxygen on glucose-limited growth of Streptococcus mutans.

Aerotolerance in the growth of Streptococcus mutans and related streptococci was examined under glucose-limited conditions. The growth rate of all strains tested was more or less retarded when they were transferred from anaerobic to aerobic conditions. As for growth yield, however, some strains (group 1) showed reduced values for the increment of cellular dry weight change (in grams per mole of glucose), whereas others showed either unaltered (group 2) or increased (group 3) yields. The characteristic feature of strains in groups 2 and 3 was their high activity of both glucose- and pyruvate-dependent oxygen uptake when strains were grown under aerobic conditions. By contrast, the activity of pyruvate-dependent oxygen uptake by group 1 strains was negligibly low, whether grown under aerobic or anaerobic conditions. Some strains (group 1a) consumed oxygen in the presence of glucose at a much faster rate than others did (group 1b). There seems to be a good correspondence of these aerotolerance groupings to those based on serotypes of S. mutans. Thus, the groups 1a, 1b, 2, and 3 correspond to serotypes g, a+d, c+f, and b, respectively.

Aerobiosis↗

PubMed1989

Impairment of melibiose utilization in Streptococcus mutans serotype c gtfA mutants.

The Streptococcus mutans serotype c gtfA gene encodes a 55-kilodalton sucrose-hydrolyzing enzyme. Analysis of S. mutans gtfA mutants revealed that the mutant strains were specifically impaired in the ability to use melibiose as a sole carbon source. S. mutans gtfA mutant strains synthesized less alpha-galactosidase activity inducible by raffinose than wild-type strains. Melibiose (an inducer in wild-type strains) failed to induce significant levels of alpha-galactosidase in the mutant strains. We hypothesize that melibiose use by S. mutans requires the interaction of the GtfA enzyme, or another gene product under the control of the gtfA promoter, with other gene product(s) involved in melibiose transport or hydrolysis.

Disaccharides↗

PubMed1999

Virulence of a spaP mutant of Streptococcus mutans in a gnotobiotic rat model.

Streptococcus mutans, the principal etiologic agent of dental caries in humans, possesses a variety of virulence traits that enable it to establish itself in the oral cavity and initiate disease. A 185-kDa cell surface-localized protein known variously as antigen I/II, antigen B, PAc, and P1 has been postulated to be a virulence factor in S. mutans. We showed previously that P1 expression is necessary for in vitro adherence of S. mutans to salivary agglutinin-coated hydroxyapatite as well as for fluid-phase aggregation. Since adherence of the organism is a necessary first step toward colonization of the tooth surface, we sought to determine what effect deletion of the gene for P1, spaP, has on the colonization and subsequent cariogenicity of this organism in vivo. Germ-free Fischer rats fed a diet containing 5% sucrose were infected with either S. mutans NG8 or an NG8-derived spaP mutant strain, PC3370, which had been constructed by allelic exchange mutagenesis. At 1-week intervals for 6 weeks after infection, total organisms recovered from mandibles were enumerated. At week 6, caries lesions also were scored. A significantly lower number of enamel and dentinal carious lesions was observed for the mutant-infected rats, although there was no difference between parent and mutant in the number of organisms recovered from teeth through 6 weeks postinfection. Coinfection of animals with both parent and mutant strains resulted in an increasing predominance of the mutant strain being recovered over time, suggesting that P1 is not a necessary prerequisite for colonization. These data do, however, suggest a role for P1 in the virulence of S. mutans, as reflected by a decrease in the cariogenicity of bacteria lacking this surface protein.

Animals↗

PubMed1995

Effect of dentine and collagen on the lethal photosensitization of Streptococcus mutans.

Suspensions of the cariogenic bacterium, Streptococcus mutans were treated with either toluidine blue O or aluminium disulphonated phthalocyanine and then exposed to light from a helium-neon or gallium-aluminium-arsenide laser, respectively, after passing through demineralized dentine slices. Bacteria were also embedded in a collagen matrix prior to sensitization and exposure to the laser light. When dentine slices were interposed between the laser light and the bacterial suspension, substantial kills (10(7) CFU) were achieved at energy doses of 876, 1,752, and 3,504 mJ with the helium-neon laser and of 1,188, 2,376, and 4,752 mJ with the gallium-aluminium-arsenide laser. There was no apparent relationship between the extent of killing and the degree of demineralization of the dentine. Prolonging the exposure of the sensitized bacteria to the laser light increased the kill achieved. Substantial numbers (10(8) to 10(10) CFU) of S. mutans were also killed when embedded in a collagen matrix and exposed to 438 and 1,314 mJ of helium-neon laser light and 594 and 1,782 mJ of light from the gallium-aluminium-arsenide laser. These results imply that lethal photosensitization may be effective at killing S. mutans in a carious lesion, even when the organism is embedded in demineralized dentine.

Animals↗

PubMed1986

Ferrous iron transport in Streptococcus mutans.

Radioiron uptake from 59FeCl3 by Streptococcus mutans OMZ176 was increased by anaerobiosis, sodium ascorbate, and phenazine methosulfate (PMS), although there was a 10-min lag before PMS stimulation was evident. The reductant ascorbate may have provided ferrous iron. The PMS was reduced by the cells, and the reduced PMS then may have generated ferrous iron for transport; reduced PMS also may have depleted dissolved oxygen. We conclude that S. mutans transports only ferrous iron, utilizing reductants furnished by glucose metabolism to reduce iron prior to its uptake.

Anaerobiosis↗

PubMed2001

Cell density modulates acid adaptation in Streptococcus mutans: implications for survival in biofilms.

Streptococcus mutans normally colonizes dental biofilms and is regularly exposed to continual cycles of acidic pH during ingestion of fermentable dietary carbohydrates. The ability of S. mutans to survive at low pH is an important virulence factor in the pathogenesis of dental caries. Despite a few studies of the acid adaptation mechanism of this organism, little work has focused on the acid tolerance of S. mutans growing in high-cell-density biofilms. It is unknown whether biofilm growth mode or high cell density affects acid adaptation by S. mutans. This study was initiated to examine the acid tolerance response (ATR) of S. mutans biofilm cells and to determine the effect of cell density on the induction of acid adaptation. S. mutans BM71 cells were first grown in broth cultures to examine acid adaptation associated with growth phase, cell density, carbon starvation, and induction by culture filtrates. The cells were also grown in a chemostat-based biofilm fermentor for biofilm formation. Adaptation of biofilm cells to low pH was established in the chemostat by the acid generated from excess glucose metabolism, followed by a pH 3.5 acid shock for 3 h. Both biofilm and planktonic cells were removed to assay percentages of survival. The results showed that S. mutans BM71 exhibited a log-phase ATR induced by low pH and a stationary-phase acid resistance induced by carbon starvation. Cell density was found to modulate acid adaptation in S. mutans log-phase cells, since pre-adapted cells at a higher cell density or from a dense biofilm displayed significantly higher resistance to the killing pH than the cells at a lower cell density. The log-phase ATR could also be induced by a neutralized culture filtrate collected from a low-pH culture, suggesting that the culture filtrate contained an extracellular induction component(s) involved in acid adaptation in S. mutans. Heat or proteinase treatment abolished the induction by the culture filtrate. The results also showed that mutants defective in the comC, -D, or -E genes, which encode a quorum sensing system essential for cell density-dependent induction of genetic competence, had a diminished log-phase ATR. Addition of synthetic competence stimulating peptide (CSP) to the comC mutant restored the ATR. This study demonstrated that cell density and biofilm growth mode modulated acid adaptation in S. mutans, suggesting that optimal development of acid adaptation in this organism involves both low pH induction and cell-cell communication.

Amino Acid Sequence↗

PubMed1986

Detection and specificity of antibodies secreted by spleen cells in mice immunized with Streptococcus mutans.

Immune responses of mice to Streptococcus mutans serotype c were analyzed by means of the enzyme-linked immunospot assay to determine the predominant specificities of the antibodies developed. In general, the numbers of splenic antibody-secreting cells correlated with serum antibody levels. A low dose (10(8) CFU) of killed whole cells injected twice intraperitoneally induced antibodies mainly against surface protein antigen I/II. A higher dose (10(9) CFU) given two to six times also resulted in a predominance of antigen I/II antibody-secreting cells and, in addition, antibody responses to surface protein antigen III and lipoteichoic acid occurred. Cells producing antibodies to serotype c polysaccharide were elicited only on repeated immunization. These results agreed with the development of antibodies in rabbits repeatedly immunized intravenously with killed whole cells of S. mutans, S. rattus, and S. sobrinus, which induced specific antibodies in accordance with the surface antigens that they express. Mice immunized twice with the same dose of purified antigens I/II and III developed greater numbers of antigen I/II splenic antibody-forming cells than antigen III splenic antibody-forming cells and higher serum antibody levels to antigen I/II than to antigen III. Furthermore, a single injection of antigen I/II but not of antigen III was sufficient to induce a strong specific-antibody response. Some evidence was also obtained for weak polyclonal stimulation of spleen cells by S. mutans cells and by antigen I/II, a result which could be relevant to the induction by S. mutans of antibodies reactive with mammalian tissues. It was concluded that for the antigens examined, S. mutans elicited the strongest antibody response against antigen I/II, which was also highly immunogenic in purified form.

Animals↗

PubMed1979

Effect of growth rate and glucose concentration on the activity of the phosphoenolpyruvate phosphotransferase system in Streptococcus mutans Ingbritt grown in continuous culture.

Streptococcus mutans Ingbritt was grown anaerobically in a chemostat with a glucose limitation, as well as with an excess of glucose (amino acid limitation) at dilution rates (D) between 0.05 and 0.4 h(-1) (mean generation time = 12 to 1.5 h). The glucose-limited culture produced cells having 1.5- to 6.0-fold greater glycolytic activity than the cells from the glucose-excess culture. The preferred substrate for these cells was glucose, with the glycolytic rate for sucrose being only slightly lower; the rate for fructose was half that of glucose. The glycolytic rate of the glucose-limited cells was maximum at D = 0.1 h(-1), with a decline in rate as the growth rate approached D = 0.4 h(-1). A comparison of the activity of phosphoenolpyruvate phosphotransferase system (PTS) in the two types of cells showed that the glucose-limited cells had 1.7- to 5.6-fold greater PTS activity for the three sugars than the glucose-excess-grown cells. Whereas little difference was seen between the three sugars with the latter cells, the glucose-PTS had the greatest activity with glucose-limited cells, with the maximum in cells grown at D = 0.1 h(-1). Comparison of the rate of sugar uptake in the chemostat with the rate of PTS transport activity in the cells at each growth rate demonstrated that only under conditions of slow growth with a glucose limitation was the PTS system capable of supporting growth on glucose. Furthermore, PTS activity in cells grown with an excess of glucose was insignificant when compared with glucose uptake during growth in the chemostat. This evidence supports the observation that S. mutans possesses at least one other system, in addition to the PTS, for the transport of glucose into the cell. The organism was, however, devoid of glucose-proton symport transport activity.

Biological Transport, Active↗