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PubMed1984

Function of anti-Streptococcus mutans antibodies: anti-ribosomal antibodies inhibit acid production, growth, and glucose phosphotransferase activity.

Antibodies induced in sera and saliva of rats and rabbits immunized with ribosomal preparations from Streptococcus mutans 6715 inhibited transport of glucose by the phosphotransferase system by greater than 60%, acid production from sucrose by greater than 95%, and growth of the homologous S. mutans by greater than 59%. Inhibition of growth and acid production by immune sera and saliva were abrogated by prior adsorption with S. mutans 6715 whole cells, glucosyltransferase, lipoteichoic acid, or alpha 1-6 or alpha 1-3 dextran. These results indicate that antibodies induced to an S. mutans ribosomal preparation react with cell surface determinants and suggest that the antibodies inhibit sucrose-induced acid formation and growth of virulent S. mutans by neutralizing the glucose-phosphotransferase system.

Animals↗

PubMed2006

Dispensable genes and foreign DNA in Streptococcus mutans.

A range of properties, including the ability to utilize various sugars, bind macromolecules and produce mutacins, are known to vary in their occurrence in different strains of Streptococcus mutans. In addition, insertion-sequence elements show a limited distribution and sequencing of the genome of S. mutans UA159 has revealed the presence of putative genomic islands of atypical base composition indicative of foreign DNA. PCR primers flanking regions suspected of having inserted DNA were designed on the basis of the genome sequence of S. mutans UA159 and used to explore variation in a collection of 39 strains isolated in various parts of the world over the last 40 years. Extensive differences between strains were detected, and similar insertion/deletion events appear to be present in the genomes of strains with very different origins. In two instances, insertion of foreign DNA appears to have displaced original S. mutans genes. Together with previous results on the occurrence of deletions in genes associated with sugar metabolism, the results indicate that S. mutans has a core genome and a dispensable genome, and that dispensable genes have become widely distributed through horizontal transfer.

Bacterial Proteins↗

PubMed1981

Role of interbacterial adherence in colonization of the oral cavities of gnotobiotic rats infected with Streptococcus mutans and Veillonella alcalescens.

The role of interbacterial adherence in the colonization of the rate oral cavity was investigated with aggregating and nonaggregating strains of Veillonella alcalescens and Streptococcus mutans. V. alcalescens V-1 and S. mutans M-7 rapidly formed large stable aggregates when mixed in vitro. Aggregates could be reduced in size by sonication, but they could not be completely dispersed, indicating that bonding between the organisms was strong. V. alcalescens V-1 did not coaggregate with S. mutans C67-1, and V. alcalescens OMZ193 did not coaggregate with either S. mutans strain C67-1 or M-7. Osborne-Mendel rats monoassociated with either S. mutans C67-1 or M-7 were inoculated with veillonellae, molar teeth were removed at 2 h and at 14 days, and the number of veillonellae was determined. At 2 h post-inoculation there were 600 times as many colony-forming units of V. alcalescens V-1 adherent to the teeth of animals monoassociated with S. mutans M-7 when compared with animals monoassociated with the nonaggregating S. mutans C67-1. The number of colony-forming units of V. alcalescens V-1 was 1,000 times greater than the number of nonaggregating V. alcalescens OMZ193 in S. mutans M-7-infected animals. Similar results were obtained when teeth were samples 14 days after inoculation. Veillonellae inoculated into the mouths of germfree animals rapidly disappeared from tooth surfaces.

Animals↗

PubMed1980

Immunochemical properties of antigen-specific monkey T-cell suppressor factor induced with a Streptococcus mutans antigen.

Antigen-specific suppressor factor could be released from monkey suppressor T cells induced in vitro with a protein antigen isolated from the carcinogenic bacterium Streptococcus mutans. The suppressor activity was due to the factor itself and not to carryover of free antigen. Characterization of the monkey factor revealed it to have a molecular weight of ca. 70,000, and to contain a constant region and determinants encoded by the major histocompatibility complex. The presence of immunoglobulin determinants could not be demonstrated. However, by virtue of its adsorption to specific antigen, an antigen-combining site was shown to be present. The possible regulatory role of streptococcal antigen-specific suppressor factor in protection against dental caries is discussed.

Animals↗

PubMed1988

Sequence analysis of the gtfC gene from Streptococcus mutans GS-5.

The nucleotide sequence of the gtfC gene, which codes for glucosyltransferase synthesizing both water-soluble and water-insoluble glucans, and its flanking regions from Streptococcus mutans GS-5, was determined. Although the gtfC gene (4218 bp) is preceded by a Shine-Dalgarno (SD) sequence, a promoter-like sequence for this gene could not be identified. The gtfC gene product composed of 1375 amino acid residues (approx. 153 kDa) is generally hydrophilic with three small hydrophobic domains. Two direct repeating units were found near the C terminus of the peptide. The gtfC gene has extensive homology with the previously sequenced gtfB gene. The homologous regions correspond to the signal sequence, an internal region, and the direct repeating units of the peptide. An open reading frame preceded by an SD sequence and followed by an inverted repeat sequence was found immediately downstream from the gtfC gene. The combined sequences of the gtfB and gtfC genes as well as flanking regions suggest that the two gtf genes and the small downstream coding region could be coordinately expressed within an operon. The possible evolution of the gtfC gene in S. mutans GS-5 is also discussed.

Amino Acid Sequence↗

PubMed1988

Electron-microscopic observation of adherence of serotype c Streptococcus mutans to the enamel surface due to glucan synthesis.

Cellular adherence of three strains with water-insoluble glucan (IG)-synthesizing ability and a strain lacking the ability of serotype c Streptococcus mutans to the saliva-coated human enamel surface was examined by scanning (SEM) and transmission (TEM) electron-microscopy. SEM revealed that organisms of all strains used adhered directly to the enamel surface in the absence of sucrose. Cell-to-cell attachment was scarcely observed in the absence of sucrose. Cell-to-cell attachment via amorphous substance on the cell surface was observed by SEM when the strains with IG-synthesizing ability were incubated with the saliva-coated enamel in the presence of sucrose. TEM revealed that cell-associated enzymes of these strains synthesized filamentous and double-stranded fibrillar structures from sucrose. The strain lacking IG-synthesizing ability was unable to induce cell-to-cell attachment in the presence of sucrose, nor was it able to synthesize the amorphous substance. These results indicate that production of IG by cell-associated glucosyltransferase participates in cellular accumulation of serotype c S. mutans.

Bacterial Adhesion↗

PubMed1996

Molecular cloning and sequence analysis of the gene encoding the H2O-forming NADH oxidase from Streptococcus mutans.

To discover the molecular properties of two distinct NADH oxidases, corresponding to H2O2-forming oxidase (NOX-1) and H2O-forming oxidase (NOX-2) induced in Streptococcus mutans, for the first step we had cloned and sequenced the nox-1 gene encoding NOX-1. In this paper, a nox-2 gene encoding NOX-2 from S. mutans was cloned, and the nucleotides sequenced. The nox-2 gene comprises 1371 base-pairs, encoding a polypeptide of 457 amino acid residues. The deduced relative molecular mass (M(r) = 49919) agreed with the previous value obtained from the purified NOX-2 protein. The nox-2 gene was expressed in Escherichia coli using its own promoter. Alignment of the NOX-2 protein sequence with that of the NOX-1 showed that the proteins do not significantly resemble each other. Comparisons with the NADH oxidase from Streptococcus faecalis 10C1 yield identities of 41%. The redox-active cysteine in the enzyme from S. faecalis was found to correspond to Cys 44 in the NOX-2.

Amino Acid Sequence↗

PubMed1983

Prevalence of Streptococcus mutans with different colonial morphologies in human plaque and saliva.

Plaque and saliva samples were obtained twice from 58 children at an interval of 1 year and examined for the prevalence of Streptococcus mutans on Mitis salivarius (MS) and Mitis salivarius bacitracin (MSB) agar. Two types of S. mutans colonies with different colonial morphologies were seen on both media. They were serologically identified as serotypes c/e/f and d/g respectively. The first type, morphogroup c/e/f, had the typical "frosted-glass" appearance. It was the most prevalent and was found in 97% of the children. The second type, morphogroup d/g, had a creamy marzipan consistency with a dull, granular surface, gray to brown in color and often with some liquid around or on top of the colony. Group d/g was detected in 21 children (36%) and then together with colonies of group c/e/f. Children infected with single or multiple morphogroups of S. mutans generally harbored the same groups 1 year later. There was a significant positive correlation between the proportion of S. mutans in plaque and their numbers in saliva.

Adolescent↗

PubMed1981

Use of combined immunization routes in induction of a salivary immunoglobulin A response to Streptococcus mutans in Macaca fascicularis monkeys.

Various combinations of immunization routes were examined for ability to elicit or prolong (or both) a salivary secretory immunoglobulin A response to Streptococcus mutans strain Ingbritt (serotype c) in Macaca fascicularis monkeys. Intraductal (i.d.), per os (p.o.), and subcutaneous (s.c.) routes were utilized. Four groups of three to five monkeys each were immunized by the following schedules: group I--p.o., s.c., i.d.; group II--i.d., p.o., i.d.; group III--s.c., p.o., i.d.; and group IV--control. Immune responses in the serum and parotid fluid were quantitated by using passive hemagglutination assays with purified serotype-specific polysaccharide and by indirect immunofluorescent staining assays. Both s.c. and i.d., but not p.o., routes resulted in detectable serum antibody responses. Only i.d. immunization resulted in a measurable salivary response. Indirect immunofluorescent staining revealed specific secretory immunoglobulin A antibodies in the parotid fluid which correlated with passive hemagglutination titers. The p.o. procedures used in this study did not result either in a prolonged immune response or in measurable tolerance related to the humoral or secretory immune system.

Administration, Oral↗

PubMed1977

Distribution of dextransucrase in Streptococcus mutans and observations on the effect of soluble dextran on dextransucrase activities.

Total and insoluble dextransucrase activities were measured in cell-associated and supernatant fractions of Streptococcus mutans GS-5 grown in several media. Although the amount of cell-associated and supernatant activity varied greatly as a function of medium, the total activity appeared constant. The distribution of dextransucrase could be altered without changing the total dextransucrase activity. This indicates that the distribution of the enzyme can be regulated independently of its synthesis. Strain GS-5 had significant cell-associated activity in media devoid of sucrose. In all cases, the ratio of insoluble to total dextransucrase activity was higher in the cell-associated fractions than in the cell-free supernatants. It is also demonstrated that exogenous soluble dextran caused a decrease in insoluble dextransucrase activity and an increase in soluble dextransucrase activity in both the cell-associated fraction and the culture supernatant. The stimulation of soluble dextran-synthesizing activity was not due to de novo synthesis. The inhibition of insoluble dextran-synthesizing activity is shown to be noncompetitive. These results support a physical rather than metabolic mechanism for the effect of soluble dextran on dextransucrase activities.

Chloramphenicol↗

PubMed1985

Serum antibodies against oral Streptococcus mutans in young children in relation to dental caries and maternal close-contacts.

Thirty-six children aged 2.6-4.9 years were studied with respect to dental caries, Streptococcus mutans counts in dental plaque, and the estimates of total amount and avidity of serum IgG, IgM and IgA antibodies against Strep. mutans 10449, serotype c. A significant positive correlation (r = 0.49, p less than 0.01) was found between the number of Strep. mutans and caries-index in children. Two children with dental caries had no oral Strep. mutans. In median tests, high antibody titre and avidity of serum IgG antibodies against Strep. mutans were associated (p less than 0.05) with low counts of Strep. mutans. No such relationship was found with IgM or IgA antibodies. Children who had had frequent maternal close-contacts in their first year had significantly more (p less than 0.05) IgG antibodies against Strep. mutans than children with rare close-contacts.

Antibodies, Bacterial↗

PubMed2006

[Buffering effects of plaque solid, Streptococcus mutans and glucans].

OBJECTIVE: To investigate the buffer capacity of insoluble plaque mass including bacteria and glucans matrix. METHODS: Plaque samples (starved or incubated 1 h with 10% sucrose), Streptococcus mutans (S. mutans) mass, and insoluble/soluble glucans were titrated with 1 mmol/L HCl. Meanwhile, the density of bacteria was counted and related to buffer capacity. RESULTS: The bacteria density had significant effects on acid buffer capacity in dental plaque, but the effect reduced with consuming sugar. S. mutans mass with no sucrose incubating contributed to the buffer capacity of (0.609 +/- 0.202) mmol/L, and S. mutans mass with 2% sucrose had only the buffer capacity of (0.099 +/- 0.047) mmol/L. In the mean time, glucans had no effect on acid buffering (0.028 - 0.032 mmol/L). CONCLUSIONS: The bacteria including S. mutans may be the main contributor to acid buffering in plaque solid.

Acids↗

PubMed2001

The time-course of acid excretion, levels of fluorescence dependent on cellular nicotinamide adenine nucleotide and glycolytic intermediates of Streptococcus mutans cells exposed and not exposed to air in the presence of glucose and sorbitol.

The aim of this study was to examine glucose and sorbitol metabolism in Streptococcus mutans cells exposed and not exposed to air at the coexistence of these compounds by measuring acid excretion, levels of fluorescence dependent on cellular NADH and glycolytic intermediates. An aliquot of bacterial cells grown under strictly anaerobic conditions (anaerobic cells) was exposed temporarily to air (aerobic cells). When glucose was added to the anaerobic cells metabolizing sorbitol, the acid excretion was increased. The level of NADH decreased initially and then increased to the higher plateau level than that during glucose metabolism. The aerobic cells neither metabolized sorbitol nor contained glycolytic intermediates. However, 2 min after glucose was added in the presence of sorbitol, the acid excretion was started slowly and the intermediates appeared. The level of NADH was decreased at first and then increased. These results suggested that the anaerobic S. mutans cells metabolized glucose and sorbitol simultaneously, and that in the presence of sorbitol the aerobic cells could start to metabolize glucose 2 min after glucose was added, as the intermediates (phosphoenopyruvate potential) for the glucose transport were accumulated.

Acids↗

PubMed1989

Free arachidonic acid source for PGE2 and TXB2 production in guinea pig peritoneal macrophages exposed to insoluble glucan from Streptococcus mutans.

1. Macrophages are an important source of the lipid mediators arachidonic acid (AA) and its metabolites that are produced during inflammation. 2. Previously, we reported that insoluble glucans from Streptococcus mutans in dental plaque could induce macrophages to secrete PGE2 and TXB2. 3. Studies were undertaken to identify the phospholipid substrates that can serve as a source of AA in macrophages exposed to the insoluble glucan. 4. When macrophage cell prelabelled with [3H]AA, stimulation with insoluble glucan resulted in a loss of label mainly from phosphatidylcholine (PC) and phosphatidylinositol (PI). 5. In addition, the PC-, and PI-specific phospholipase A2-mediated mechanisms for AA release may be activated in guinea peritoneal macrophages exposed to the insoluble glucan from S. mutans.

Animals↗

PubMedDate not supplied

Effect of povidone-iodine on Streptococcus mutans in children with extensive dental caries.

PURPOSE: The purpose of this pilot project was to determine the effect of a 10% povidone-iodine solution on plaque Streptococcus mutans and on incidence of new caries in young children following dental rehabilitation under general anesthesia. METHODS: Twenty-five children ages 2 to 7 years, scheduled for dental treatment under general anesthesia, were enrolled. Children in the experimental group (N = 13) had povidone-iodine applied 3 times at 2-month intervals. Control children (N = 12) had no treatment. Plaque samples were taken from all children at baseline, 6 months and cultured for total bacteria and S mutans. Dental examinations were conducted at baseline, 6 months, and 1 year. RESULTS: Experimental and control children had similar dietary habits, caries experience, and S mutans levels at baseline. All children's S mutans counts decreased significantly at 6 months (P = .003). The difference between the 2 groups was not significant (P = .58). At 1 year, 5 of 8 children in the control group had new caries compared to 2 of 11 children in the experimental group (P = .06). Povidone-iodine was well accepted by participating families. CONCLUSIONS: Extensive one-time restorative dental treatment resulted in a significant suppression S mutans levels at 6 months. Further exploration of the role of povidone-iodine in caries management is indicated.

Anti-Infective Agents, Local↗

PubMedDate not supplied

Structure-activity studies on inhibition of Streptococcus mutans by long-chain aliphatic diamines.

A series of long-chain aliphatic diamines, R1R2N(CH2)mNR3-CnH2n+1' was tested for in vitro inhibition of Streptococcus mutans. In general, high activity was found for all analogs with alkyl chains containing 14 to 18 carbons. The nature of the substituents on the remainder of the alkylenediamine were of secondary importance. N-hydroxyethyl substituents tend to decrease activity. Good correlations of activity with quadratic functions of diamine critical micelle concentrations were obtained.

Chemical Phenomena↗

PubMed2004

Roles of Streptococcus mutans dextranase anchored to the cell wall by sortase.

In order to clarify the role that sortase (SrtA) plays in anchoring dextranase (Dex) to the cell wall of Streptococcus mutans, both Dex- and SrtA- mutants were constructed by insertional inactivation of the respective genes. Western blot analysis with a Dex antiserum showed that in the srtA mutant the Dex was not bound to the cell wall but was secreted into the culture supernatant. In contrast, in the wild type, Dex remained cell-wall-associated. Biological properties of the srtA mutant were examined in dextran fermentation, colony morphology and adherence to a smooth surface. The srtA mutant, as well as the wild type, retained the ability to ferment dextran. However, the colony morphology of the srtA mutant on Todd Hewitt agar containing sucrose was much larger than that of the wild type and showed a ring-like structure. In addition, the srtA mutant was more adhesive to a smooth surface than the wild type when sucrose was present. However, the adhesion of the srtA mutant remarkably decreased by addition of exogenous dextranase. These studies suggest that the SrtA mediates Dex-anchoring to the cell wall in S. mutans, and cell wall-anchored Dex plays a role in controlling both the adhesive properties of extracellular glucan and the ability to utilize extracellular glucan as a nutrient source. In contrast, extracellular Dex is only responsible for degrading extracellular glucan as a nutrient source.

Aminoacyltransferases↗

PubMed1996

Insertional mutagenesis and recovery of interrupted genes of Streptococcus mutans by using transposon Tn917: preliminary characterization of mutants displaying acid sensitivity and nutritional requirements.

New vectors were constructed for efficient transposon Tn917-mediated mutagenesis of poorly transformable strains of Streptococcus mutans(pTV1-OK) and subsequent recovery of interrupted genes in Escherichia coli (pT21delta2TetM). In this report, we demonstrate the utility of Tn917 mutagenesis of a poorly transformable strain of S. mutans (JH1005) by showing (i) the conditional replication of pTV1-OK, a repA(Ts) derivative of the broad-host-range plasmid pWVO1 harboring Tn9l7, in JH1005 at the permissive temperature (30 degrees C) versus that at the nonpermissive temperature (45 degrees C); (ii) transposition frequencies similar to those reported for Bacillus subtilis (10(-5) to 10(-4)) with efficient plasmid curing in 90 to 97% of the erythromycin-resistant survivors following a temperature shift to 42 to 45 degrees C; and (iii) the apparent randomness of Tn917 insertion as determined by Southern hybridization analysis and the ability to isolate nutritional mutants, mutants in acid tolerance, and mutants in bacteriocin production, at frequencies ranging from 0.1 to 0.7%. Recovery of transposon-interrupted genes was achieved by two methods: (i) marker rescue in E. coli with the recovery vector pTV21delta2TetM, a tetracycline-resistant and ampicillin-sensitive Tn9l7-pBR322 hybrid, and (ii) "shotgun" cloning of genomic libraries of Tn917 mutants into pUC19. Sequence analyses revealed insertions at five different genetic loci in sequences displaying homologies to Clostridium spp.fhs (66% identity), E. coli dfp (43% identity), and B. subtilis ylxM-ffh (58% identity), icd (citC [69% identity]), and argD (61% identity). Insertions in icd and argD caused nutritional requirements; the one in ylxM-ffh caused acid sensitivity, while those in fhs and dfp caused both acid sensitivity and nutritional requirements. This paper describes the construction of pTV1-OK and demonstrates that it can be efficiently employed to deliver Tn917 into S. mutans for genetic analyses with some degree of randomness and that insertions in the chromosome can be easily recovered for subsequent characterization. This represents the first published report of successful Tn9l7 mutagenesis in the genus Streptococcus.

Bacterial Proteins↗