PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Streptococcus mutans”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,099 records · Page 61Linked to original sources
PubMed1984

Streptococcus mutans in saliva: intraindividual variations and relation to the number of colonized sites.

Analysis of the salivary levels of Streptococcus mutans may contribute to the evaluation of the caries risk. It is therefore important to identify factors that might influence the outcome of such analyses. This investigation consisted of three parts. The first aim was to evaluate the short-term variation of S. mutans concentration in saliva. Furthermore, we estimated the effect of discontinued oral hygiene on salivary S. mutans. We also analyzed the relation between salivary levels of S. mutans and the number of colonized approximal and occlusal sites. Tongue samples were also included in the comparison. Systematic short-term variation could not be demonstrated. A 95% confidence interval for an observed S. mutans value was obtained by multiplying and dividing the observed value by a factor of 5 (for S. mutans samples less than 10(6) or 2.3 (S. mutans greater than 10(6). One week of discontinued oral hygiene did not significantly change the level of S. mutans in saliva. Saliva samples correlated significantly with tongue samples and with the number of colonized approximal sites. The results of these studies confirm the stability of the S. mutans colonization level.

Adult↗
PubMed2003

Effect of sodium nitrite and ascorbic acid on the growth and acid production of Streptococcus mutans.

UNLABELLED: Nitrite at acid pH has been shown to be antibacterial particularly against the highly cariogenic species Streptococcus mutans. Nitrite might yield nitrosamines in vivo but ascorbic acid (vitamin C) could counteract these potential ill effects. The aim of this study is to determine whether ascorbic acid would interfere with the ability of sodium nitrite to suppress growth and acid production of S. mutans, NCTC 10449(T) and NCTC 10832. Strains were grown in Fastidious Anaerobe Broth before exposure to 200 mM nitrite in the presence of various concentrations of ascorbic acid (0.0, 5.7, 11.4, 17.0, 22.7, 28.4, 56.8, 85.2 mM). End pH was measured after 24 h exposure and cultures were serially diluted for viable counts. Statistical significance of differences in end pH values, each from 10 experiments, was determined using the Mann-Whitney U-Test. At all concentrations of ascorbic acid plus 200 mM nitrite plus S. mutans the pH was higher than with controls lacking ascorbic acid and/or nitrite (p>/=0.001). S. mutans was viable (between 4.5 x 10 (8) and 7.9 x 10 (9) cfuml (-1)) after growth in the presence of ascorbic acid at all concentrations without nitrite, whereas it was not detected when 200 mM nitrite was also present. CONCLUSIONS: ascorbic acid does not prevent the action of nitrite against S. mutans. Therefore ascorbic acid could be used in conjunction with nitrite to help counteract potential ill effects for humans.

Acids↗
PubMed2006

In vitro activity of xanthorrhizol against Streptococcus mutans biofilms.

AIMS: We determined the effect of xanthorrhizol (XTZ) purified from the rhizome of Curcuma xanthorrhiza Roxb. on the Streptococcus mutans biofilms in vitro. METHODS AND RESULTS: The biofilms of S. mutans at different phases of growth were exposed to XTZ at different concentrations (5, 10 and 50 micromol l(-1)) and for different time exposures (1, 10, 30 and 60 min). The results demonstrated that the activity of XTZ in removing S. mutans biofilm was dependent on the concentration, exposure time and the phase growth of biofilm. A concentration of 5 micromol l(-1) of XTZ completely inhibited biofilm formation by S. mutans at adherent phases of growth, whereas 50 micromol l(-1) of XTZ removed 76% of biofilm at plateau accumulated phase when exposed to S. mutans biofilm for 60 min. CONCLUSIONS: Xanthorrhizol isolated from an edible plant (C. xanthorrhiza Roxb.) shows promise as an antibacterial agent for inhibiting and removing S. mutans biofilms in vitro. SIGNIFICANCE AND IMPACT OF THE STUDY: XTZ could be used as a potential antibacterial agent against biofilm formation by S. mutans.

Biofilms↗
PubMed2002

Prevalence of salivary Streptococcus mutans in mothers and in their preschool children.

OBJECTIVES: To establish the prevalence and possible relationship of oral Streptococcus mutans colonization in mother-child pairs. DESIGN AND SETTING: An analytical cross-sectional study was carried out at a well-baby evaluation clinic held at the Public Dental Clinic, Varberg, Sweden. SAMPLE AND METHODS: Two hundred preschool children, 100 of which were 18 months old and the remaining 100 were 3 years old, and their mothers attended the clinic. All mothers were interviewed and their children's medical history, oral hygiene routines and dietary habits established. All children were clinically examined. The presence and level of S. mutans was estimated in the mother-child pairs with the aid of the Strip mutans chair-side test. RESULTS: Nearly 50% of mothers exhibited high levels of salivary S. mutans, prevalence among the 18-month- and 3-year-olds was 30% and 42%, respectively. A statistically significant (P < 0.01) mother-child relationship was found; a greater presence in mothers led to a higher number of children found harbouring the bacteria. Logistic regression analysis found that high maternal S. mutans levels (P < 0.001), daily sweet intake (P < 0.01) and sugary drinks in feeding bottles (P < 0.05) were significant factors for S. mutans colonization in children. Absence of daily toothbrushing and use of feeding bottles at night failed to fit into the model. Caries prevalence (initial and manifest decayed surfaces) was significantly related to S. mutans colonization (P < 0.01). CONCLUSION: The results support the concept of vertical transmission (mother-child), emphasizing the importance of the dietary component, and justifying a primary preventive approach with targeted action directed at mothers with high levels of S. mutans colonization.

Adult↗
PubMed2001

HtrA protease and processing of extracellular proteins of Streptococcus mutans.

A homologue of the HtrA family of stress-response proteases was detected by analysis of the Streptococcus mutans genome sequence. Disabling of the S. mutans htrA gene by insertional inactivation resulted in bacterial clumping in liquid medium, altered colony morphology and a reduced ability to withstand high temperature, extremes of pH or oxidative stress. Seven different extracellular or wall-associated proteins that are known to be subject to post-translational proteolysis were examined in cultures of wild-type S. mutans and an htrA mutant. Inactivation of the htrA protease had no effect on degradation of the proteins.

Amino Acid Sequence↗
PubMed1989

Cariogenicity of a lactate dehydrogenase-deficient mutant of Streptococcus mutans serotype c in gnotobiotic rats.

A lactate dehydrogenase-deficient (Ldh-) mutant of a human isolate of Streptococcus mutans serotype c was tested in a gnotobiotic rat caries model. Compared with the wild-type Ldh-positive (Ldh+) strains, it was significantly (alpha less than or equal to 0.005) less cariogenic in experiments with two different sublines of Sprague-Dawley rats. The Ldh- mutant strain 044 colonized the oral cavity of the test animals to the same extent as its parent strain 041, although its initial implantation was slightly but not significantly (P greater than or equal to 0.2) less. Multiple oral or fecal samples plated on 2,3,5-triphenyltetrazolium indicator medium revealed no evidence of back mutation from Ldh- to Ldh+ in vivo. Both Ldh+ strain 041 and Ldh- strain 044 demonstrated bacteriocinlike activity in vitro against a number of human strains of mutans streptococci representing serotype a (S. cricetus) and serotypes c and e (S. mutans). Serotypes b (S. rattus) and f (S. mutans) and strains of S. mitior, S. sanguis, and S. salivarius were not inhibited. Thus, Ldh mutant strain 044 possesses a number of desirable traits that suggest it should be investigated further as a possible effector strain for replacement therapy of dental caries. These traits include its stability and low cariogenicity in the sensitive gnotobiotic rat caries model, its bacteriocinlike activity against certain other cariogenic S. mutans (but not against more inocuous indigenous oral streptococci), and the fact that it is a member of the most prevalent human serotype of cariogenic streptococci.

Animals↗
PubMed2004

Inactivation of srtA gene of Streptococcus mutans inhibits dextran-dependent aggregation by glucan-binding protein C.

A sortase-deficient mutant of Streptococcus mutans was prepared by insertional inactivation of a sortase gene (srtA). The srtA mutant was defective in cell wall-anchoring of two surface proteins 200 and 75 kDa in size. A previous study has shown that the 200 kDa protein is a surface protein antigen PAc and that the sortase catalyzes cell wall-anchoring of PAc in S. mutans. In this study another surface protein 75 kDa in size was examined by immunologic and physiologic methods. Western blot analysis with a specific antiserum showed that the 75 kDa protein was a surface protein, glucan-binding protein C. The protein was overexpressed under a stress condition including a sublethal concentration of tetracycline. The srtA mutant cells also lost the ability of dextran-dependent aggregation. These results suggest that the S. mutans sortase mediates cell wall-anchoring of the glucan-binding protein C and dextran-dependent aggregation of this organism.

Adhesins, Bacterial↗
PubMed1993

Molecular characterization of a STreptococcus mutans mutant altered in environmental stress responses.

A mutant defective in aciduricity, GS5Tn1, was constructed following mutagenesis of Streptococcus mutans GS5 with the conjugative transposon Tn916. The mutant grew poorly at acidic pH levels and was sensitive to high osmolarity and elevated temperatures. These properties resulted from a single insertion of Tn916 into the GS5 chromosome, and the DNA fragment harboring the transposon was isolated into the cosmid vector, charomid 9-20. Spontaneous excision of Tn916 from the cosmid revealed that Tn916 inserted into a 8.6-kb EcoRI fragment. On the basis of the restriction analyses of insert fragments, it was found that Tn916 inserted into a 0.9-kb EcoRI-XbaI fragment. Nucleotide sequence analysis of this fragment indicated the presence of two open reading frames, ORF1 and ORF2. By using a marker rescue strategy, a 6.0-kb HindIII fragment including the target site for Tn916 insertion and the 5' end of ORF1 was isolated and sequenced. The deduced amino acid sequences of ORF1 and ORF2 showed significant homology with the diacylglycerol kinase and Era proteins, respectively, from Escherichia coli. Nucleotide sequence analysis of the Tn916 insertion junction region in the GS5Tn1 chromosome revealed that the transposon inserted near the 3' terminus of ORF1. Restoration of ORF1 to its original sequence in mutant GS5Tn1 was carried out following transformation with integration vector pVA891 containing an intact ORF1. The resultant transformant showed wild-type levels of aciduricity as well as resistance to elevated temperatures and high osmolarity. These results suggest that the S. mutans homolog of diacylglycerol kinase is important for adaptation of the organism to several environmental stress signals.

Amino Acid Sequence↗
PubMed1990

Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt.

The nucleotide sequence of the gbp gene, which encodes the glucan-binding protein (GBP) of Streptococcus mutans, was determined. The reading frame for gbp was 1,689 bases. A ribosome-binding site and putative promoter preceded the start codon, and potential stem-loop structures were identified downstream from the termination codon. The deduced amino acid sequence of the GBP revealed the presence of a signal peptide of 35 amino acids. The molecular weight of the processed protein was calculated to be 59,039. Two series of repeats spanned three-quarters of the carboxy-terminal end of the protein. The repeats were 32 to 34 and 17 to 20 amino acids in length and shared partial identity within each series. The repeats were found to be homologous to sequences hypothesized to be involved in glucan binding in the GTF-I of S. downei and to sequences within the protein products encoded by gtfB and gtfC of S. mutans. The repeated sequences may represent peptide segments that are important to glucan binding and may be distributed among GBPs from other bacterial inhabitants of plaque or the oral cavity.

Amino Acid Sequence↗
PubMed2004

A two-component covRS regulatory system regulates expression of fructosyltransferase and a novel extracellular carbohydrate in Streptococcus mutans.

The expression of fructosyltransferase (FTF), the enzyme that synthesizes fructan from sucrose, is regulated in the cariogenic bacterium Streptococcus mutans. However, the exact mechanism of FTF regulation is unknown. In this study, the role of a two-component regulatory system (covRS) in FTF expression was investigated. A CovR-defective mutant of S. mutans NG8 was constructed by homologous recombination. By use of immunoblotting, the mutant was shown to overexpress FTF in the absence of sucrose, while the wild type and a covRS-complemented mutant showed sucrose-inducible FTF expression. Reverse transcription-PCR showed that the ftf transcript levels were increased in the covR mutant, suggesting regulation at the transcriptional level. The covR mutant was also found to overproduce extracellular carbohydrate, and this phenotype was reversed by covRS complementation. Paper chromatographic studies and chemical tests showed that the extracellular carbohydrate contained glucose and glucuronic acid but not fructose. These results suggest that the extracellular carbohydrate was not fructan. The production of a glucose- and glucuronic acid-containing extracellular carbohydrate has not been reported for S. mutans and may be considered novel. In conclusion, the results indicate that the expression of FTF and a glucose- and glucuronic acid-containing carbohydrate was negatively regulated by the covRS two-component regulatory system in S. mutans.

Bacterial Proteins↗
PubMed1980

Immunisation with a purified protein from Streptococcus mutans against dental caries in rhesus monkeys.

A purified protein antigen, molecular weight 185,000, was prepared from Streptococcus mutans and used in the immunisation of monkeys against dental caries. 1 mg of this antigen, mixed with adjuvant and injected subcutaneously, elicited serum IgG and to a lesser extent IgA antibodies. Compared with sham-immunised monkeys, those receiving this antigen had a 70% reduction in dental caries and a smaller growth of Strep. mutans from dental plaque. The results suggest that the defined protein material isolated from Strep. mutans may be one of the antigens eliciting a protective immune response against dental caries. This antigen seems to be a suitable candidate for consideration as a vaccine for man.

Animals↗
PubMed1986

Transformation of Streptococcus mutans with chromosomal and shuttle plasmid (pYA629) DNAs.

Transformation (i.e., DNase-sensitive genetic transfer) of strains of Streptococcus mutans representing serotypes c and e was accomplished by using chromosomal DNA from a Rifr Strr Spcr isolate of strain GS5 (UAB525) and a chimeric plasmid, pYA629. Shuttle plasmid pYA629 comprises the S. mutans plasmid pVA318, an inducible erythromycin resistance determinant originally isolated from a group A streptococcal strain, the tetracycline resistance gene and replication region of the Escherichia coli plasmid pBR322, and the promoter region of the S. mutans gene for aspartate beta-semialdehyde dehydrogenase. The strains examined for recipient ability included those known to lack a cryptic plasmid (GS5, UA130, UA159, and MT8148) and those known to contain a widely disseminated 5.8-kilobase cryptic plasmid (LM7, V318, UA101, UA174, and 3098791). The transformation frequencies in GS5 for GS5 chromosomal antibiotic resistance markers were comparable to those reported by others, but UA101, UA130, UA159 and UA174 were transformed with both chromosomal and plasmid markers at much higher efficiencies. In a larger strain survey, strains containing the 5.8-kilobase cryptic plasmid were more frequently transformable with both chromosomal and pYA629 DNAs than were strains lacking this cryptic plasmid. All plasmid-containing strains except LM7 lost their resident cryptic plasmids when transformed with pYA629. LM7 transformed with pYA629 retained pLM7. There are therefore at least two incompatibility groups among S. mutans cryptic plasmids. yPA629 DNA isolated from either E. coli or S. mutans transformed S. mutans with equal efficiency. pYA629 DNA isolated from S. mutans transformed both restriction-deficient and restriction-proficient E. coli recipients. Therefore, the strains of S. mutans used lack a restriction-modification system for pYA629 DNA sequences. S. mutans strains that are readily transformable, display maximal cariogenicity in gnotobiotic rats, and give high scores for in vitro measures of important virulence attributes have been identified to facilitate studies on the genetic basis and control of virulence.

Animals↗
PubMed1976

Streptococcus mutans dextransucrase: mode of interaction with high-molecular-weight dextran and role in cellular aggregation.

The interaction between Streptococcus mutans dextransucrase (EC 2.4.1.5) and high-molecular-weight dextran was studied in both the presence and absence of substrate sucrose. Equivalent weight-percent solutions of primer dextrans that differed 200-fold in molecular weight were found to be equally efficient in priming new dextran synthesis. Sodium borohydride reduction of dextran had no effect on its priming ability. These results suggest that dextran synthesis proceeds by addition of glucosyl residues to nonreducing termini of primer dextrans and that several enzyme molecules simultaneously bind to single high-molecular-weight dextran molecules. Kinetic data suggested that dextransucrase contains only one dextran binding site per enzyme molecule. The nature of the commonly observed highly aggregated state of dextransucrase was also studied. Two types of enzyme aggregates were distinguished: (i) oligomeric enzyme aggregates that formed in the absence of dextran and were dissociated by 1 M KCl; and (ii) dextran-induced enzyme aggregates that were stable to 3 M salt. Oligomeric enzyme aggregates were obtained from supernatants of fructose-grown cultures, whereas dextran-induced enzyme aggregates appeared to be present in glucose-grown cultures. The molecular weight of the smallest species of dextran-free detransucrase observed in solutions of 1 M KCl was estimated to be 40,000 by gel column chromatography. Addition of dextran to primer-dependent dextransucrase resulted in formation of complexes that were stable in CsCl density gradients and exhibited a buoyant density of 1.382 g/cm3 as compared with a buoyant density of 1.302 g/cm3 exhibited by dextransucrase. The enzyme-dextran complexes observed in CsCl density gradients contained about 25% dextran. This corresponded to 150 enzyme molecules (molecular weight, 40,000) per dextran molecule (molecular weight, 2 X 10(6)). The implication of these results to the mechanism of sucrose- and dextran-induced aggregation of S. mutans is discussed.

Binding Sites↗
PubMed1998

[The experimental study of immunization with purified surface protein antigen I/II from streptococcus mutans in BALB/c mice].

OBJECTIVE: To study the immunogenicity and immunoreactivity of purified surface protein antigen I/II from streptococcus mutans. METHODS: Purified antigen I/II was used to immune BALB/c mice by subcutaneous injection route, and S. mutans whole cells were used as comparison. RESULTS: ELISA showed immunization with antigen I/II highly induced both specific serum IgG antibody and specific salivary IgA antibody against antigen I/II (P < 0.01), but immunization with whole cells only induced specific serum IgG antibody (P < 0.05). CONCLUSION: The study suggest purified antigen I/II is an effective candidate vaccine.

Animals↗
PubMed2001

Influence of starvation and biofilm formation on acid resistance of Streptococcus mutans.

The aim of this study was to investigate acid resistance induced by starvation or biofilm formation in Streptococcus mutans ATCC 25175. The artificial biofilms were made on cover glasses, starved for 24 h and immersed in 0.1 M lactate buffer at pH 3.8 for 10 min. The biofilms were also exposed to 5% sucrose solution for 20 min to simulate acid shock produced by sucrose metabolism. Confocal laser scanning microscopy with fluorescein isothiocyanate staining measured the resultant minimum pH in biofilms. Live and dead organisms in biofilms were differentiated by confocal laser scanning microscopy with proidium iodide and SYTO9 staining. The same processes were used to treat planktonic organisms. The results showed that starved biofilms or planktonic cells showed significantly more viable bacteria after acid shock induced either by lactic acid or during sucrose consumption than non-starved biofilms or planktonic cells. In addition, biofilms showed greater resistance to acid shock induced by lactic acid than planktonic cells, whereas similar results were obtained where sucrose was used as a carbon source to reduce pH in biofilms and planktonic cells. Thus, it is suggested that starvation protects both biofilm and planktonic S. mutans from acid shock induced either by lactic acid or during sucrose consumption, while biofilm formation seemed to protect bacteria only from acid shock induced by pH 3.8 lactate buffer but not the acid shock of a slightly higher pH produced during sucrose consumption.

Biofilms↗
PubMed1992

Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and sugar-specific phosphotransferase system components of the lactose operon of Streptococcus mutans.

The complete nucleotide sequences of lacRABCDF and partial nucleotide sequence of lacE from the lactose operon of Streptococcus mutans are presented. Comparison of the streptococcal lac determinants with those of Staphylococcus aureus and Lactococcus lactis indicate exceptional protein and nucleotide identity. The deduced polypeptides also demonstrate significant, but lower, sequence similarity with the corresponding lactose proteins of Lactobacillus casei. Additionally, LacR has sequence homology with the repressor (DeoR) of the Escherichia coli deoxyribonucleotide operon, while LacC is similar to phosphokinases (FruK and PfkB) from E. coli. The primary translation products of the lacRABCDFE genes are polypeptides of 251 (M(r) 28,713), 142 (M(r) 15,610), 171 (M(r) 18,950), 310 (M(r) 33,368), 325 (M(r) 36,495), 104 (M(r) 11,401), and 123 (NH2-terminal) amino acids, respectively. As inferred from their direct homology to the staphylococcal lac genes, these determinants would encode the repressor of the streptococcal lactose operon (LacR), galactose-6-phosphate isomerase (LacA and LacB), tagatose-6-phosphate kinase (LacC), tagatose-1,6-bisphosphate aldolase (LacD), and the sugar-specific components enzyme III-lactose (LacF) and enzyme II-lactose (LacE) of the S. mutans phosphoenolpyruvate-dependent phosphotransferase system. The nucleotide sequence encompassing the S. mutans lac promoter appears to contain repeat elements analogous to those of S. aureus, suggesting that repression and catabolite repression of the lactose operons may be similar in these organisms.

Amino Acid Sequence↗