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PubMed1991

Effect of variation in growth conditions on the activity of dextranase inhibitor in continuous cultures of Streptococcus sobrinus.

The activity of free extracellular dextranase inhibitor was determined in strains of Streptococcus sobrinus which were grown in a chemostat under a variety of defined conditions. Maximum release of dextranase inhibitor occurred at low growth rate in glucose-limited medium at pH 6.5. Free inhibitor could not be detected when the strains were grown at high growth rate or in batch culture.

Culture Media↗

PubMed2001

Purification and characterization of an oligo-isomaltosaccharide synthase from a Streptococcus sobrinus glucosyltransferase-I deficient mutant.

One glucosyltransferase (GTF) -I deficient mutant of Streptococcus sobrinus strain B13N was isolated through chemical mutagenesis with ethyl methanesulfonate, and characterized. This mutant, designated as B13N-Id, readily allowed us to purify a homogeneous oligo-isomaltosaccharide synthase (GTF-S) from its culture fluid. The purified GTF-S was only recognized with rabbit polyclonal antibody against recombinant GTF-S from an Ecsherichia coli MD124 clone expressing the B13N gtfS gene, and showed the almost same enzymatic properties as the recombinant enzyme. A double reciprocal plot of the B13N GTF-S for sucrose was biphasic, and the affinity for this substrate was high compared to that of GTF-S enzymes from other strains.

Chromatography, High Pressure Liquid↗

PubMed1999

Immunolabeling of the major cell surface protein antigen of Streptococcus sobrinus with monoclonal antibody.

OBJECTIVE: The purpose of this study was to determine the accessibility of monoclonal antibody (McAb), specific for the major cell surface protein antigen (PAg) of Streptococcus sobrinus, to the surface of its native epitopes. MATERIALS AND METHODS: An indirect immunogold labeling technique was used to detect the reaction of McAb with S. sobrinus 6715. The reactions of polyclonal antibodies (PcAbs) against S. sobrinus 6715 or PAg with S. sobrinus 6715, S. mutans Ingbritt C and S. rattus BHT were studied as controls. RESULTS: The results indicated that PAg was localized on the outer cell surface of S. sobrinus, and McAb was reactive with only a few epitopes of the cell surface, whereas PcAbs were found to be reactive with more epitopes. CONCLUSIONS: McAb was specific for the PAg, but there was cross-reaction with S. mutans. Also there seemed to be an association between the fuzzy coat on the surface of S. sobrinus and PAg.

Adhesins, Bacterial↗

PubMed2003

Effects of low-concentrated chlorhexidine on growth of Streptococcus sobrinus and primary human gingival fibroblasts.

The aim of this study was to investigate the in vitro effects of low concentrations of chlorhexidine (CHX) on the proliferation of Streptococcus sobrinus (ATCC 33478) and primary human gingival fibroblasts (HGF). Liquid cultures of bacteria or human gingival fibroblasts were exposed to CHX concentrations ranging from 0.07 to 40 microM in microtiter plates at 37 degrees C for 24 h. Bacteria or cells grown without CHX served as controls. The effects of CHX were determined either by measurements of the optical density (OD) of bacterial cultures or by evaluation of cell growth with the DNA-intercalating fluorescent stain H33342 in comparison to untreated controls. Results were evaluated calculating means and standard deviations. Data were statistically analyzed by an ANOVA using Post Hoc tests ( p<0.005). No growth inhibition of S. sobrinus was found at concentrations between 0.07 and 0.15 microM CHX, whereas 0.3 microM CHX led to an elongated (2 h more) lag phase and 0.6 microM CHX induced a lag phase of 4 h more and a minor inclination of the curve in the log phase. Concentrations of CHX>/=1.25 microM completely inhibited growth of S. sobrinus. On the contrary, CHX showed no significant effect on growth of HGF at concentrations </=5 microM. A slight growth inhibition was only observed at a concentration of 5 microM. CHX-concentrations of 10 and 20 microM reduced cell growth to 88 or 75% of control assays. Data analysis showed that overall treatment effects were highly significant ( p<0.005). Our data reveal that chlorhexidine inhibits proliferation of S. sobrinus even at very low concentrations while concentrations of CHX</=5 microM are not cytotoxic to human gingival fibroblasts.

Analysis of Variance↗

PubMed1999

Structure and enzymatic properties of genetically truncated forms of the water-insoluble glucan-synthesizing glucosyltransferase from Streptococcus sobrinus.

Glucosyltransferase-I (GTF-I: 175 kDa) of a cariogenic bacterium, Streptococcus sobrinus 6715, mediates the conversion of water-soluble dextran (alpha-1,6-glucan) into a water-insoluble form by making numerous alpha-1,3-glucan branches along the dextran chains with sucrose as the glucosyl donor. The structures and catalytic properties were compared for two GTF-I fragments, GTF-I' (138 kDa) and GS (110 kDa). Both lack the N-terminal 84 residues of GTF-I. While GTF-I' still contains four of the six C-terminal repeats characteristic of streptococcal glucosyltransferases, GS lacks all of them. Electron microscopy of negatively stained samples indicated a double-domain structure for GTF-I', consisting of a spherical head with a smaller spherical tail, which was occasionally seen as a long extension. GS was seen just as the head portion of GTF-I'. In the absence of dextran, both fragments simply hydrolyzed sucrose with similar K(m) and k(cat) values at low concentrations (<5 mM). At higher sucrose concentrations (>10 mM), however, GTF-I' exhibited glucosyl transfer activity to form insoluble alpha-1, 3-glucans. So did GS, but less efficiently. Dextran increased the rate and efficiency of the glucosyl transfer by GTF-I'. On removal of the C-terminal repeats of GTF-I' by mild trypsin treatment, this dextran-stimulated transfer was completely lost and the dextran-independent transfer became less efficient. These results indicate that the N-terminal two-thirds of the GTF-I sequence are organized as a structurally and functionally independent domain to catalyze not only sucrose hydrolysis but also glucosyl transfer to form alpha-1,3-glucan chains, although not efficiently; the C-terminal repeat increases the efficiency of the intrinsic glucosyl transfer by the N-terminal domain as well as rendering the whole molecule primer-dependent for far more efficient insoluble glucan synthesis.

Bacterial Proteins↗

PubMed1995

Oral immunization with recombinant Salmonella typhimurium expressing surface protein antigen A of Streptococcus sobrinus: dose response and induction of protective humoral responses in rats.

An attenuated, recombinant Salmonella typhimurium mutant, chi 4072(pYA2905), expressing the surface protein antigen A (SpaA) of Streptococcus sobrinus was investigated for its effectiveness in inducing protective immune responses against S. sobrinus-induced dental caries in an experimental caries model. Fischer rats were orally immunized with either 10(8) or 10(9) CFU of S. typhimurium chi 4072(pYA2905). Persistence of salmonellae in Peyer's patches and spleens and the induction of immune responses were determined. Maximum numbers of salmonellae were recovered from Peyer's patches of rats within the first week of immunization, with higher numbers recovered from rats given 10(9) CFU than from those given 10(8) CFU. Serum anti-Salmonella and anti-SpaA responses increased more rapidly in rats given 10(9) CFU than in rats given 10(8) CFU. The salivary antibody response to SpaA increased with time, but the response varied in the two groups. In a separate study, rats were orally immunized with the recombinant Salmonella mutant and then challenged with cariogenic S. sobrinus 6715. The levels of serum and salivary antibody and caries activity were assessed at the termination of the experiment. Higher levels of salivary immunoglobulin A antibody to SpaA and Salmonella carrier were detected in rats given 10(9) CFU than in those given 10(8) CFU, and these responses were higher than those in nonimmunized controls. Mandibular molars from immunized rats had lower numbers of recoverable streptococci and less extensive carious lesions than those from nonimmunized, control rats. These data indicate that oral immunization with an attenuated recombinant S. typhimurium expressing SpaA of S. sobrinus induces the production of antigen-specific mucosal antibody and confers protection against dental caries.

Administration, Oral↗

PubMed1989

Molecular and immunochemical characterization of recombinant Escherichia coli containing the spaA gene region of Streptococcus sobrinus.

We identified and characterized a recombinant Escherichia coli containing the entire gene for surface protein antigen A (spaA) of Streptococcus sobrinus 6715. The recombinant E. coli was isolated from a cosmid gene bank of size-fractionated S. sobrinus DNA fragments, and recombinants expressing the SpaA protein were detected immunologically. Subcloning experiments showed that the DNA sequences encoding the SpaA protein could be isolated on two contiguous EcoRI fragments, 3.7 and 3.3 kilobases (kb) in size, both contained on a 16.2-kb BglII fragment. Southern blot hybridization experiments using the EcoRI fragments to probe genomic DNAs from various serotypes of the mutans group of streptococci revealed DNA sequence homology not only to S. sobrinus 6715 (serotype g) chromosomal DNA but also to S. sobrinus serotype d DNA. Weak hybridization signals to Streptococcus mutans serotypes c, e, and f and to Streptococcus cricetus serotype a were observed with the 3.3-kb EcoRI fragment. These results suggest that the coding sequence for the spaA gene is probably conserved in S. sobrinus strains. Plasmid-encoded polypeptides made in E. coli minicells revealed that transcription of the spaA gene was initiated on the 3.7-kb EcoRI fragment and that its product size was about 210 kilodaltons. The cloned SpaA protein was purified from the periplasmic protein of E. coli, and monospecific antiserum against the cloned product was prepared in rabbits. The data obtained from various physiochemical and immunological procedures allowed us to conclude that the coding sequence for the entire spaA gene of S. sobrinus 6715 had been successfully cloned in E. coli and that faithful expression of the cloned product could be obtained.

Bacterial Proteins↗

PubMed1989

Characterisation of monoclonal antibodies to common protein epitopes on the cell surface of Streptococcus mutans and Streptococcus sobrinus.

Three monoclonal antibodies (MAb) were prepared against a cell surface antigen which cross-react between Streptococcus mutans (serotypes c, e and f) and Streptococcus sobrinus (serotypes d and g). Two of the MAb also recognise a determinant on the surface of Streptococcus cricetus (serotype a). The common antigen shared between S. mutans and S. sobrinus was demonstrated by Western blotting to be about 200 kD in size. This antigen is shared not only by the cell surfaces of serotypes a, c, d, e, f and g, but also by the major cell surface antigen of S. mutans of 185 kD and another of 150 kD. These MAb identify all but one mutans type of streptococci and can be utilised as analytical reagents.

Antibodies, Monoclonal↗

PubMed1999

Effects of monoclonal antibody on colonization of Streptococcus sobrinus and development of dental caries in rats.

OBJECTIVE: To investigate the effect of local application of monoclonal antibody (McAb) raised against the 210KD cell surface protein antigen (PAg) of Streptococcus sobrinus on the colonization of rats' teeth and the development of dental caries. MATERIALS AND METHODS: Thirty Wistar rats were divided into 3 groups: group 1 received McAb against PAg; group 2 received unrelated mice ascites; group 3 received pure buffered saline. The bacteria were applied 6 times to the occlusal surfaces of molars and to the labial surfaces of incisors. After three applications, streptomycin-resistant S. sobrinus 6715 was applied to the teeth and the rats were fed with caries-inducing diet 2000. The number of colonized S. sobrinus was counted on the streptomycin-supplemented mutans streptocci agar and expressed as a percentage of the total colonies on BHI agar. The presence of caries was examined and scored following Keyes' procedure. RESULTS: There were significantly lower levels of colonization by S. sobrinus on rats' teeth and lower mean caries scores on the teeth treated with McAb compared with those in the control groups. CONCLUSION: Local passive immunization with McAb against PAg may be an effective way to prevent colonization by implanted S. sobrinus and development of dental caries.

Analysis of Variance↗

PubMed1992

Genetic analysis of scrA and scrB from Streptococcus sobrinus 6715.

A DNA fragment containing scrA and scrB, which encode enzyme II of the phosphoenolpyruvate-dependent sucrose phosphotransferase system and sucrose-6-phosphate hydrolase, respectively, was isolated from a lambda gt10 genomic DNA library of Streptococcus sobrinus 6715. Both genes were located on a 4.2-kb DNA fragment which was maintained stably in Escherchia coli on low-copy-number vector pGB2. The recombinant E. coli clone expressed sucrose-hydrolytic activity on MacConkey agar base supplemented with raffinose or sucrose. Results from deletion analysis showed that the sucrose-metabolic activity was contained within a 3.5-kb region. The lactic acid bacterium Lactococcus lactis subsp. lactis LM0230, which is devoid of sucrose-metabolic activity, was used to study the enzyme activities encoded by scrA and scrB from S. sobrinus 6715. L. lactis transformants carrying the 4.2-kb S. sobrinus-derived DNA fragment on E. coli-Streptococcus shuttle vector pDL278 were able to grow at the expense of sucrose and exhibited enzyme II and sucrose-6-phosphate hydrolase activities. Results from hybridization studies and a comparison of the restriction endonuclease maps of the scrA- and scrB-containing chromosomal regions from S. mutans GS5 and S. sobrinus 6715 suggested considerable divergence.

DNA Probes↗

PubMed1989

Genetic characterization of the spaA1 determinant of the surface protein antigen gene from Streptococcus sobrinus 6715.

1. The surface protein antigen-encoding gene spaA1, previously cloned from Streptococcus sobrinus 6715 (serotype g) into the plasmid pACYC184, was examined. 2. The gene product of pYA726 was identified both by the minicell method and by in vitro transcription-translation system as a protein whose mol. wt was estimated to be 140,000. 3. The spaA1 gene was localized on the 3.75 kb AvaI-BamHI fragment of the cloned DNA. 4. An internal spaA1 promoter located close to one end of the 1.25 kb AvaI fragment within the 3.75 kb AvaI-BamHI fragment initiated the transcription for the insert DNA of S. sobrinus autonomously.

Bacterial Proteins↗

PubMed1991

Chain formation and de-chaining in Streptococcus sobrinus SL-1.

Regulation of chain length by chain-forming bacteria is believed to depend on wall-associated autolytic activity and environmental conditions. In this study, the chain length of Streptococcus sobrinus SL-1 was determined under various initial culture and pH conditions and NaF concentrations. Crude wall extracts were prepared by dilute alkali treatment of whole cells and were tested for de-chaining activity. The results indicate that S. sobrinus SL-1 grows primarily as short chains under alkaline growth conditions and at high (3.0 mM) medium fluoride levels, and growth as long chains occurs under acidic growth conditions. De-chaining activity was observed following incubation of the longer chain form of the organism with crude wall extracts. The evidence suggests that the chain length of S. sobrinus SL-1 depends on environmental conditions, including pH and fluoride, and that cell wall-associated factors may be active in regulating the chain length of the organism.

Autolysis↗

PubMed1993

Immune responses to Streptococcus sobrinus surface protein antigen A expressed by recombinant Salmonella typhimurium.

In this study, we used a vaccine strain of Salmonella typhimurium to express antigenic determinants of the SpaA antigen of Streptococcus sobrinus, which is involved in the caries-forming process. We cloned either a single repeat (pYA2901) or three tandem repeats (pYA2905) of the 0.48-kb fragment of the spaA gene, which codes for an important component of the SpaA protein, plus a 1.2-kb minor antigenic determinant and measured the resulting immune responses to SpaA in orally immunized BALB/c mice. The single or triple repeat of the spaA gene fragment was inserted into the Asd+ vector pYA292 and was transformed into the S. typhimurium delta cya delta crp vaccine strain chi 4072 containing delta asd in the chromosome. Female BALB/c mice were then orally immunized with two doses of the S. typhimurium containing either of the two SpaA constructs, and the immune responses to the expressed SpaA protein were assessed. Significant serum immunoglobulin G (IgG) anti-SpaA titers were detected in mice immunized with chi 4072(pYA2905) but not chi 4072(pYA2901). Salivary anti-SpaA IgA titers were minimal and were only detected in mice immunized with S. typhimurium expressing the SpaA encoded by pYA2905. Intestinal anti-SpaA IgA titers, however, were detected in both groups of mice, particularly in mice immunized with chi 4072(pYA2905). An oral booster 26 weeks after the initial series of immunizations resulted in increased serum IgG titers in both chi 4072(pYA2901)- and chi 4072(pYA2905)-immunized animals, particularly in the chi 4072(pYA2905)-immunized animals. No anamnestic IgA response was detected in the saliva following the booster immunization.

Animals↗

PubMedDate not supplied

Peroxidase reaction as a parameter for discrimination of Streptococcus mutans and Streptococcus sobrinus.

425 strains of mutans streptococci and 12 reference strains were investigated by membrane fatty acid spectra (MFAS) and peroxidase reaction (PR) after aerobic and anaerobic incubation. 423 strains were identified as Streptococcus mutans. The remaining 2 strains were identified as Streptococcus sobrinus. The PR of 29 strains was doubtful; immediately after anaerobic incubation a negative PR changed into a slightly positive PR. To test the diagnostic value of PR the strains were additionally investigated by means of species-specific polymerase chain reactions (PCR). The species-specific PCRs were developed on the basis of the respective genes of 16S rRNA of the pathogens S. mutans and S. sobrinus. Specificity and sensitivity were tested on reference strains (n = 17) and negative control strains (n = 39). The results of this investigation showed that an anaerobic incubation regime could lead to false-positive (S. mutans) or false-negative (S. sobrinus) PR. The 425 MS strains were classified as either S. mutans (n = 420) or S. sobrinus (n = 5). The findings on the reference strains required a reclassification of S. mutans V 100 into S. sobrinus V 100. Summarising, it is possible now to differentiate strains of mutans streptococci by MFAS and PR after aerobic incubation.

Aerobiosis↗

PubMed1997

Screening of antiadherent activity on Streptococcus sobrinus culture.

The mutans group of streptococci is considered to play a key role in the etiology of dental caries. We have evaluated the ability of different substances to prevent dental plaque formation without affecting Streptococcus sobrinus viability. Viable organisms were detected as CFU/mL in agar plates and bacterial adherence was assessed by dry weight. We studied 23 compounds and we demonstrated that phenyl salicylate, phenylmercuric nitrate and potassium iodate are more effective to inhibit adhesion without showing antibacterial activity.

Anti-Infective Agents, Local↗

PubMed1989

Use of 13C-n.m.r. spectroscopy for the quantitative estimation of 3-O- and 3,6-di-O-substituted D-glucopyranosyl residues in alpha-D-glucans formed by the D-glucosyltransferases of Streptococcus sobrinus.

The 13C-n.m.r. spectra of the three alpha-D-glucans from Streptococcus sobrinus and the dextran from Leuconostoc mesenteroides, which differ widely in the ratios of omega (terminal, nonreducing) D-glucopyranosyl groups: 3-:6-:3,6-linked D-glucopyranosyl (Glc) residues, were measured in 0.5M NaOH at 22 degrees. The C-1 signals of 3-O-substituted Glc in a linear sequence, 6-O-substituted Glc in a linear sequence, 3,6-di-O-substituted Glc in a (1----6)-linked sequence, and Glc attached to O-3 of 3,6-di-O-substituted Glc were distinguished from each other. The C-3 signal of 3,6-linked Glc appeared downfield by 0.6 to 1.0 p.p.m. compared to the C-3 signal of 3-linked Glc in a linear sequence. The C-6 signals of omega-terminal, 3-linked, 6-linked, and 3,6-linked Glc were also assigned. The C-2 signal of 3-linked Glc in a linear sequence appeared separately, at 73.76 p.p.m. Based on these assignments, the various D-glucopyranosyl residues of the S. sobrinus alpha-D-glucans were quantitatively estimated from the signal areas of the C-2 atom of 3-linked Glc, the C-3 atom of 3-linked and 3,6-linked Glc, the C-6 atom of 6-linked and 3,6-linked Glc, and the C-6 atom of the omega-Glc groups and 3-linked Glc residues. The figures thus derived for the linkage ratios were close to those obtained by methylation analysis.

Carbohydrate Conformation↗

PubMed1993

Effect of monoclonal antibodies on the colonization of rats by Streptococcus sobrinus.

Local passive immunization has been suggested as a method of preventing colonization of teeth by mutans streptococci. In this study we describe the effect of local application of monoclonal antibodies (Mabs) on the colonization of Streptococcus sobrinus. The rats, 37 days old, were divided in 4 groups: group 1 received Mab OMVU10 (Mab reactive with Antigen B of S. sobrinus, IgG2b), group 2 received Clone 24 (Mab reactive with lipid A of Escherichia coli, IgG2b), group 3 received uninoculated culture medium, and group 4 received phosphate-buffered saline (PBS). Mabs were applied 6 times on the surfaces of the molars and the labial surfaces of the incisors of the rats, on days 37, 40, 44, 46, 49 and 54 after birth. After the third application of Mabs, all rats were inoculated with S. sobrinus (day 45). Subsequently, the rats were fed a cariogenic diet containing 20% sucrose and 5% glucose. The rats were killed 34 days after inoculation and the maxillary molars were extracted and homogenized in order to determine the numbers of S. sobrinus. The proportions of S. sobrinus, expressed as a percentage of the total cultivable microflora, in rats which received OMVU10 (group 1) were 23.1 +/- 14.8%, whereas in rats which received Clone 24, culture medium or PBS the levels were 34.5 +/- 11.3%, 40.7 +/- 14.9% and 36.7 +/- 9.7%, respectively. Statistical analysis showed that the level of colonization of rats which received OMVU10 was significantly lower than that of rats which received Clone 24, culture medium or PBS (p < 0.001, p < 0.013 and p < 0.01, respectively).(ABSTRACT TRUNCATED AT 250 WORDS)

Analysis of Variance↗

PubMed1991

The extension of alpha-D-1,3-branch linkages by 1,3-alpha-D-glucan synthase from Streptococcus sobrinus.

In the presence of an acceptor, 1,3-alpha-D-glucan synthase of Streptococcus sobrinus synthesizes water-insoluble glucans from sucrose. Under such conditions, 1,3-alpha-D-glucoside linkages were extended without any change in the glucose-residue number between the 1,3,6-branch points on the acceptor. From these results, the mechanisms of water-insoluble-glucan formation were proposed as follows: (i) the attachment of an acceptor to the glucan binding sites of 1,3-alpha-D-glucan synthase occurs during the initiation of the reaction, and concurrently determines the positions of the branched portions of 1,3,6 on the acceptor, and (ii) the 1,3-alpha-D-glucoside linkage extends from these positions.

Carbohydrate Conformation↗