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PubMed1995

Immunization of rats with synthetic peptide constructs from the glucan-binding or catalytic region of mutans streptococcal glucosyltransferase protects against dental caries.

Previously, we have described peptide constructs from two regions of glucosyltransferase (GTF) of mutans streptococci. A putative catalytic site in the amino-terminal half of the molecule and a repeated glucan-binding site in the carboxyl-terminal half of GTF were the regions upon which sequences were based. The present study explored the effects of immunization with these peptide constructs (called CAT or GLU) and with streptococcal GTFs from Streptococcus sobrinus and S. mutans on immunological, microbiological, and disease parameters. Groups of immunized Sprague-Dawley rats were infected with either 10(8) S. sobrinus 6715 or 10(8) S. mutans SJ32 organisms. Serum immunoglobulin G antibody levels, determined by enzyme-linked immunosorbent assay, to the respective peptide constructs and to the appropriate streptococcal GTF were significantly increased (after immunization) prior to infection and at the end of the experiment. Also, serum antibody from CAT-, GLU-, and S. sobrinus GTF-immunized rats inhibited S. sobrinus GTF-mediated insoluble glucan synthesis (all) and S. mutans GTF-mediated soluble glucan synthesis (all except anti-GLU) from sucrose. Immunization with the CAT or GLU peptide construct resulted in significantly reduced smooth surface and sulcal caries after infection with S. sobrinus. Sulcal dental caries after infection with S. mutans SJ32 were also significantly reduced in CAT- and GLU-immunized rats. Thus, immunization with peptides whose sequences are based on putative functional domains of mutans streptococcal GTF are protective toward a cariogenic S. sobrinus or S. mutans infection.

Amino Acid Sequence↗

PubMed2005

Immunological and protective effects of diepitopic subunit dental caries vaccines.

As a prelude to development of broader-spectrum vaccines for dental caries, we explored the immune potential of constructs combining epitopes from mutans streptococcal glucosyltransferases (GTF) and glucan binding protein B (GbpB). Two diepitopic peptide constructs were synthesized in a multiple antigenic peptide (MAP) format. Both constructs contained SYI, a 20-mer GbpB peptide that included a sequence having major histocompatibility complex class II binding characteristics. One diepitopic construct (SYI-CAT) also contained a 22-mer sequence from the catalytic domain of GTF. Another diepitopic construct (SYI-GLU) contained a 22-mer sequence from the glucan binding domain of GTF. To assess the ability of each construct to induce antibody reactive with GbpB and GTF native proteins, rats were injected subcutaneously with SYI-CAT, SYI-GLU, or the constituent monoepitopic constructs. Only the SYI-CAT construct induced significant levels of serum immunoglobulin G (IgG) and IgA antibody to both pathogenesis-associated proteins. Also, immunization with SYI-CAT significantly (P < 0.001) enhanced the antibody response to the CAT peptide. Experiments then compared experimental dental caries after immunization with SYI-CAT, SYI, or CAT MAP constructs, followed by infection with Streptococcus mutans strain SJr. Dental caries were lower in each peptide-immunized group than in the sham-injected group. The level of protection after SYI-CAT immunization was similar to that after immunization with constituent MAP constructs. In another experiment, rats were infected with Streptococcus sobrinus strain 6715 under an identical protocol. Significant protection was observed on buccal surfaces in both SYI-CAT and CAT construct-immunized, but not in the SYI construct-immunized, groups. Thus, addition of the GbpB-derived SYI peptide to the GTF-derived CAT peptide construct not only enhanced the immunological response to CAT and GTF epitopes, but also extended the protective effect of the construct to include both S. mutans and S. sobrinus.

Animals↗

PubMed2000

Shifts in membrane fatty acid profiles associated with acid adaptation of Streptococcus mutans.

Cells of Streptococcus mutans UA159 physiologically adapted to acidification during growth at pH 5 in glucose-limited chemostat cultures were enriched in mono-unsaturated and longer chain fatty acids compared with unadapted cells grown under the same conditions but at pH 7. Ratios of unsaturated to saturated fatty acids in the cells were, respectively, 1.2 and 0.3. Cyclopropane fatty acids were not detected. Streptococcus sobrinus 6715, which is known to have minimal acid-adaptive capacity, showed only minimal change in membrane fatty acids.

Adaptation, Physiological↗

PubMed1988

Influence of desalivation in rats on incidence of caries in intact cagemates.

The evidence that dental caries is an infectious and transmitted disease in rodents is unequivocal. However, the factors controlling the transmission of micro-organisms from one animal to another have not been extensively explored. Results from previous studies in our laboratory showed that desalivated animals became infected by Streptococcus sobrinus in a shorter period of time than did intact animals. Furthermore, an additional study in our laboratory showed that animals with intact salivary function caged with desalivated animals harbored more S. sobrinus immediately following establishment of infection than did intact animals housed with other intact animals. Therefore, it seemed appropriate to determine the influence on caries development of caging a desalivated animal with an intact animal. In this study, intact Sprague-Dawley rats were caged with desalivated animals; additional groups of intact animals were housed with chlorhexidine-treated animals that were either intact or desalivated. Although chlorhexidine suppressed both caries development and the level of infection by S. sobrinus, nevertheless, intact animals caged with desalivated animals invariably developed more caries than did intact animals housed with other intact animals. Treating intact animals with chlorhexidine did not affect caries scores in untreated intact cagemates. Overall, the results suggest that a highly acidogenic flora with enhanced virulence (including S. sobrinus) is selected in the desalivated animals; this flora is apparently readily transmitted to intact cagemates, leading to enhanced levels of smooth-surface caries.

Animals↗

PubMed2006

Protective efficacy of a targeted anti-caries DNA plasmid against cariogenic bacteria infections.

We have previously reported that a targeted anti-caries DNA plasmid pGJA-P/VAX which was constructed against the antigenic determinants of Streptococcus mutans (S. mutans) successfully induced antibody responses in mice and monkeys. The present study explored the protective efficacy of pGJA-P/VAX against cariogenic bacterial challenge. Groups of rats were orally challenged with S. mutans or Streptococcus sobrinus (S. sobrinus) and then immunized with pGJA-P/VAX or the vector pVAX1 intranasally. Serum IgG and salivary IgA antibody levels were assessed by an enzyme-linked immunosorbent assay and caries activity was evaluated by the Keyes method. The results showed that specific salivary IgA antibody responses were induced following intranasal vaccination with pGJA-P/VAX. Moreover, immunization with pGJA-P/VAX resulted in significantly reduced enamel and dentinal caries lesions in rats after S. mutans infection and significantly reduced enamel caries lesions after S. sobrinus infection. Thus, pGJA-P/VAX was not only protective toward S. mutans infection, but also provided cross-strain protection against S. sobrinus infection in rats.

Administration, Intranasal↗

PubMed1995

Sequence analysis of the Streptococcus mutans Ingbritt dexA gene encoding extracellular dextranase.

The complete nucleotide sequence (3,747 bp) of the dextranase gene (dexA) and flanking regions of the chromosome of Streptococcus mutans Ingbritt (serotype c) were determined. The open reading frame for dexA was 2,550 bp, ending with a stop codon TGA. A putative ribosome-binding site, promoter preceding the start codon, and potential stem-loop structure were identified. The presumed dextranase protein (DexA) consisting of 850 amino acids was estimated to have a molecular size of 94,536 Da and a pI of 4.79. The nucleotide sequence and the deduced amino acid sequences of S. mutans dexA exhibited homologies of 57.8% and 47.0%, respectively, to those of Streptococcus sobrinus dex. The homologous region of dex of S. sobrinus was in the N-terminal half. The C terminus of DexA consisted of a hexapeptide LPQTGD, followed by 7 charged amino acids, 21 amino acids with a strongly hydrophobic character, and a charged hexapeptide tail, which have been reported as a common structure of C termini of not only the surface-associated proteins of Gram-positive cocci but also the extracellular enzymes such as beta-fructosidase of S. mutans and dextranase of S. sobrinus. The DexA protein had no significant homology with the glucosyltransferases, the glucan-binding protein, or the dextranase inhibitor of mutans streptococci.

Amino Acid Sequence↗

PubMed1990

Interaction of structural isomers of sucrose in the reaction between sucrose and glucosyltransferases from mutans streptococci.

Structural isomers of sucrose, i.e. disaccharides composed of glucose and fructose molecules with different glucosidic linkages, were examined for their effect on the reaction between sucrose and various glucosyltransferases (GTases) from Streptococcus mutans MT8148 and Streptococcus sobrinus 6715. Trehalulose (alpha 1-1), turanose (alpha 1-3), maltulose (alpha 1-4), and palatinose (alpha 1-6) were used as the sucrose analogues. Mutans streptococci were found not to utilize these sucrose analogues. Analysis of enzymatic products of GTase and sucrose with thin layer chromatography clearly revealed that glucan synthesis from [14C]sucrose by the various purified GTase preparations from S. mutans and S. sobrinus was inhibited in the presence of these sucrose analogues except turanose, resulting in the release of increased amounts of [14C]fructose and [14C]oligosaccharides. It was also found that the fructose residues in the oligosaccharides were derived from those of sucrose analogues but not sucrose itself. The Lineweaver-Burk plots of the substrate saturation kinetics of GTase vs sucrose indicated increased Km and Vmax in the presence of sucrose analogue, as compared with sucrose alone. Finally, these sucrose analogues except turanose inhibited sucrose dependent cellular adherence of S. sobrinus 6715 to a glass surface, while they scarcely inhibited the adherence of S. mutans MT8148. Among the analogues, maltulose appeared the most effective inhibitor against GTases in general.

Chromatography, Thin Layer↗

PubMed1990

Enumeration of mutans streptococci in clinical samples by using monoclonal antibodies.

Mutans streptococci have been strongly associated with dental caries. Two members of this group of bacteria, Streptococcus mutans and Streptococcus sobrinus, are often found in human dental plaque. Identification of mutans streptococci on the basis of sugar fermentation is troublesome and easily leads to erroneous conclusions. Furthermore, the recovery on selective media differs for different species. This causes incorrect enumeration of S. mutans and S. sobrinus in clinical samples. The aim of this study was to develop a method for simultaneous identification and enumeration of S. mutans and S. sobrinus in dental plaque and saliva samples. With this immunoblot technique (IBT), significantly more plaque samples containing S. sobrinus were detected than on the selective medium Trypticase-yeast-cysteine-sucrose-bacitracin agar (TYCSB) (P less than 0.01). The numbers of plaque samples harboring S. mutans were equal on TYCSB and by IBT. However, the numbers of CFU of S.mutans as well as of S. sobrinus detected with the IBT were significantly higher than those obtained on TYCSB (P less than 0.001). The recovery of primary isolations of S. sobrinus on TYCSB seems to have been inhibited in 26 of the 45 S. sobrinus-containing plaque samples. False-positive or false-negative reactions with the IBT were not found.

Animals↗

PubMed1997

Tonsillar application of killed Streptococcus mutans induces specific antibodies in rabbit saliva and blood plasma without inducing a cross-reacting antibody to human cardiac muscle.

When Streptococcus mutans cells are injected into the skeletal muscle of rabbits, an antibody against human cardiac muscle, as well as an anti-S. mutans antibody, is induced in blood plasma. Our previous study showed that when sheep erythrocytes are applied to palatine tonsils, an antibody against the applied cells is induced both in blood plasma and saliva. This antibody has no activity against cardiac muscle. It is not clear, however, if S. mutans application to the tonsils evokes an antibody response against cardiac muscle. In this study, we immunized rabbits against S. mutans or Streptococcus sobrinus by tonsillar application or by intramuscular injection every 3 days for 6 weeks. Tonsillar applications of formalin-killed cells of S. mutans induced saliva immunoglobulin A (IgA) and blood plasma IgG to the applied cells. In contrast, intramuscular injection of such cells induced only blood plasma IgG. When the route of immunization was intramuscular injection, antibodies in blood plasma cross-reacted with cardiac muscle. By enzyme-immunohistochemistry and Ouchterlony immunodiffusion tests, no cross-reaction to cardiac muscle was observed with the antibody in saliva or in blood plasma after the tonsillar applications. Western blotting of the S. mutans antigen showed that blood plasma from rabbits injected with S. mutans reacted with antigens of 46, 52, 62, and 85 kDa, while that from rabbits subjected to tonsillar application of S. mutans did not react with these bands. Similar results were obtained for S. sobrinus applications. Thus, tonsillar applications of mutants group streptococci induce antibodies differing in antigen specificity and do not induce any cross-reacting antibody to cardiac muscle.

Animals↗

PubMed1990

Analysis of the Streptococcus downei gtfS gene, which specifies a glucosyltransferase that synthesizes soluble glucans.

The complete nucleotide sequence was determined for the Streptococcus downei (previously Streptococcus sobrinus) MFe28 gtfS gene which specifies a glucosyltransferase (GTF-S) producing water-soluble glucan. A single open reading frame which encodes a mature protein with a molecular weight of 147,408 (1,328 amino acids) and a putative signal peptide 36 or 37 amino acids in length was detected. GTF-S shares extensive sequence similarity with GTF-I (gtfI) from S. downei and GTF-I (gtfB) and GTF-SI (gtfC) from Streptococcus mutans. GTF-S contains a highly conserved enzymatic domain and C-terminal repeated sequences which appear to be involved in glucan binding. Comparison of the deduced GTF-S protein sequence with other sequenced GTF genes of mutans streptococci revealed that these C-terminal repeats occurred in all cases, although the patterns of repeated sequences varied with respect to each other and to the glucan-binding protein of S. mutans. GTF-S contains four C-terminal repeat sequences ranging from 49 to 51 amino acids in length and a partial repeat of 13 amino acids. Nuclear magnetic resonance analysis of the glucan produced by GTF-S revealed that the product consisted of more than 90% alpha-1,6-linked glucosyl residues.

Amino Acid Sequence↗

PubMed1986

Comparison of extracellular protein profiles of seven serotypes of mutans streptococci grown under controlled conditions.

Extracellular proteins produced by the four human commensal species of mutans streptococci were analysed. The organisms used were Streptococcus mutans, serotypes c, e and f, Streptococcus cricetus, serotype a, Streptococcus rattus, serotype b, and Streptococcus sobrinus, serotypes d and g. They were grown in continuous culture at different generation times and pH values in media containing either glucose or fructose to determine the extent of variation in extracellular protein production that could occur for an individual strain. The results for different organisms grown under the same conditions were then compared. The total amount of protein of molecular mass greater than or equal to 60 kDa varied considerably with the growth conditions and with the strain. Generally more protein was present at a higher pH, conditions under which the organisms also form more lipoteichoic acid. With respect to individual protein components SDS-PAGE proved better than isoelectric focusing for detecting phenotypic responses by a particular strain to environmental changes and differences between the different strains. Differences in the molecular masses of protein components were particularly pronounced in the regions designated P1 (185-200 kDa), P2 (130-155 kDa) and P3 (60-95 kDa). Every strain produced at least one component in the P1 region that cross-reacted with antiserum to the purified protein from S. mutans serotype c, a protein which is indistinguishable from antigens B and I/II. Two components in the P2 region were dominant in the case of S. cricetus and S. sobrinus strains and showed glucosyltransferase (GTF) activity. GTF activity was also detected in the P3 region, particularly with S. mutans strains.

Bacterial Proteins↗

PubMed2001

[A study on transmission of pathogenic bacteria of rampant caries from mothers to children].

OBJECTIVE: In order to prevent rampant caries in children, the transmission from mothers to children of pathogenic bacteria of rampant caries will be investigated in this study. METHODS: By using fingerprint technique, the genetic diversities of Streptococcus mutans(S. mutans) were examined respectively in 10 children with rampant caries, 10 children without rampant caries S. mutans, 10 2-year-old caries-free children, and their mothers. The levels of S. mutans in saliva of mothers were also examined. For fingerprinting, chromosomal DNA of isolates obtained from plaques of these children and from saliva of their mothers were digested with restriction endonuclease HindIII and examined by electrophoresis on 0.7% agarose gel. DNA fingerprints were obtained and analyzed for genotypic similarities. RESULTS: The DNA fingerprint patterns showed that the proportion of children whose genotypes of S. mutans matched their mothers in the children with rampant caries was 70%, which is similar to that in the children without rampant caries and the caries-free children (60% respectively). The number of distinct genotypes of S. mutans harbored in children with rampant caries was, on average, greater than the number of genotypes present in children without rampant caries and caries-free children (1.7, 1.2 and 1.1 respectively, P < 0.05). Mothers of children with rampant caries had similar levels of S. mutans in saliva as those mothers of children without rampant caries and caries-free children. However, mothers of children with rampant caries had significantly higher DMFT scores and higher levels of Streptococcus sobrinus (S. sobrinus) in saliva than the mothers of caries-free children did. CONCLUSION: In all child groups, mothers were probably the main source of infection with S. mutans. Rampant caries in children is associated with DMFT scores and levels of S. sobrinus in saliva of mothers. In the initiation of rampant caries experienced by a child, the transmission of pathogenic bacteria from mothers to children may be the main source.

Adult↗

PubMed1990

Antiplaque activity of some antimicrobial agents using a simple in vitro method.

Some antimicrobial compounds were tested for their antiplaque activity by a simple method involving measurement of the weight of Streptococcus sobrinus plaque on a glass surface. Chlorhexidine, cetylpyridinium chloride, and n-tetradecylamine reduced the weight of plaque produced by S. sobrinus in vitro; some N-palmityl and palmitoyl derivatives of polymethylenediamines were also found to possess antiplaque activity. The results suggest that an antiplaque effect does not necessarily depend on high bactericidal activity.

Amines↗

PubMed1989

DNA homology of surface protein antigen A gene in mutans streptococci.

1. A recombinant plasmid, pYA724, containing an 8.45 kb DNA fragment encoding surface protein antigen A (spaA) from Streptococcus sobrinus 6715 was used to examine the DNA homology of the spaA gene with chromosomal DNA of various mutans streptococci strains. 2. Restriction endonuclease BamHI-digested pYA724 DNA was radio-labeled by nick-translation, and a DNA-DNA hybridization experiment was carried out. pYA724 DNA hybridized with chromosomal DNA of serotypes a, c, d, e, f and g strains, but not with b by dot DNA-hybridization and Southern blot DNA hybridization. 3. Chromosomal DNAs were isolated from several serotype c Streptococcus mutans strains, digested with BamHI, and analyzed by Southern blot DNA hybridization. pYA724 DNA hybridized with different sizes and numbers of BamHI-digested DNA fragments of the chromosomal DNAs. 4. These data indicated that all mutans streptococci strains except serotype b have DNA homologous with the spaA gene, although within the same serotype strain the spaA gene has a diversity of arrangement within the chromosome.

Antigens, Bacterial↗

PubMed1988

The in vitro dental plaque inhibitory properties of a series of N-[1-alkyl-4(1H)-pyridinylidene]alkylamines.

A series of novel N-[1-alkyl-4(1H)-pyridinylidene]alkylamine hydrohalides has been prepared and evaluated as inhibitors of dental plaque formation, in vitro. Several members of the series exhibited potency ca. 9-fold greater than that of chlorhexidine vs Streptococcus sobrinus 6715-13. The di-n-octyl analogue, 11 (pirtenidine), was found to be highly efficacious against several other oral plaque-forming microorganisms and is presently undergoing preclinical evaluation.

Actinomyces↗

PubMed1993

Comparison of aminopeptidase activities in four strains of mutans group oral streptococci.

In this study, native cells of Streptococcus mutans VA-29R and Streptococcus rattus FA-1 displayed significantly higher aminopeptidase activity than did cells of Streptococcus cricetus AHT or Streptococcus sobrinus 6715 toward the nitroanilide derivatives of leucine, alanine, methionine, arginine, and lysine. These differences in cellular aminopeptidase activity led us to investigate the subcellular localization of the aminopeptidase in these mutans group streptococci. Following conversion of native cells to protoplasts by treatment with lysozyme, most of the aminopeptidase activity detected in the native-cell preparations remained associated with the intact protoplasts. After lysis of protoplasts and differential centrifugation, most of the total cellular aminopeptidase activity was recovered with the cytoplasmic fraction. Membrane-associated aminopeptidases represented only minor activities in these mutans group streptococci. Although the four strains showed no differences with respect to a predominant cytoplasmic localization for the aminopeptidase activities, the levels of activity in the cytoplasmic fractions from S. cricetus AHT and S. sobrinus 6715 were significantly lower than those measurable in the corresponding fractions from S. mutans VA-29R and S. rattus FA-1. These results support the conclusion that the differences in aminopeptidase activity expressed by these streptococci reflect quantitative differences rather than differences in enzyme subcellular localization.

Amino Acids↗

PubMed1989

Comparative cariogenicity and dental plaque-forming ability in gnotobiotic rats of four species of mutans streptococci.

The four species, each represented by two strains, all produced high levels of fissure caries in the upper and lower jaws of gnotobiotic Fisher rats. Streptococcus rattus strains and Streptococcus mutans NCTC 10832 gave low levels of approximal caries, whereas Streptococcus cricetus, Streptococcus sobrinus and Strep. mutans NCTC 10449 gave high levels. The only strains to produce buccal surface lesions were Strep. sobrinus and Strep. cricetus. All strains were able to form dense plaque in the central fissure of the second molar. Strep. cricetus, Strep. rattus and Strep. sobrinus strains were capable of producing smooth-surface plaque. This difference in plaque-forming ability did not correlate precisely with differences in cariogenicity, and such differences occurred between strains of the same species.

Animals↗

PubMed1999

Simultaneous induction of specific immunoglobulin A--producing cells in major and minor salivary glands after tonsillar application of antigen in rabbits.

The immunoglobulin A (IgA)-producing cells in the stroma of major salivary glands are induced by antigenic stimulation of the mucosal immune system. Whether such cells also are induced in minor salivary glands by this stimulation remains to be determined. After application of sheep red blood cells to the palatine tonsils every 3 days for 6 weeks, anti-sheep red blood cell IgA was detected in saliva both by agglutination tests and by enzyme-linked immunosorbent assay. Using enzyme-linked immunospot assay, an increase in the number of anti-sheep red blood cell IgA-producing cells was found in minor as well as in major salivary glands of the sixth week of application; such cells constituted 4.9% to 5.9% of the total number of IgA-producing cells in these tissues. Tonsillar application of whole cells of formalin-killed Streptococcus sobrinus induced anti-S. sobrinus IgA in saliva. The number of anti-S. sobrinus IgA-producing cells in the above glands simultaneously increased over 6 weeks, and reached 5.2-5.6% of the total number of IgA-producing cells.

Animals↗