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PubMed1980

Cross-reactivity of Streptococcus mutans antigens and human heart tissue.

Rocket and two-dimensional immunoelectrophoreses were used to demonstrate that antisera from rabbits immunized with Streptococcus mutans strain B13 cross-reacted with human heart tissue. Absorption of the anti-S. mutans serum with S. mutans whole cells removed all reactivity to heart tissue, but did not remove the reactivity of an added antibody marker to its corresponding antigen. The anti-S. mutans serum reacted most intensely with heart tissue antigen and to a lesser degree with skeletal muscle, but not with liver or kidney tissues. These results support the conclusion that antigens of S. mutans cross-react with mammalian heart tissue and, further, suggest that caution should be exercised in the formulation of a dental caries vaccine containing S. mutans antigens.

Antigens, Bacterial↗

PubMed1981

Antibody responses of monkeys to oral and local immunization with Streptococcus mutans.

Monkeys were immunized with Streptococcus mutans by a number of routes in an attempt to elicit exclusively a secretory immunoglobulin A (IgA) response. Antibody responses were detected by a sensitive radioimmunoassay. Monkeys primed subcutaneously and boosted submucosally with formolized cells of S. mutans had high serum IgG, IgA, and IgM radioimmunoassay titers and only slight salivary IgG titers. Instillation of killed cells of S. mutans into the right parotid salivary duct elicited good IgG, IgA, and IgM responses in both the right parotid saliva and serum, but only a weak IgM response was detected in the left parotid saliva. Administration of killed cells of S. mutans in enterically coated capsules did not elicit a detectable antibody response or have a discernible effect on the antibody response to subsequent immunization by instillation. No increase in antibody titer was detected in the serum or whole saliva from monkeys orally immunized with enterically coated capsules containing viable S. mutans or in the serum, whole saliva, or intestinal contents from monkeys immunized with uncoated capsules containing killed cells of the same organism. These results do not support the concept that oral immunization with S. mutans is effective in stimulating a generalized secretory IgA response in primates.

Administration, Oral↗

PubMed1981

Influence of growth medium on adsorption of Streptococcus mutans, Actinomyces viscosus, and Actinomyces naeslundii to saliva-treated hydroxyapatite surfaces.

The influence of the growth medium on the ability of strains of Streptococcus mutans, Actinomyces viscosus and A. naeslundii to attach to saliva-treated hydroxyapatite (S-HA) surfaces was studied. Preliminary experiments indicated that cells of each species harvested in lag, log, and early stationary phases of growth adsorbed comparably to S-HA; thus, early stationary phase cells were used in all subsequent assays. Strains were grown in chemically defined medium (CDM), in CDM supplemented with gastric mucin or with filter-sterilized or (60)Co-irradiated saliva from human donors of blood types A, B, or O, and in Trypticase soy broth (BBL Microbiology Systems) and Todd-Hewitt broth. Adherence of S. mutans H12 to S-HA tended to vary when the streptococci were grown in saliva-supplemented CDM, but the number of cells which attached was generally within twofold of that of CDM-grown cells. Attachment of A. viscosus S2 and LY7 and of A. naeslundii S4 and L13 was generally similar when grown in CDM or in CDM supplemented with saliva, but it tended to increase for organisms grown in CDM supplemented with gastric mucin. None of the strains studied appeared to destroy the blood group reactivity of the added salivary components, and they attached equally well to HA treated with homologous or heterogous saliva from that present in the medium in which they were grown. The A. viscosus strains adsorbed in 25 to 40% higher numbers to HA treated with blood type B saliva than with type A saliva, irrespective of the medium used for growth. S. mutans H12 cells displayed alpha- and beta-glucosidase and alpha-galactosidase activity; the Actinomyces strains exhibited these activities plus beta-galactosidase when grown in all media. However, the levels of these glycoside hydrolases did not correlate with cell adsorption to S-HA. The apparent weak influence of the growth medium on attachment of S. mutans was studied further. Strains of S. mutans isolated from the saliva of five human donors were made resistant to streptomycin, grown in CDM, and then added to new saliva samples from the respective donors from which they were obtained. The in vitro-grown cells were found to attach to S-HA comparably to S. mutans cells present naturally in the saliva.

ABO Blood-Group System↗

PubMed1982

Effect of neonatal thymectomy on immune responses of rats to Streptococcus mutans.

The effect of neonatal thymectomy on secretory and systemic antibody responses in rats was studied. Groups of normal or thymectomized (Tx) rats were infected or immunized and infected with Streptococcus mutans 6715. Tx rats exhibited a significantly lower level of salivary immunoglobulin A (IgA) antibody to S. mutans after a 45- to 65-day infection. Similarly, after multiple local injections of formalinized S. mutans, Tx rats showed a delay in the appearance and lower levels of salivary IgA antibody to S. mutans. Serum IgG antibody levels were also decreased in Tx rats with both experimental protocols. In contrast, salivary IgG and serum IgM anti-S. mutans activity in Tx and normal rats were similar during the experiments. These results demonstrated that thymus deprivation at birth produces profound effects on the ability of rats to manifest secretory IgA antibody responses to the pathogenic microorganism S. mutans.

Animals↗

PubMed1983

Correlation of level and duration of Streptococcus mutans infection with incidence of dental caries.

The caries incidence at various levels of Streptococcus mutans infection was analyzed in a control group and a test group. In the control group, the incidence of caries and the duration of S. mutans infection were significantly correlated. In the test group, the S. mutans infection was suppressed by antimicrobial measures when the number of S. mutans exceeded 250 X 10(3) CFU per ml of saliva. The results illustrate that the level and duration of the S. mutans infection are strongly correlated to the incidence of caries. The findings support the concept of S. mutans as a key cariogenic microorganism and illustrate the value of antimicrobial treatment in the prevention of caries.

Adolescent↗

PubMed1983

Prevalence, distribution of serotypes, and cariogenic potential in hamsters of mutans streptococci from elderly individuals.

The prevalence of mutans streptococci (Streptococcus mutans, Streptococcus cricetus, Streptococcus sobrinus, and Streptococcus rattus) was determined in the salivas of 169 elderly individuals ranging in age from 60 to 87 years. Approximately 40% of these individuals were edentulous and wore full upper and lower dentures. With the exception of a higher proportion of saliva counts below 1,000 CFU/ml in the full-denture wearers, the prevalence and the serotype and species distributions of the mutans streptococci were similar in the denture wearers and individuals with natural teeth only. The species and serotype distributions of mutans streptococci in this elderly population were also consistent with reported observations of other workers on younger, more caries-prone populations. A total of 87 representative isolates of the mutans streptococci were tested for cariogenic potential in a hamster model system. A considerable degree of variation in virulence between different strains was observed. However, these differences were not relatable to individual species or serotypes or to whether the organisms were isolated from denture wearers or naturally dentate subjects. The results of our studies indicate that elderly individuals with either natural or artificial dentitions may be a hitherto unrecognized reservoir of mutans streptococci having varying degrees of potential cariogenicity. Hence, in close family situations they could serve, along with parents and siblings, as vectors in the initial transmission of cariogenic microorganisms to young children.

Aged↗

PubMed1985

Competitive displacement of mutans streptococci and inhibition of tooth decay by Streptococcus salivarius TOVE-R.

The ability of Streptococcus salivarius TOVE-R to displace virulent representatives of the most prevalent human mutans streptococci from the teeth of rats, and thereby to inhibit caries, was studied. Streptococcus mutans 10449S- or Streptococcus sobrinus 6715-13WT-infected specific-pathogen-free rats consuming a high-sucrose diet were inoculated by TOVE-R. The infectants were differentially recovered from swabs of the teeth over the time course of infection and from sonically treated material of extracted teeth and excised tongues. Despite initial colonization of the teeth by the mutans streptococci, TOVE-R colonized the teeth, unlike other essentially nonvirulent plaque formers already described. It did not colonize the tongues of the rats. TOVE-R emerged and persisted as a prominent member of the plaque ecology. There was an associated decline in the mutans streptococci on the teeth, and this decline was associated with significant inhibition of the caries component attributable to 10449S infection (56%) and to 6715-13WT infection (52%). TOVE-R did not reliably inhibit the component of fissure caries attributable to the nonmutans indigenous flora of the rats. TOVE-R itself induced no detectable decay. The data suggest the potential therapeutic utility of TOVE-R to inhibit caries by displacement of mutans streptococci from the teeth. These results supplement the already reported ability of TOVE-R to preempt initial colonization of teeth by the mutans streptococci.

Animals↗

PubMed1985

Antibody specificity and antigen characterization of rat monoclonal antibodies against Streptococcus mutans cell wall-associated protein antigens.

Monoclonal antibodies to Streptococcus mutans OMZ175 (serotype f) cell wall-associated antigens (wall-extracted antigens [WEA]) were derived from the fusion of Lou C plasmocytoma rat cells (IR 983 F) and spleen cells from Wistar R inbred rats immunized with WEA. Four cell lines producing monoclonal antibodies directed against a component of S. mutans WEA have been established. All four monoclonal antibodies reacted only with two antigens of WEA from S. mutans OMZ175 by Western blotting and immunoprecipitation techniques, enzyme-linked immunosorbent assay (ELISA), and competitive ELISA. Western blot analysis of WEA showed that the four monoclonal antibodies recognized two related cell wall-associated proteins with apparent molecular weights of 125,000 and 76,000. Immunoprecipitation of whole cells with the monoclonal antibodies confirmed the surface localization of the two antigens. The ELISA and competitive ELISA were used to analyze the distribution of the epitopes on seven S. mutans serotypes. All S. mutans serotypes were found to express the recognized epitopes; however, different reactivity patterns could be distinguished among the various strains tested, and the four monoclonal antibodies reacted only weakly with S. mutans serotypes d and g.

Animals↗

PubMed1986

Salivary immunoglobulin A and serum antibodies to Streptococcus mutans ribosomal preparations in dental caries-free and caries-susceptible human subjects.

Caries-free subjects or individuals with low caries susceptibility exhibited significantly higher (P less than 0.001) levels of naturally occurring salivary immunoglobulin A (IgA) and serum IgG, IgA, and IgM antibodies to a Streptococcus mutans ribosomal preparation than subjects with high caries susceptibility. Absorption of saliva and serum samples with S. mutans ribosomal preparations, but not with other S. mutans antigens or with Escherichia coli and Neisseria gonorrhoeae ribosomal preparations, removed the antibody activity. Absorption with Streptococcus sanguis ribosomes and NH4Cl-washed S. mutans ribosomes partially removed the anti-S. mutans ribosome antibody activity. These results provide evidence that naturally occurring salivary and serum antibodies to the S. mutans ribosomal preparation correlate with susceptibility to dental caries.

Antibodies, Bacterial↗

PubMed1987

Isolation and characterization of monoclonal antibodies specific for antigen P1, a major surface protein of mutans streptococci.

A panel of 15 murine monoclonal antibodies (MAbs; 14 immunoglobulin G1, 1 immunoglobulin G2a) directed against antigen P1, a major surface protein of mutans streptococci, was prepared. All of these MAbs reacted by the enzyme-linked immunosorbent assay with solubilized wall material from Streptococcus mutans Ingbritt 175 (a serotype c strain which retains significant amounts of P1 in its cell wall), culture supernatant fluid from Ingbritt 162 (a strain which excretes large amounts of P1 into the culture medium), and purified P1. By Western immunoblotting, these MAbs were observed to react with a high-molecular-weight polypeptide which comigrated with antigen P1. None of these MAbs cross-reacted with human heart tissue or with various eucaryotic proteins. When whole cells of various strains of mutans streptococci were screened against the panel of MAbs, the strongest reactivities were noted with strains of serotype c and e S. mutans, while a serotype f strain of S. mutans, along with S. sobrinus and S. cricetus strains, reacted somewhat more weakly. S. rattus strains were completely negative. Results obtained with bacterial culture supernatants were qualitatively similar. The surface localization of antigen P1 was confirmed by electron microscopy with an indirect immunogold technique. In sectioned S. mutans cells, labeling appeared to be associated with a fibrillar "fuzzy coat" layer, which was far more prominent on cells of Ingbritt 175 than on those of Ingbritt 162.

Animals↗

PubMed1990

Regulation of expression of Streptococcus mutans genes important to virulence.

Studies were initiated to investigate the regulation of Streptococcus mutans genes which are believed to be important to virulence. Operon fusions were constructed between S. mutans gene regulatory regions and a promoterless chloramphenicol acetyltransferase gene (cat) found on the plasmid pMH109. Specifically, fusions were generated between cat and the S. mutans genes encoding fructosyltransferase (ftf) and the glucosyltransferase B/C (gtfB/C) operon. Constructs were confirmed by restriction enzyme analysis, and the fusions were subcloned into the integration vehicle pVA891. Following generation of multimeric DNA, recombinant plasmids were introduced into the s. mutans genome by Campbell-type insertion, resulting in single-copy operon fusions. Chloramphenicol acetyltransferase specific activities were used to monitor the expression of the S. mutans gtfB/C operon and ftf determinants. The expression of these genes is increased by the presence of sucrose and is followed by a rapid decline in expression over time. Additionally, expression of the gtfB/C operon is increased in S. mutans cells bound to artificial tooth pellicles.

Chloramphenicol O-Acetyltransferase↗

PubMed1991

Oral passive immunization against dental caries in rats by use of hen egg yolk antibodies specific for cell-associated glucosyltransferase of Streptococcus mutans.

The effect of polyclonal egg yolk immunoglobulin G antibodies (yIgG) raised against whole cells, cell-free (CF) glucosyltransferase (GTase), or cell-associated (CA) GTase of serotype c Streptococcus mutans was examined in terms of in vitro inhibition of virulence-related factors of S. mutans and protection of S. mutans-infected rats against the development of dental caries. Hens (18 weeks old) were immunized with formalin-treated whole cells, purified CF-GTase, or CA-GTase together with Freund's complete adjuvant. In addition, yIgG to surface protein antigen was used in some in vitro experiments for comparison with other antibodies. yIgG was purified by ammonium sulfate precipitation followed by DEAE-Sephacel column chromatography or fractional precipitation with ethanol. Purified yIgG was found to be a 220-kDa protein, which was dissociated into heavy and light chains upon addition of 2-mercaptoethanol. yIgG to whole cells and surface protein antigen gave a heavy aggregation of S. mutans organisms, while yIgG to CF- and CA-GTase specifically inhibited the enzymatic activity of the respective GTase. yIgG to CA-GTase and whole cells was found to clearly suppress the adherence of S. mutans cells to a glass surface. Specific-pathogen-free Sprague-Dawley rats that had been infected heavily and repeatedly with S. mutans and fed diet no. 2000 developed severe dental caries, while rats fed diet 2000 containing greater than or equal to 0.1% yIgG to CA-GTase showed a statistically significant reduction in dental plaque accumulation and caries development. Administration of yIgG to CF-GTase and whole cells failed to protect against caries. These results clearly suggest that yIgG to S. mutants CA-GTase specifically inhibited a virulence factor of this organism, i.e., insoluble glucan-synthesizing CA-GTase, resulting in a significant reduction in the development of dental caries.

Administration, Oral↗

PubMed1991

Effects of anaerobiosis and aerobiosis on interactions of human polymorphonuclear leukocytes with the dental plaque bacteria Streptococcus mutans, Capnocytophaga ochracea, and Bacteroides gingivalis.

Human polymorphonuclear leukocytes (PMN) were able to generate and release superoxide anions upon stimulation of Streptococcus mutans, Bacteroides gingivalis, and Capnocytophaga ochracea when incubated aerobically but not when incubated anaerobically. Lysozyme release and phagocytosis by PMN were independent of oxygen, and no difference between PMN incubated aerobically or anaerobically was observed (PMN stimulated by B. gingivalis released 7.6% total lysozyme when aerobic and 6.9% when anaerobic). There were variations in lysozyme release and phagocytosis for the three organisms, particularly for phagocytosis. B. gingivalis and C. ochracea yielded lower phagocytosis values than those for S. mutans, e.g., at 1 h 67% of the initial inoculum of S. mutans was phagocytosed (versus only 40% for B. gingivalis). Transmission electron microscopy showed that both S. mutans and B. gingivalis were internalized into classical phagolysosomes. In contrast, C. ochracea showed two forms of internalization; C. ochracea either formed a classical phagolysosome or was tightly bound in the cytoplasm with no surrounding cell membrane. Intracellular killing of S. mutans and C. ochracea was unaffected by anaerobiosis, but killing of C. ochracea was much lower than that of S. mutans (1 x 10(7) to 2 x 10(7) bacteria killed compared with 5.1 x 10(7) bacteria killed at 6 h). In contrast, a greater number of B. gingivalis was killed in the presence of oxygen (5.3 x 10(7) bacteria were killed when aerobically incubated and 1.9 x 10(7) bacteria were killed when anaerobically incubated). These results suggest that the ability to survive anaerobically may enable some bacteria to evade PMN killing; however, abnormal phagocytosis may represent a more efficient way to evade both oxygen-dependent and -independent killing mechanisms, leading to enhanced virulence of the organism.

Aerobiosis↗

PubMed1992

Glucans synthesized in situ in experimental salivary pellicle function as specific binding sites for Streptococcus mutans.

Many researchers have suggested that the role of glucan-mediated interactions in the adherence of Streptococcus mutans is restricted to accumulation of this cariogenic bacterium following its sucrose (i.e., glucan)-independent binding to saliva-coated tooth surfaces. However, the presence of enzymatically active glucosyltransferase in salivary pellicle suggests that glucans could also promote the initial adherence of S. mutans to the teeth. In the present study, the commonly used hydroxyapatite adherence assay was modified to include the incorporation of glucosyltransferase and the synthesis of glucans in situ on saliva-coated hydroxyapatite beads. Several laboratory strains and clinical isolates of S. mutans were examined for their ability to adhere to experimental pellicles, either with or without the prior formation of glucans in situ. Results showed that most strains of S. mutans bound stereospecifically to glucans synthesized in pellicle. Inhibition studies with various polysaccharides and fungal dextranase indicated that alpha 1,6-linked glucose residues were of primary importance in the glucan binding observed. Scanning electron microscopic analysis showed direct binding of S. mutans to hydroxyapatite surface-associated polysaccharide and revealed no evidence of trapping or cell-to-cell binding. S. mutans strains also attached to host-derived structures in experimental pellicles, and the data suggest that the bacterial adhesins which recognize salivary binding sites were distinct from glucan-binding adhesins. Furthermore, glucans formed in experimental pellicles appeared to mask the host-derived components. These results support the concept that glucans synthesized in salivary pellicle can promote the selective adherence of the cariogenic streptococci which colonize human teeth.

Bacterial Adhesion↗

PubMed1992

Cloning of a locus involved in Streptococcus mutans intracellular polysaccharide accumulation and virulence testing of an intracellular polysaccharide-deficient mutant.

The streptococcal transposon Tn916 (Tcr) was used to isolate mutants of Streptococcus mutans altered in glycogen accumulation to investigate whether glycogenlike intracellular polysaccharides (IPS) play an important role in S. mutans-induced caries formation. S. mutans UA130 (serotype c) was transformed with the Escherichia coli plasmid pAM620 (Tn916), and the resultant transposon libraries were screened for glycogen content by iodine staining. A transposon mutant, designated SMS201, demonstrated a glycogen-deficient phenotype on glucose-enriched medium. Quantitative electron microscopy confirmed that IPS concentrations were significantly reduced in SMS201 relative to the wild-type progenitor strain, UA130. Importantly, reversion to wild type correlated at all times with loss of the transposon. Transposon excisants were used to facilitate cloning of the streptococcal gene(s) involved in glycogen biosynthesis and storage. A 2.1-kb chromosomal determinant (glgR) which encodes a putative regulator of S. mutans glycogen accumulation was isolated. A stable deletion mutation (delta glgR) was subsequently generated in E. coli and introduced into S. mutans by allelic exchange. The resultant glycogen synthesis-deficient mutant, SMS203, demonstrated a significantly reduced cariogenic potential (P less than 0.01) on the buccal, sulcal, and proximal surfaces of teeth in germfree rats, relative to animals challenged with the glycogen synthesis-proficient progenitor strain, UA130. These observations confirm previous reports (J. M. Tanzer, M. L. Freedman, F. N. Woodiel, R. L. Eifert, and L. A. Rinehimer, p. 597-616, in H. M. Stiles, W. J. Loesche, and T. L. O'Brien, ed., Proceedings in Microbiology. Aspects of Dental Caries. Special Supplement to Microbiology Abstracts, vol. 3, 1976) which implicate IPS as significant contributors to the S. mutans cariogenic process.

Animals↗

PubMed1996

Detachment of Streptococcus mutans biofilm cells by an endogenous enzymatic activity.

Previous studies have shown that Streptococcus mutans NG8 possesses an endogenous surface protein-releasing enzyme (SPRE) activity that liberates its own surface proteins (S. F. Lee, Infect. Immun. 60:4032-4039, 1992). The present study was initiated to investigate the possible role of the release of surface proteins by SPRE in the detachment of biofilm cells in vitro. Initially, the characteristics of surface protein release by the strain (S. mutans BM71) used in this study were shown to be the same as those previously described for S. mutans NG8. BM71 displayed characteristics identical to those of NG8 in terms of pH optima and inhibitor sensitivity for protein release. Monolayer biofilms of S. mutans BM71 were formed on hydroxylapatite rods in a modified chemostat. Detachment of the biofilm cells was measured by viable cell counts of bacteria liberated after incubation of the biofilms in buffers. Results showed that biofilm cells were detached in a pH- dependent manner with a maximum rate of pH 5 (P = 0.016) to 6 (P = 0.002), a range similar to that for optimal surface protein release. The detachment of the biofilm cells was found to be inhibited by ZnCl2 (P = 0.002 to 0.023), which also inhibited surface protein release. Detachment was not inhibited significantly by CaCl2 (P = 0.525 to 0.784), precluding an ionic effect on inhibition by ZnCl2. The extent of detachment could be increased (P = 0.046) by the addition of an SPRE preparation from S. mutans but not heat-inactivated SPRE (P = 0.665) or SPRE in the presence of ZnCl2 (P = 0.199). Detachment was also studied by using biofilms of resting (viable but not dividing) cells. Results similar to those for biofilms formed from growing cells were obtained, indicating that cells detached from biofilms were not daughter cells. The results presented above show that monolayer biofilm cells of S. mutans under conditions of minimal shear force have the ability to detach from a surface and suggest that this detachment was mediated by an endogenous SPRE activity.

Bacterial Adhesion↗

PubMed1996

Characterization of a P1-deficient strain of Streptococcus mutans that expresses the SpaA protein of Streptococcus sobrinus.

The Streptococcus sobrinus SpaA protein and the Streptococcus mutans P1 protein share 66% sequence homology at the amino acid level. To determine if the SpaA protein can be expressed in S. mutans and functionally replace the P1 protein, the spaA gene of S. sobrinus 6715 was isolated from plasmid pX1303 and inserted into the Escherichia coli-Streptococcus shuttle vector pVA838. The resulting plasmid pX1600 was transformed into the P1-deficient strain S. mutans 834 that has defects in saliva-mediated aggregation and in the ability to adhere to saliva-coated hydroxyapatite surfaces. Western blot (immunoblot) analysis of cellular protein fractions of S. mutans 834 (pX1600) detected in mutanolysin-solubilized cell walls a major protein of 210 kDa with an electrophoretic mobility similar to that of S. sobrinus SpaA protein and a minor 210-kDa protein and a major 64-kDa protein in the extracellular protein fraction. Analysis of virulence traits showed that expression of SpaA protein by S. mutans 834(pX1600) cells had restored the ability of the S. mutans 834 cells to aggregate in the presence of saliva or salivary agglutinin but not to adhere to saliva-coated hydroxyapatite. This cell aggregation was inhibited specifically by antisera to S. sobrinus SpaA protein. These results indicate that SpaA plays a role in the virulence of S. sobrinus by specifically interacting with fluid-phase salivary agglutinin to mediate cell aggregation.

Agglutinins↗

PubMed1999

Functional and immunogenic characterization of two cloned regions of Streptococcus mutans glucosyltransferase I.

Glucosyltransferase (GTF) enzymes of mutans streptococci are considered virulence factors due to their ability to synthesize adhesive glucans, which facilitate cell-to-cell adherence and accumulation. In this study we report the cloning, expression, and characterization of the catalytic (CAT) and glucan-binding (GLU) domains of S. mutans GTF-I encoded by gtfB. The CAT and GLU polypeptides represent amino acid residues 253 to 628 and 1183 to 1473, respectively, of S. mutans GTF-I. Antibodies to recombinant CAT and GLU were generated in rabbits and purified by affinity chromatography. Purified anti-CAT antibodies significantly inhibited water-insoluble glucan synthesis by S. mutans and S. sobrinus GTFs (P < 0.0001 and P < 0.05, respectively). The purified anti-GLU antibodies significantly inhibited both water-insoluble and water-soluble glucan synthesis by S. mutans GTFs (P < 0.0001 and P < 0.05, respectively). These results demonstrate that anti-CAT and anti-GLU antibodies are capable of inhibiting a variety of GTF activities. Since antibodies to S. mutans in saliva are implicated in protection against disease, we next assessed the ability of CAT and GLU polypeptides to induce mucosal antibody responses in mice. Intranasal (i.n.) immunization of mice with CAT showed significantly (P < 0.005) elevated levels of specific immunoglobulin G (IgG) antibody activity in serum and specific IgA antibody activity in serum, saliva, vaginal washes, and fecal samples. GLU immunized animals showed significantly (P < 0.005) elevated levels of specific IgA antibody activity in serum and vaginal secretions. Taken together, these results demonstrate that the recombinant CAT and GLU polypeptides are effective in inducing both mucosal and systemic immune responses. The ability of these polypeptides to induce a mucosal IgA immune response in mice after i.n. immunization supports their use as subunit vaccine candidates in the development of an anticaries vaccine.

Animals↗