Disease relevance of Streptococcus mutans

• A number of PTS components, including HPr, Enzyme I and some Enzymes II, have been studied at the biochemical and/or genetical level in Streptococcus salivarius, Streptococcus mutans and Streptococcus sobrinus [1].
• The gtfB gene coding for glucosyltransferase-I (GTF-I) activity previously isolated from Streptococcus mutans GS-5 was insertionally inactivated with the newly constructed transposon MudE in an Escherichia coli background [2].
• Sucrose-derived exopolysaccharides of Streptococcus mutans V403 contribute to infectivity in endocarditis [3].
• Streptococcus mutans Ingbritt grown under standardized conditions adhered less effectively to saliva-coated hydroxyapatite beads than did Streptococcus sanguis G9B, and there was competition for binding [4].
• However, potentially odontopathic Streptococcus mutans and Lactobacillus were isolated three to four times more frequently from plaque samples of control subjects than from plaque samples of subjects with hereditary fructose intolerance [5].

High impact information on Streptococcus mutans

• In this study, using protein I/II from Streptococcus mutans as a model activator of FAK, we investigated the potential link between FAK and TLR pathways [6].
• Thermal destabilization of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans upon phosphate binding in the active site [7].
• Peptide mapping of a novel discontinuous epitope of the major surface adhesin from Streptococcus mutans [8].
• Salivary agglutinin/DMBT1 is known for its Streptococcus mutans agglutinating properties [9].
• These proteins are implicated in bacterial adherence to various oral tissues, and we showed recently that the SR protein, an I/II Ag-related protein, from Streptococcus mutans OMZ 175 serogroup f possesses Ag mimicry with human IgG [10].

Chemical compound and disease context of Streptococcus mutans

• Water insoluble, sticky glucan was synthesized by reacting glucosyltransferase obtained from the sulture filtrate of cariogenic Streptococcus mutans OMZ 176 on sucrose [11].
• Studies on the antibacterial activity of dodecylglycerol. Its limited metabolism and inhibition of glycerolipid and lipoteichoic acid biosynthesis in Streptococcus mutans BHT [12].
• Growth-inhibitory concentrations of racemic sn-1(3)-dodecylglycerol inhibit the incorporation of [14C] glycerol into lipids and lipoteichoic acid of Streptococcus mutans BHT and alter the per cent composition of the glycerolipids [12].
• Catalysis by the NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Streptococcus mutans, a member of the aldehyde dehydrogenase (ALDH) family, relies on a local conformational reorganization of the active site [7].
• In order to address the molecular basis of the specificity of aldehyde dehydrogenase for aldehyde substrates, enzymatic characterization of the glyceraldehyde 3-phosphate (G3P) binding site of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Streptococcus mutans has been undertaken [13].

Biological context of Streptococcus mutans

• Streptococcus mutans GS-5 was transformed to erythromycin resistance with streptococcal plasmid pVA736 [14].
• Virulence of Streptococcus mutans: revertants of mutant C4 [15].
• Gnotobiotic rats infected with Streptococcus mutans 6715 at 19 days of age and fed a purified diet (305) containing 5% sucrose developed extensive caries lesions on all molar surfaces within 16 days (35 days of age) [16].
• Identification of the operon for the sorbitol (Glucitol) Phosphoenolpyruvate:Sugar phosphotransferase system in Streptococcus mutans [17].
• At pH 7.0, 25 mM NaF was required to completely inhibit glycolysis by glucose-limited cells at D = 0.05 h-1, whereas a concentration of only 11 mM NaF was required with cells of Streptococcus mutans grown and incubated under identical conditions [18].

Anatomical context of Streptococcus mutans

• Inhibition of complement-mediated lysis of sheep erythrocytes by cell-free preparations from Streptococcus mutans BHT [19].
• Purification and characterization of a rhamnose-containing cell wall antigen of Streptococcus mutans B13 (serotype d) [20].
• Cell membranes of Streptococcus mutans BHT serotype b were prepared after glass bead disruption or mutanolysin digestion of whole cells [21].
• Activation of human monocytes by Streptococcus mutans serotype f polysaccharide: immunoglobulin G Fc receptor expression and tumor necrosis factor and interleukin-1 production [22].
• Rats (COBS/CD) provided Formalin-killed Streptococcus mutans 6715, C211 in their drinking water (10(8) to 10(9) equivalent colony-forming units [CFU] per ml) had high levels of specific antibodies in saliva, colostrum, and milk [23].

Gene context of Streptococcus mutans

• Streptococcus mutans surface alpha-enolase binds salivary mucin MG2 and human plasminogen [24].
• We have shown that MUC7 can bind to cariogenic strains of Streptococcus mutans and that this binding requires a structural determinant in the N-terminal region [25].
• The mannitol-specific enzyme II (mtlA) gene and the mtlR gene of the PTS of Streptococcus mutans [26].
• Salivary mucin as related to oral Streptococcus mutans in elderly people [27].
• We also found that the ability of Streptococcus mutans protein AgI/II to stimulate cytokine release was partially dependent on CD14 and TLR4 [28].

Analytical, diagnostic and therapeutic context of Streptococcus mutans

• Epitope mapping of Streptococcus mutans SR protein and human IgG cross-reactive determinants, by using recombinant proteins and synthetic peptides [10].
• Southern blot analysis under the less stringent condition (allowing up to 35% base mismatch) revealed that the probe covering the proline-rich region hybridized to DNA preparations from strains of Streptococcus cricetus, Streptococcus sobrinus and Streptococcus downei as well as Streptococcus mutans [29].
• Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt [30].
• Molecular cloning and characterization of the glucosyltransferase C gene (gtfC) from Streptococcus mutans LM7 [31].
• Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis identified enolase as a cell surface component of Streptococcus mutans, which was confirmed by enzyme-linked immunosorbent assay, Western blotting, and transmission electron microscopy [24].

References