Diminished Virulence of Glucan Synthesis-Defective Mutants of
            <i>Streptococcus mutans</i>

Tanzer, Jason M.; Freedman, Michael L.; Fitzgerald, Robert J.; Larson, Ronald E.

doi:10.1128/iai.10.1.197-203.1974

Cited by 178 publications

(103 citation statements)

References 43 publications

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“…When sugars are supplied in excess, S. mutans can store the overload as IPS (van Houte et al, 1969;van Houte and Saxton, 1971;Freedman and Coykendall, 1975;Huis in 't Veld and Backer Dirks, 1978;Birkhed and Tanzer, 1979;Takahashi et al, 1991;Spatafora et al, 1999;Takahashi and Nyvad, 2011) which is used as a source to acid production when sugar surplus is stopped (van Houte et al, 1969;1970;Tanzer et al, 1974;Freedman and Coykendall, 1975;Hamilton, 1977;Spatafora et al, 1995;Busuioc et al, 2009). In fact, when IPS accumulation is disrupted, S. mutans becomes less virulent, less acidogenic and is removed faster from dental plaque (Busuioc et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

The ADP‐glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes

Diez

Demonte

Guerrero

et al. 2013

Molecular Microbiology

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Streptococcus mutans is the leading cause of dental caries worldwide. The bacterium accumulates a glycogen-like internal polysaccharide, which mainly contributes to its carionegic capacity. S.mutans has two genes (glgC and glgD) respectively encoding putative ADP-glucose pyrophosphorylases (ADP-Glc PPase), a key enzyme for glycogen synthesis in most bacteria. Herein, we report the molecular cloning and recombinant expression of both genes (separately or together) followed by the characterization of the respective enzymes. When expressed individually GlgC had ADP-Glc PPase activity, whereas GlgD was inactive. Interestingly, the coexpressed GlgC/GlgD protein was one order of magnitude more active than GlgC alone. Kinetic characterization of GlgC and GlgC/GlgD pointed out remarkable differences between them. Fructose-1,6-bis-phosphate activated GlgC by twofold, but had no effect on GlgC/GlgD. Conversely, phospho-enol-pyruvate and inorganic salts inhibited GlgC/GlgD without affecting GlgC. However, in the presence of fructose-1,6-bis-phosphate GlgC acquired a GlgC/GlgD-like behaviour, becoming sensitive to the stated inhibitors. Results indicate that S. mutans ADP-Glc PPase is an allosteric regulatory enzyme exhibiting sensitivity to modulation by key intermediates of carbohydrates metabolism in the cell. The particular regulatory properties of the S.mutans enzyme agree with phylogenetic analysis, where GlgC and GlgD proteins found in other Firmicutes arrange in distinctive clusters.

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Section: Discussionmentioning

confidence: 99%

The ADP‐glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes

Diez

Demonte

Guerrero

et al. 2013

Molecular Microbiology

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“…We have observed, in a recent series of beenshown to have reduced pathogenicity in the experiments, that GTF is present in the saliva rat caries model (5,6). It has also been shown coat which forms on the surface of hydroxyapatite when this mineral is briefly exposed to whole, * On leave of absence from the University of Oslo.…”

mentioning

confidence: 98%

Adsorption of glucosyltransferase to saliva coated hydroxyapatite Possible mechanism for sucrose dependent bacterial colonization of teeth

Rölla

Ciardi

Schultz

1983

European J Oral Sciences

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Rolla G, Ciardi JE, Schultz SA. Adsorption of glucosyltransferase to saliva coated hydroxyapatite: possible mechanism for sucrose dependent bacterial colonization of teeth. Scand J Dent Res 1983; 91: 112-7.Abstract -Glucosyltransferase (GTF) adsorbed to hydroxyapatite and to saHva coated hydroxyapatite in vitro. Several proteins which are known to be present in the "pellicle" which forms on hydroxyapatite when this mineral is exposed to whole saliva were shown to stimulate or inhibit GTF. It is suggested that these proteins may interact with GTF and cause binding ofthe enzyme to saliva coated hydroxyapatite. A model is suggested where GTF adsorbed to tooth surfaces may induce binding of microorganisms to tooth surfaces.

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“…Both types of GTase can promote cell adherence in the presence of sucrose. Therefore, the enzyme plays a crucial role in the formation of dental plaque and in the development of dental caries (8,20,34,36).…”

mentioning

confidence: 99%

Serotype‐Dependent Inhibition of Glucan Synthesis and Cell Adherence of Streptococcus mutans by Antibody against Glucosyltransferase of Serotype e S. mutans

Hamada

Tai

Slade

1979

Microbiology and Immunology

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Diminished Virulence of Glucan Synthesis-Defective Mutants of Streptococcus mutans

Cited by 178 publications

References 43 publications

The ADP‐glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes

The ADP‐glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes

Adsorption of glucosyltransferase to saliva coated hydroxyapatite Possible mechanism for sucrose dependent bacterial colonization of teeth

Serotype‐Dependent Inhibition of Glucan Synthesis and Cell Adherence of Streptococcus mutans by Antibody against Glucosyltransferase of Serotype e S. mutans

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