Fructosyltransferase Activity of a Glucan-binding Protein from Streptococcus mutans

Russell, R. R. B.; Donald, Ann C.; Douglas, C. W. I.

doi:10.1099/00221287-129-10-3243

Cited by 30 publications

(38 citation statements)

References 24 publications

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“…Cariogenic streptococci produce several glucan-binding proteins, including GTF, fructosyltransferase (FTF), and non-enzymatic lectin-like proteins (McCabe and Hamelik, 1978;Russell, 1979;Russell et al, 1983). Results from the present study indicate that a significant amount of glucans synthesized by GTF adsorbed to saliva-coated surfaces remain attached to the mineral surface (Table 3).…”

Section: Discussionmentioning

confidence: 53%

The Activity of Glucosyltransferase Adsorbed onto Saliva-coated Hydroxyapatite

1988

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This study aimed to determine physical and kinetic properties ofglucosyltransferase (GTF) adsorbed onto hydroxyapatite (HA) surfaces.For development of a solid-phase enzyme assay, 4.0-mg samples of washed HA powder were exposed to centrifuged whole saliva (WSHA) or buffer, and subsequently exposed to a GTF solution. The activities of GTF adsorbed to H4 and that remaining in solution were measured. WSH4 was more effective in adsorbing GTF than was naked HA. Enzyme activity on the surface of WSHA was enhanced; more activity was detected on WSHA than was apparently removed from solution. A similar effect was observed when GTF was adsorbed to naked HA from a mixture with lysozyme or saliva; however, no enhancement was seen when GTF was adsorbed from a mixture with albumin. Compared with GTF in solution, adsorbed GTF displayed activity over a much wider range ofpH values. Temperature-activity profiles indicated that GTF adsorbed to surfaces had a lower temperature optimum (400C) than did soluble enzyme (45'C), and that the bound enzyme was more resistant to adverse effects of heat at elevated temperatures. The majority of glucan made by GTF adsorbed to parotid saliva-coated HA remained attached to the surface. The activity of lysozyme adsorbed to HA was reduced by adsorption of GTF to the same surface and was almost completely abolished by formation of glucans by the adsorbed GTF. These results suggest that soluble bacterial enzymes found in saliva can be incorporated into pellicle, interact with host-derived molecules on the surfaces of teeth, express enzymatic activity, and potentially influence the biological properties ofpellicle.

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Section: Discussionmentioning

confidence: 53%

The Activity of Glucosyltransferase Adsorbed onto Saliva-coated Hydroxyapatite

1988

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“…have molecular masses of more than 100 kDa, the average bacterial FTFs molecular size. In 1983, Russell et al reported a glucan binding protein with FTF activity in S. mutans, but no explanation could be given for this property (29), so it is possible that the same recombination had taken place in S. mutans.…”

Section: Resultsmentioning

confidence: 99%

Molecular Characterization of Inulosucrase fromLeuconostoc citreum: a Fructosyltransferase within a Glucosyltransferase

2003

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The gene coding for inulosucrase in Leuconostoc citreum CW28, islA, was cloned, sequenced, and expressed in Escherichia coli. The recombinant enzyme catalyzed inulin synthesis from sucrose like the wild-type enzyme. Inulosucrase presents an unusual structure: its N-terminal region is similar to the variable region of glucosyltransferases, its catalytic domain is similar to fructosyltransferases from various microorganisms, and its C-terminal domain presents similarity to the glucan binding domain from alternansucrase, a glucosyltransferase from Leuconostoc mesenteroides NRRL B-1355. From sequence comparison, it was found that this fructosyltransferase is a natural chimeric enzyme resulting from the substitution of the catalytic domain of alternansucrase by a fructosyltransferase. Two different forms of the islA gene truncated in the C-terminal glucan binding domain were successfully expressed in E. coli and retained their ability to synthesize inulin but lost thermal stability. This is the first report of an inulosucrase bearing structural features of both glucosyltransferases and fructosyltransferases.

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“…mutans tends to break down to yield multiple bands in the mol. wt range 50000-70000 (Russell et al, 1983a) and the GBP in E. coli lysates (Fig. lb) appears also to yield such minor bands.…”

Section: R E S U L T Smentioning

confidence: 99%

“…mutans supports our previous evidence for the apparent identity of GBP to one of the forms of FTF of S . mutans (Russell et al, 1983a).…”

Section: R E S U L T Smentioning

confidence: 99%

Expression of a Gene for Glucan-binding Protein from Streptococcus mutans in Escherichia coli

1985

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The structural gene for a glucan-binding protein (GBP) of Streptococcus mutans has been inserted into a bacteriophage A vector and expressed in Escherichia coli K12. Lysates of E. coli infected with the recombinant phage contain an antigenic protein of the same size as S . mutans GBP. The GBP synthesized in E. coli can be affinity-purified on immobilized glucan and antiserum raised against it has been shown to precipitate fructosyltransferase activity from S . mutans.

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Fructosyltransferase Activity of a Glucan-binding Protein from Streptococcus mutans

Cited by 30 publications

References 24 publications

The Activity of Glucosyltransferase Adsorbed onto Saliva-coated Hydroxyapatite

The Activity of Glucosyltransferase Adsorbed onto Saliva-coated Hydroxyapatite

Molecular Characterization of Inulosucrase fromLeuconostoc citreum: a Fructosyltransferase within a Glucosyltransferase

Expression of a Gene for Glucan-binding Protein from Streptococcus mutans in Escherichia coli

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