Multiple Forms of Dextran-Binding Proteins from Streptococcus Mutans

McCabe, Mead M.; Hamelik, Ronald M.

doi:10.1007/978-1-4684-3369-2_84

Cited by 25 publications

(21 citation statements)

References 26 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: 67%

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: 67%

The Activity of Glucosyltransferase Adsorbed onto Saliva-coated Hydroxyapatite

1988

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“…This protein was shown to be capable of binding specifically to ␣-1,6-linked glucans, including those synthesized by the S. sobrinus GTFs. These researchers also isolated a number of other GBPs during the affinity chromatography step of purification, in addition to the expected GTFs (16). These additional GBPs were obtained at concentrations severalfold lower than that of the dominant GBL.…”

Section: Discussionmentioning

confidence: 99%

“…Many of the streptococci produce glucan-binding lectins (GBLs) or glucan-binding proteins (GBPs). Several years ago, McCabe and colleagues were able to purify streptococcal GBPs by using Sephadex as an affinity matrix (12,16,17). Others have now used similar chromatographic techniques to purify streptococcal GBPs (2,14,22,23,28,29).…”

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confidence: 99%

Multiple glucan-binding proteins of Streptococcus sobrinus

Lassiter

Banas

et al. 1996

J Bacteriol

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Several proteins from culture supernatants of Streptococcus sobrinus were able to bind avidly to Sephadex G-75. The proteins could be partially eluted from the Sephadex by low-molecular-weight ␣-1,6 glucan or fully eluted by 4 M guanidine hydrochloride. Elution profiles were complex, yielding proteins of 16, 45, 58 to 60, 90, 135, and 145 kDa, showing that the wild-type strain possessed multiple glucan-binding proteins. Two mutants of Streptococcus sobrinus incapable of aggregation by high-molecular-weight ␣-1,6 glucan were isolated. One mutant was spontaneous, from a cell suspension to which glucan had been added, whereas the other was induced by ethyl methanesulfonate. Both mutants were devoid of a 60-kDa protein, as shown by gel electrophoresis of culture supernatants and whole cells. Amino acid analysis showed that the 58-to 60-kDa protein and the 90-kDa protein were distinct, although both were N-terminally blocked. Both mutants retained their ability to adhere to glass in the presence of sucrose and to ferment mannitol and sorbitol. Both mutants retained their glucosytransferase activities, as shown by activity gels. Western blots (immunoblots), employing antibody against a glucan-binding protein of Streptococcus mutans, failed to reveal cross-reactivity with S. sobrinus proteins. The results show that even though S. sobrinus produces several proteins capable of binding ␣-1,6 glucans, the 60-kDa protein is probably the lectin needed for glucan-dependent cellular aggregation.Bacterial lectins seem to have evolved for the purpose of permitting the bacteria to adhere to glycoconjugate-containing surfaces. Members of the genus Streptococcus, found in the oral cavities of humans and animals, are able to adhere to a variety of surfaces when incubated in the presence of sucrose. The disaccharide sucrose serves as a substratum for glucosyltransferases (GTFs) to yield glucans rich in ␣-1,6 and/or ␣-1,3 linkages. Many of the streptococci produce glucan-binding lectins (GBLs) or glucan-binding proteins (GBPs). Several years ago, McCabe and colleagues were able to purify streptococcal GBPs by using Sephadex as an affinity matrix (12,16,17). Others have now used similar chromatographic techniques to purify streptococcal GBPs (2,14,22,23,28,29). Banas et al. (3) were able to clone and sequence a GBP from Streptococcus mutans Ingbritt. In addition to GBLs, the streptococcal GTFs possess glucan-binding domains (19,27). Many of the bacteria which possess cell surface GTFs are not aggregated by glucans, suggesting that the GTFs do not act as lectins. The purpose of the present study was to define which surface protein of Streptococcus sobrinus is involved in glucan-dependent aggregation. To avoid confusion, a GBP is defined as any protein capable of binding reversibly to Sephadex, whereas a GBL is defined as any Sephadex-binding protein capable of conferring the ability of the bacteria to be aggregated by ␣-1,6 glucan. It is here shown that S. sobrinus possesses at least five GBPs, but only one of these, the 60-kDa band of ...

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“…Several glucan-binding proteins (GBP) have been identified by their ability to block dextranmediated agglutination (Olson, 1978) or by affinity chromatography on columns of immobilized dextran or mutan (McCabe et al, 1977;McCabe & Hamelik, 1978;Russell, 1979~). Such affinity columns bound GTF from serotype c strains as well as a GBP of estimated molecular weight 74000 (Russell, 1979~).…”

Section: Introductionmentioning

confidence: 99%

Fructosyltransferase Activity of a Glucan-binding Protein from Streptococcus mutans

1983

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Streptococcus mutans serotype c produces several extracellular proteins which bind to affinity columns of immobilized glucans. The proteins are three distinct glucosyltransferases and another glucan-binding protein (molecular weight 74000) which is now shown to be a fructosyltransferase. This enzyme is antigenically distinct and genetically independent of two other fructosyltransferases produced by the same organism. A mutant is described which lacks the glucan binding fructosyltransferase and has defective ability to form adherent colonies in the presence of sucrose. Although the production of glucans from sucrose results in the glucan binding protein becoming bound to the bacterial surface, and hence perhaps contributing to adherence, the fructans synthesized by the enzyme do not appear to contribute to this phenomenon.

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Multiple Forms of Dextran-Binding Proteins from Streptococcus Mutans

Cited by 25 publications

References 26 publications

The Activity of Glucosyltransferase Adsorbed onto Saliva-coated Hydroxyapatite

The Activity of Glucosyltransferase Adsorbed onto Saliva-coated Hydroxyapatite

Multiple glucan-binding proteins of Streptococcus sobrinus

Fructosyltransferase Activity of a Glucan-binding Protein from Streptococcus mutans

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