Dextran Receptors as Immunogens in Caries Prophylaxis

Olson, Gerald A.

doi:10.1007/978-1-4684-3369-2_87

Cited by 6 publications

(5 citation statements)

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“…Olson (38) conducted studies in which isolated "dextran receptors" used as immunogens in rats afforded reduction in caries development. Also, antisera were able to inhibit glucan-mediated aggregation, and it was concluded that protection in vivo resulted from interference with bacterial binding of glucan (38,39). Of particular relevance was the finding that multiple forms of the GBL exist (28).…”

Section: Discussionmentioning

confidence: 99%

“…It has been suggested that the surface glucan-binding lectin (GBL) is a virulence factor in promoting the colonization of the mutans streptococci (13,25,29,30,38). Because dextrans (glucans rich in ot-1,6 anomeric linkages) are synthesized from sucrose by several oral streptococci (4,7,14,17,20,33), specific interactions with the GBL may be important in adherence and accumulation processes, resulting in an extracellular matrix firmly bound to tooth surfaces (11, 13, 15, 22-25, 30, 37, 44).…”

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confidence: 99%

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Specificity of the glucan-binding lectin of Streptococcus cricetus

et al. 1988

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The specificity of the glucan-binding lectin (GBL) of Streptococcus cricetus AHT was determined. Examination of the kinetics of aggregation of cell suspensions with glucans containing various percentages of a-1,6, a-1,4, a-1,3, and a-1,2 anomeric linkages revealed that only glucans with at least 80% a-1,6 linkages promoted strong aggregation. Moreover, only linear glucans with molecular weights greater than 5 x 105 were capable of causing rapid aggregation of the bacteria. The lectin was observed to be present on S. cricetus strains, on Streptococcus sobrinus, and on several Streptococcus mutans strains. Preincubation of suspensions of S. cricetus AHT with glucan T10 (molecular weight of 10,000) before the addition of high-molecular-weight glucan resulted in competitive inhibition in a concentration-dependent manner. Inhibition was achieved also with isomaltopentaose, isomaltohexaose, and isomaltooctaose, but at higher concentrations than glucan T10. In contrast, no inhibition was observed with maltoheptaose, providing additional evidence for the specificity of GBL. Treatment of suspensions of S. cricetus AHT with trypsin before and after aggregation with high-molecular-weight glucan revealed a substantial level of protection of GBL when in a bound state. Collectively, these results indicated that GBL has an absolute affinity for glucans rich in at-1,6 linkages and possesses an active site which recognizes internal sequences and accommodates isomaltosaccharides of at least nine residues. This unusual specificity may contribute to the colonization of S. cricetus, S. sobninus, and S. mutans in glucan-containing plaque in the oral cavity.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Specificity of the glucan-binding lectin of Streptococcus cricetus

et al. 1988

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“…During the investigations of MS aggregation properties, it was noted that a certain proportion of extracellular GTFs could become cell-associated in the presence of glucan or commercially prepared dextran (Gibbons and Fitzgerald, 1969;Gibbons and van Houte, 1973;Mukasa and Slade, 1974). This cell-association of GTFs was determined to be due to binding by the GTFs to glucan or dextran that coated the bacteria (Mukasa and Slade, 1974;Kuramitsu and Ingersoll, 1978) in conjunction with a proposed proteinaceous receptor for glucan (Scherp, 1971;Kelstrup and Funder-Neilsen, 1974;Kuramitsu, 1974;Olson et al, 1974;McCabe andSmith, 1975, 1976;McCabe, 1976;Slade, 1977;Kuramitsu and Ingersoll, 1978;Montville et al, 1978;Olson, 1978;Wu-Yuan et al, 1978). Several groups examined Streptococcus mutans proteins, most often via affinity chromatography, using glucan or dextran, in attempts to isolate and identify the putative cell-surface receptor or protein(s) that might contribute to overall plaque development McCabe and Hamelik, 1978;Russell, 1979;Smith et al, 1979Smith et al, , 1994Smith et al, , 1998Landale and McCabe, 1987;Wu-Yuan and Gill, 1992;Sun et al, 1994;Sato et al, 1997).…”

Section: Discovery Of Glucan-binding Proteinsmentioning

confidence: 99%

Glucan-binding Proteins of the Oral Streptococci

Banas

Vickerman

2003

Critical Reviews in Oral Biology & Medicine

290

262

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ABSTRACT:The synthesis of extracellular glucan is an integral component of the sucrose-dependent colonization of tooth surfaces by species of the mutans streptococci. In investigators' attempts to understand the mechanisms of plaque biofilm development, several glucan-binding proteins (GBPs) have been discovered. Some of these, the glucosyltransferases, catalyze the synthesis of glucan, whereas others, designated only as glucan-binding proteins, have affinities for different forms of glucan and contribute to aspects of the biology of their host organisms. The functions of these latter glucan-binding proteins include dextran-dependent aggregation, dextranase inhibition, plaque cohesion, and perhaps cell wall synthesis. In some instances, their glucan-binding domains share common features, whereas in others the mechanism for glucan binding remains unknown. Recent studies indicate that at least some of the glucan-binding proteins modulate virulence and some can act as protective immunogens within animal models. Overall, the multiplicity of GBPs and their aforementioned properties are testimonies to their importance. Future studies will greatly advance the understanding of the distribution, function, and regulation of the GBPs and place into perspective the facets of their contributions to the biology of the oral streptococci.

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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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Dextran Receptors as Immunogens in Caries Prophylaxis

Cited by 6 publications

References 11 publications

Specificity of the glucan-binding lectin of Streptococcus cricetus

Specificity of the glucan-binding lectin of Streptococcus cricetus

Glucan-binding Proteins of the Oral Streptococci

Fructosyltransferase Activity of a Glucan-binding Protein from Streptococcus mutans

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