Synthesis of adherent insoluble glucan by the concerted action of the two glucosyltransferase components of <i>Streptococcus mutans</i>

Inoue, Masakazu; Kinoshita, Toshihiko; Sato, Sestuko; Hamada, Shigeyuki

doi:10.1016/0014-5793(82)80282-2

Cited by 42 publications

(28 citation statements)

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“…However, in conjunction with GTF-S, this GTF-I can produce an adherent WIG (ad-WIG) (7,20,37,53). It seems that ad-WIG is synthesized by the concerted action of the two GTFs (GTF-I and GTF-S), which make ad-WIG with a certain ratio of ␣-1,3/␣-1,6 linkages (20,26,37,50,54).…”

Section: Discussionmentioning

confidence: 99%

“…Dei derived from S. sobrinus UAB108 can inhibit only Dex from S. sobrinus (serotypes d and g), S. downei (previously S. sobrinus, serotype h), and S. macacae (serotype h). This finding suggests the Dei is another important protein existing in some serotypes of the mutans group of streptococci which participates in sucrose metabolism through its interaction with Dex.The mutans group strains of streptococci are capable of converting dietary sucrose to water-soluble glucan (WSG) and water-insoluble glucan (WIG) (9,20,22,26). These glucans, particularly the latter, are the principal materials for the development of human dental plaque and subsequent caries formation (2, 22, 51, 58).…”

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confidence: 99%

“…These glucans, particularly the latter, are the principal materials for the development of human dental plaque and subsequent caries formation (2, 22, 51, 58). There are several enzymes and proteins involved in sucrose metabolism, such as glucosyltransferases (GTFs), which include WSG synthase (GTF-S) (18,19,33,35) and WIG synthase (GTF-I) (2,15,26,29), glucan-binding protein (GBP) (34,40,42), and dextranase (Dex), responsible for the cleavage of ␣-1,6 linkages in glucan molecules (5,17,45). All of these proteins exist simultaneously in mutans group strains of streptococci.…”

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confidence: 99%

“…The mutans group strains of streptococci are capable of converting dietary sucrose to water-soluble glucan (WSG) and water-insoluble glucan (WIG) (9,20,22,26). These glucans, particularly the latter, are the principal materials for the development of human dental plaque and subsequent caries formation (2,22,51,58).…”

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confidence: 99%

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Purification, characterization, and specificity of dextranase inhibitor (Dei) expressed from Streptococcus sobrinus UAB108 gene cloned in Escherichia coli

1995

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The dextranase inhibitor gene (dei) from Streptococcus sobrinus UAB108 was previously cloned, expressed, and sequenced. Its gene product (Dei) has now been purified as a single band with apparent molecular mass of 43 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The specific activity of Dei increased 121-fold upon purification. Most Dei activity (91.2%) was located in the periplasmic fraction from recombinant Escherichia coli cells. Dei competitively inhibits dextranase (Dex). This competitive inhibition mechanism has been further shown by detection and recovery of the intermediate enzyme-inhibitor (Dex-Dei) complex by gel filtration technology using fast protein liquid chromatography. Calibration of their molecular masses indicated that native Dei exists as a tetramer, Dex exists as dimer, and the Dex-Dei complex consists of two Dex molecules with two Dei molecules. Deletion analysis indicates that the intact Dei molecule is essential for Dei activity but not for glucan binding and immune cross-reaction. Dei is a special kind of glucan-binding protein with ability to inhibit Dex with high specificity. It can inhibit endogenous Dex, which can make more branches in glucan with the cooperation of the glucosyltransferase GTF-I. This inhibition cause the accumulation of water-soluble glucan. The latter reaction product can inhibit plaque formation and adherence of the mutans group of streptococcal cells. Dei derived from S. sobrinus UAB108 can inhibit only Dex from S. sobrinus (serotypes d and g), S. downei (previously S. sobrinus, serotype h), and S. macacae (serotype h). This finding suggests the Dei is another important protein existing in some serotypes of the mutans group of streptococci which participates in sucrose metabolism through its interaction with Dex.The mutans group strains of streptococci are capable of converting dietary sucrose to water-soluble glucan (WSG) and water-insoluble glucan (WIG) (9,20,22,26). These glucans, particularly the latter, are the principal materials for the development of human dental plaque and subsequent caries formation (2, 22, 51, 58). There are several enzymes and proteins involved in sucrose metabolism, such as glucosyltransferases (GTFs), which include WSG synthase (GTF-S) (18,19,33,35) and WIG synthase (GTF-I) (2,15,26,29), glucan-binding protein (GBP) (34,40,42), and dextranase (Dex), responsible for the cleavage of ␣-1,6 linkages in glucan molecules (5,17,45). All of these proteins exist simultaneously in mutans group strains of streptococci. The functions and relationships among them, as well as their contributions to sucrose metabolism, have been a focus of research of mechanisms of cariogenicity by the mutans group of streptococci. In just a few years, the introduction of a molecular genetic approach to the study of glucan metabolism and related proteins in oral streptococci has contributed much information. Nevertheless, there remain many unsolved questions. Since 1982, another protein (Dex inhibitor [Dei]) in oral streptococci ...

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Purification, characterization, and specificity of dextranase inhibitor (Dei) expressed from Streptococcus sobrinus UAB108 gene cloned in Escherichia coli

1995

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“…Without the cooperative action of these enzymes, it wauld not be possible for this organism to have any degree of adhesion. Each of the enzymes alone lacks the ability to produce adherence to the glass of a test tube (Fukushima et al, 1981;Inoue et al, 1982). Thus, their cooperative effect is a particular characteristic of S. mutans.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of a Third Glucosyltransferase from Streptococcus Mutans Serotype g

Hanada

Takehara²,

Saeki³

1987

Microbiology

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Streptococcus mutans strain AHT (serotype g ) secretes at least two glucosyltransferases with different PI values. A novel glucosyltransferase with a PI of 5.8 was purified 244-fold from the ammonium sulphate fraction by DEAE-cellulose chromatography, FPLC (Mono Q column, Pharmacia) and hydrophobic chromatography. The enzyme preparation gave a single protein band on analysis by both PAGE and SDS-PAGE, and did not form multiple protein bands detectable by IEF. The M , was estimated to be about 130000 by SDS-PAGE and about 135000 by ultracentrifugal analysis. The apparent K , value and pH optimum of the enzyme were 3-9 f 0.2 mM (mean ~S D ) and about 4.7, respectively. The enzyme synthesized water-soluble glucan from sucrose, and the glucan consisted of over 90 mol% 1,6-a-~-glucosidic linkages. The enzyme activity was not stimulated by primer dextran. Anti-enzyme serum produced a single precipitin band with the purified enzyme preparation, whereas it did not react with either of the other two known glucosyltransferases.

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Insoluble glucans synthesized by cariogenic streptococci: a structural study

Wiater

Choma

Szczodrak

1999

J. Basic Microbiol.

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Of the three cariogenic streptococci grown in four various culture media, the strain Streptococcus mutans 20381 was found to produce large amounts of extracellular glucosyltransferase and water‐insoluble, adhesive exopolysaccharide when grown in batch culture on brain‐heart infusion broth. Methylation and nuclear magnetic resonance analyses revealed that the insoluble polymers synthesized by the crude glucosyltransferase preparations were mixed‐linkage (1 → 3), (1 → 6)‐α‐D‐glucans (so‐called mutans) with a greater proportion of 1,3 to 1,6 linkages and major branch points of 3,6‐linked glucose. The percentage content of different types of linkages in glucans varied widely and depended on the strain of cariogenic bacteria used to produce glucosyltransferase, and on the kind of medium utilized to cultivate mutans streptococci. The potential application of insoluble glucan produced by mutans streptococci is discussed.

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Synthesis of adherent insoluble glucan by the concerted action of the two glucosyltransferase components of Streptococcus mutans

Cited by 42 publications

References 10 publications

Purification, characterization, and specificity of dextranase inhibitor (Dei) expressed from Streptococcus sobrinus UAB108 gene cloned in Escherichia coli

Purification, characterization, and specificity of dextranase inhibitor (Dei) expressed from Streptococcus sobrinus UAB108 gene cloned in Escherichia coli

Purification and Characterization of a Third Glucosyltransferase from Streptococcus Mutans Serotype g

Insoluble glucans synthesized by cariogenic streptococci: a structural study

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