Glucosyltransferases of <i>Streptococcus sobrinus</i> C211 are both stimulated and inhibited by hydrogen peroxide

McAlister, D. B.; Nambiar, Sudhir; Taylor, K. Grant; Doyle, Ronald J.

doi:10.1111/j.1399-302x.1989.tb00242.x

Cited by 4 publications

(3 citation statements)

References 40 publications

(47 reference statements)

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“…1). A similar profile of GTase activities has been obtained ; 38 lower concentrations of hydrogen peroxide stimulated insoluble glucan synthesis of S. sobrinus GTases, whereas higher concentrations of this agent caused complete inhibition of glucan production by GTase-S and GTase-I. This phenomenon may be due to crosslinking of the enzyme proteins through tyrosine residues or deamination of lysyl residues of G T~s~.~~ Some surfactants, e g , cationic or ampholytic, may induce hydrophobic or ionic interactions between GTases and a functional hydrophobic group within the surfactant molecule.…”

Section: Discussionmentioning

confidence: 57%

Effects of selected surfactants on purified glucosyltransferases from mutans streptococci and cellular adherence to smooth surfaces

Kawabata

Torii²,

Minami³

et al. 1993

Journal of Medical Microbiology

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Summary. The inhibitory effect of non-ionic, anionic, cationic and ampholytic surfactants on cellular growth of Streptococcus rnutans MT8 148 and S. sobrinus 67 15, on glucan synthesis by the purified glucosyltransferase (GTase) from these organisms, and on bacterial adherence to glass surfaces was examined in ritro. Cationic surfactants exhibited marked bactericidal activities. Anionic and ampholytic compounds were less strongly bactericidal and non-ionic surfactants produced only slight inhibition of cell growth under the conditions tested. Some non-ionic compounds had no effect on this. Glucan synthesis by GTase from mutans streptococci was inhibited by anionic and cationic surfactants. Among various GTase proteins. insoluble glucan synthesising GTases, i.e., S . nzutans CA-GTase and S. sobrinus GTase-I were those most effectively inhibited by these agents. However, it was noted that whereas lower concentrations of cationic surfactants enhanced these GTase activities, higher concentrations of the surfactants were inhibitory. Non-ionic detergents stimulated soluble glucan synthesis from S . imtans CF-GTase and cationic and ampholytic surfactants enhanced or inhibited glucan synthesis depending on the concentrations of the surfactants. Sucrosedependent cellular adherence of resting cells of mutans streptococci to glass surfaces was inhibited by the addition of surfactants that annulled the GTase activities.

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Section: Discussionmentioning

confidence: 57%

Effects of selected surfactants on purified glucosyltransferases from mutans streptococci and cellular adherence to smooth surfaces

Kawabata

Torii²,

Minami³

et al. 1993

Journal of Medical Microbiology

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“…In addition, hydrogen peroxide has previously been shown to be bactericidal for oral micro-organisms (Wennstrom et al, 1979;Thomas et al, 1983). It was observed that high concentrations of hydrogen peroxide may be inhibitory to GTF and oral microbes, but low concentrations may actually enhance caries activity due to the increase in production of insoluble glucans that mediate attachment of S. mutans to smooth surfaces (McAlister et al, 1989). The present study involves Fenton chemistry, which is often cited as a model for biological processes such as in vivo oxidative damage occurring during certain disease states, carcinogenesis, and drug-associated toxicity (Ames et al, 1981;Gutteridge, 1984, 1986;Aust et al, 1985;Wink et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Glucosyltransferase Inactivation Reduces Dental Caries

Devulapalle

Mooser

2001

J Dent Res

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Dental caries has been an intractable disease in spite of intense dental research. The metabolic acids produced by mutans streptococci demineralize the tooth surface and lead to dental caries. The enzyme glucosyltransferase (GTF) produced by mutans streptococci is the key factor in this process. Oral bacterial GTFs use sucrose as a substrate in synthesis of either water-soluble or insoluble glucans. In this investigation, kinetic studies with divalent metal ions revealed their strong binding affinity to GTF. The metal ions also proved to be strong inhibitors of the enzyme. Here we describe a simple method of inactivating the enzyme that actively participates in dental caries by taking advantage of a Fenton reaction which requires metal ions such as iron or copper and peroxide. The hydroxyl radical ions produced via the Fenton reaction inactivate GTF, a factor in the production of dental caries.

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“…This indicates that the interactions between the enzymes were lost after LP was bound with its substrates. Although H 2 O 2 alone has some inhibitory effect on Gtfs from Streptococcus sobrinus [McAlister et al, 1989], concentrations used in our study were not effective. As SCN -was also ineffective, it is unlikely that minor changes in the ionic strength of the medium were responsible for loss of the inhibition and enhancements of Gtf activity.…”

Section: Discussionmentioning

confidence: 43%

Lactoperoxidase Inhibits Glucosyltransferases from <i>Streptococcus mutans </i>in vitro

Korpela¹,

Yu²,

Loimaranta³

et al. 2002

Caries Res

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This study examines the possible effect of the antimicrobial peroxidase system on the activity of streptococcal glucosyltransferases B, C and D (GtfB, GtfC and GtfD), either in solution (GtfB and GtfC) or when adsorbed to hydroxyapatite (GtfC and GtfD) at pH 6.5. The lactoperoxidase (LP) system (LP, H₂O₂, SCN^–) had no effect on the activity of dissolved GtfC, but the activity of dissolved GtfB was enhanced. The LP system, however, strongly inhibited the activities of both GtfC and GtfD in their adsorbed form. LP enzyme, without its substrates, inhibited all three Gtf enzymes: GtfB and GtfC in concentrations between 10 and 100 µg/ml in liquid phase and adsorbed GtfC and GtfD in concentrations between 25 and 50 µg/ml. This inhibition was in part abolished in liquid phase, but not in solid phase, if the substrates of LP were added. This study shows that the lactoperoxidase system can exert inhibitory activity against streptococcal Gtfs without generating oxidizing agents.

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Glucosyltransferases of Streptococcus sobrinus C211 are both stimulated and inhibited by hydrogen peroxide

Cited by 4 publications

References 40 publications

Effects of selected surfactants on purified glucosyltransferases from mutans streptococci and cellular adherence to smooth surfaces

Effects of selected surfactants on purified glucosyltransferases from mutans streptococci and cellular adherence to smooth surfaces

Glucosyltransferase Inactivation Reduces Dental Caries

Lactoperoxidase Inhibits Glucosyltransferases from <i>Streptococcus mutans </i>in vitro

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