Levan Production by a Strain of Rothia: Activation of Complement Resulting in Cytotoxicity for Human Gingival Cells

Lesher, R J; Gerencser, Vincent F.

doi:10.1177/00220345770560091401

Cited by 6 publications

(4 citation statements)

References 28 publications

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“…Several studies have demonstrated sucrosedependent production of extracellular levan by oral microorganisms such as Streptococcus salivarius (12,33,39), Actinomyces viscosus (17,25,32,34,42), Streptococcus mutans (3,4,7,47), and Rothia dentocariosa (27). The presence of levan in dental plaque also has been confirmed (5,29,46), and several studies have demonstrated or inferred that at least part of this levan can be degraded by plaque microbial enzymes (6,14,16,30).…”

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confidence: 96%

Degradation of Levan by Actinomyces viscosus

Miller

Somers

1978

Infect Immun

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Actinomyces viscosus ATCC 15987 was examined for its ability to hydrolyze its own levan. Washed whole cells and an ammonium sulfate fraction from cell-free culture fluids were shown to possess levan hydrolase activity. Analyses of reaction mixtures by gel filtration and thin-layer chromatography demonstrated that the product of levan hydrolysis was free fructose. The cell-associated and extracellular enzyme preparations also hydrolyzed inulin and the levans synthesized by Aerobacter levanicum and Bacillus subtilis. Growth of A. viscosus in media supplemented with 0.1% A. viscosus levan resulted in a 33-fold increase and a 7-fold increase in the specific activities of the respective extracellular and cell-associated enzymes when compared with those from 55 mM glucose cultures. Growth in the presence of 29.2 mM sucrose resulted in a 28-fold increase and a 5-fold increase in the specific activities of the respective enzymes when compared with those from the glucose cultures. The extracellular enzyme exhibited high activity over a wide pH range, with 87 and 89% of its pH 6.0 optimum activity at pH 5.0 and 7.0, respectively. The cell-associated enzyme also exhibited optimum activity at pH 6.0, but this was decreased to 10 and 20% at pH 5.0 and 7.0, respectively. Analysis for the presence of extracellular levan during growth of A. viscosus in sucrose broths demonstrated that peak levan concentrations occurred during the mid-exponential to late-exponential phase of growth followed by a rapid decline in extracellular levan as a result of levan hydrolase activity.

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confidence: 96%

Degradation of Levan by Actinomyces viscosus

Miller

Somers

1978

Infect Immun

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“…The presence of serum antibody against Actinomyces species in human periodontal lesions has also been demonstrated (36). Moreover, levan produced by Actinomyces species as well as several other oral microorganisms has been shown to be a mitogen for human B lymphocytes (11) and to be an activator for alternative complement pathway (4,17). It is thought that levan present in periodontal lesions interacts with the immune system and plays an important role in the induction and progress of periodontal disease.…”

Section: Discussionmentioning

confidence: 98%

“…Levan may be a structural polysaccharide in plaque (5,8,9) and may be utilized by plaque flora as a source of carbohydrate, a process which is related to acid production (24,33). Furthermore, levan has been shown to be mitogenic for human B lymphocytes (11) and to activate the alternative complement pathway (4,17,23). These properties could be important in the pathogenicity of periodontal disease.…”

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confidence: 99%

Purification and characterization of levanase from Actinomyces viscosus ATCC 19246

et al. 1987

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The extracellular levanase of Actinomyces viscosus ATCC 19246 was purified about 3,701-fold in 11% yield from the bacterial culture supernatant by means of ammonium sulfate precipitation, followed by DE52 column chromatography, Sephadex G-100 gel filtration, hydroxylapatite column chromatography, and Bio-Gel A 1.5m gel filtration. The molecular weight of the enzyme was estimated to be 89,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme was optimally reactive at pH 6.0 and at 45 degrees C. The activity was inhibited by MnCl2, BaCl2, FeCl3, ZnCl2, HgCl2, and EDTA at a final concentration of 1 mM. The inhibition by EDTA was recovered by adding CaCl2 or MgCl2. The enzyme specifically hydrolyzed levan, but not sucrose, raffinose, melezitose, inulin, and dextran. These results indicate that the purified enzyme is specific for fructan (i.e., levan), which mainly consists of beta-(2,6) linkages.

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“…The presence of fructan in dental plaque has been demonstrated by several authors (19,23,24). Fructan in dental plaque is synthesized extracellularly by many oral bacteria such as Streptococcus salivarius (11,12,14,16,27,31), Streptococcus mutans (3,4,5,8,11), Actinomyces viscosus (19,20,25,26,28,29,36,39), and Rothia dentocariosa (21). However, the fructan produced in dental plaque is not homogeneous.…”

Section: P-(26)-fructofuranosidasementioning

confidence: 99%

Isolation and properties of levanase from Streptococcus salivarius KTA-19

Takahashi¹,

Mizuno²,

Takamori³

1983

Infect Immun

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Fructan-hydrolyzing enzyme from Streptococcus salivarius KTA-19 isolated from human dental plaque was investigated. The enzyme was purified by ammonium sulfate precipitation, acetone fractionation, and column chromatography on Bio-Gel and DEAE-cellulose. The purified enzyme showed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing. Its molecular weight was 100,000 as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme exhibited an optimum pH of 6.5 and decreased its activity from pH 6.0 and especially below pH 5.5. The optimum temperature was 40 to 50°C, and enzyme activity was reduced by 90% at 55°C. Enzyme activity was markedly inhibited by Hg2+, Ag+, Cu2+, and pchloromercuribenzoate at a concentration of 10-3 M, but not by other metal ions or chemical effectors. Fructose was the only by-product of the enzyme action on levan. These results indicated that the levanase of S. salivarius KTA-19 is an exo

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Levan Production by a Strain of Rothia: Activation of Complement Resulting in Cytotoxicity for Human Gingival Cells

Cited by 6 publications

References 28 publications

Degradation of Levan by Actinomyces viscosus

Degradation of Levan by Actinomyces viscosus

Purification and characterization of levanase from Actinomyces viscosus ATCC 19246

Isolation and properties of levanase from Streptococcus salivarius KTA-19

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