Inhibition of Acyl-CoA Oxidase by Phenol and Its Implication in Measurement of the Enzyme Activity via the Peroxidase-Coupled Assay System

Gopalan, K. V.; Srivastava, D. K.

doi:10.1006/abio.1997.2186

Cited by 11 publications

(6 citation statements)

References 29 publications

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“…For the biofilm assay, bacteria were grown in BHI or TPYG broth plus 0.5% sucrose and 1% glucose. For the antagonism assay on amino acids, bacteria were grown on an 0.8% modified chemically defined agar plate (33) containing the following components (per ml): Hydrogen peroxide in liquid culture was quantified using a modified method described previously (10,32). Briefly, 1.3 ml of culture supernatant was added to 1.2 ml of solution containing 2.5 mM 4-amino-antipyrine (4-amino-2,3-dimethyl-1-phenyl-3-pyrazolin-5-one; Sigma) and 0.17 M phenol.…”

Section: Methodsmentioning

confidence: 99%

SO-LAAO, a Novell-Amino Acid Oxidase That EnablesStreptococcus oligofermentansTo OutcompeteStreptococcus mutansby Generating H₂O₂from Peptone

et al. 2008

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Section: Methodsmentioning

confidence: 99%

SO-LAAO, a Novell-Amino Acid Oxidase That EnablesStreptococcus oligofermentansTo OutcompeteStreptococcus mutansby Generating H₂O₂from Peptone

et al. 2008

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“…H 2 O 2 in liquid culture was quantified using a modified method described previously (Gopalan and Srivastava, 1997; Seki et al ., 2004). 1.3 ml of culture supernatant was added to 1.2 ml of solution containing 2.5 mM 4‐aminoantipyrine (4‐amino‐2, 3‐dimethyl‐1‐phenyl‐3‐pyrazolin‐5‐one; Sigma) and 0.17 M phenol.…”

Section: Methodsmentioning

confidence: 99%

Streptococcus oligofermentans inhibits Streptococcus mutans through conversion of lactic acid into inhibitory H₂O₂: a possible counteroffensive strategy for interspecies competition

Tong

Chen

Merritt

et al. 2006

Molecular Microbiology

124

130

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SummaryThe oral microbial flora contains over 500 different microbial species that often interact as a means to compete for limited space and nutritional resources. Streptococcus mutans, a major caries-causing pathogen, is a species which tends to interact competitively with other species in the oral cavity, largely due to its ability to generate copious quantities of the toxic metabolite, lactic acid. However, during a recent clinical study, we discovered a novel oral streptococcal species, Streptococcus oligofermentans, whose abundance appeared to be inversely correlated with that of S. mutans within dental plaque samples and thus suggested a possible antagonistic relationship with S. mutans. In this study, we used a defined in vitro interspecies interaction assay to confirm that S. oligofermentans was indeed able to inhibit the growth of S. mutans. Interestingly, this inhibitory effect was relatively specific to S. mutans and was actually enhanced by the presence of lactic acid. Biochemical analyses revealed that S. oligofermentans inhibited the growth of S. mutans via the production of hydrogen peroxide with lactic acid as the substrate. Further genetic and molecular analysis led to the discovery of the lactate oxidase (lox) gene of S. oligofermentans as responsible for this biological activity.Consequently, the lox mutant of S. oligofermentans also showed dramatically reduced inhibitory effects against S. mutans and also exhibited greatly impaired growth in the presence of the lactate produced by S. mutans. These data indicate that S. oligofermentans possesses the capacity to convert its competitor's main 'weapon' (lactic acid) into an inhibitory chemical (H 2O2) in order to gain a competitive growth advantage. This fascinating ability may be an example of a counteroffensive strategy used during chemical warfare within the oral microbial community.

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“…Hydrogen peroxide determination. Hydrogen peroxide (H 2 O 2 ) in liquid culture was quantified using a modified method described previously (10,45). Briefly, 650 l of culture supernatant was added to 600 l of solution containing 2.5 mM 4-amino-antipyrine (4-amino-2,3-dimethyl-1-phenyl-3-pyrazolin-5-one; Sigma) and 0.17 M phenol.…”

Section: Pox-lox Enables S Oligofermentans To Inhibit S Mutansmentioning

confidence: 99%

Function of the Pyruvate Oxidase-Lactate Oxidase Cascade in Interspecies Competition between Streptococcus oligofermentans and Streptococcus mutans

Liu

Tong

Dong

2012

Appl Environ Microbiol

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ABSTRACTComplex interspecies interactions occur constantly between oral commensals and the opportunistic pathogenStreptococcus mutansin dental plaque. Previously, we showed that oral commensalStreptococcus oligofermentanspossesses multiple enzymes for H2O2production, especially lactate oxidase (Lox), allowing it to out-competeS. mutans. In this study, through extensive biochemical and genetic studies, we identified a pyruvate oxidase (pox) gene inS. oligofermentans. Apoxdeletion mutant completely lost Pox activity, while ectopically expressedpoxrestored activity. Pox was determined to produce most of the H2O2in the earlier growth phase and log phase, while Lox mainly contributed to H2O2production in stationary phase. Bothpoxandloxwere expressed throughout the growth phase, while expression of theloxgene increased by about 2.5-fold when cells entered stationary phase. Since lactate accumulation occurred to a large degree in stationary phase, the differential Pox- and Lox-generated H2O2can be attributed to differential gene expression and substrate availability. Interestingly, inactivation ofpoxcauses a dramatic reduction in H2O2production from lactate, suggesting a synergistic action of the two oxidases in converting lactate into H2O2. In anin vitrotwo-species biofilm experiment, thepoxmutant ofS. oligofermentansfailed to inhibitS. mutanseven thoughloxwas active. In summary,S. oligofermentansdevelops a Pox-Lox synergy strategy to maximize its H2O2formation so as to win the interspecies competition.

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Inhibition of Acyl-CoA Oxidase by Phenol and Its Implication in Measurement of the Enzyme Activity via the Peroxidase-Coupled Assay System

Cited by 11 publications

References 29 publications

SO-LAAO, a Novell-Amino Acid Oxidase That EnablesStreptococcus oligofermentansTo OutcompeteStreptococcus mutansby Generating H₂O₂from Peptone

SO-LAAO, a Novell-Amino Acid Oxidase That EnablesStreptococcus oligofermentansTo OutcompeteStreptococcus mutansby Generating H₂O₂from Peptone

Streptococcus oligofermentans inhibits Streptococcus mutans through conversion of lactic acid into inhibitory H₂O₂: a possible counteroffensive strategy for interspecies competition

Function of the Pyruvate Oxidase-Lactate Oxidase Cascade in Interspecies Competition between Streptococcus oligofermentans and Streptococcus mutans

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Inhibition of Acyl-CoA Oxidase by Phenol and Its Implication in Measurement of the Enzyme Activity via the Peroxidase-Coupled Assay System

Cited by 11 publications

References 29 publications

SO-LAAO, a Novell-Amino Acid Oxidase That EnablesStreptococcus oligofermentansTo OutcompeteStreptococcus mutansby Generating H2O2from Peptone

SO-LAAO, a Novell-Amino Acid Oxidase That EnablesStreptococcus oligofermentansTo OutcompeteStreptococcus mutansby Generating H2O2from Peptone

Streptococcus oligofermentans inhibits Streptococcus mutans through conversion of lactic acid into inhibitory H2O2: a possible counteroffensive strategy for interspecies competition

Function of the Pyruvate Oxidase-Lactate Oxidase Cascade in Interspecies Competition between Streptococcus oligofermentans and Streptococcus mutans

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SO-LAAO, a Novell-Amino Acid Oxidase That EnablesStreptococcus oligofermentansTo OutcompeteStreptococcus mutansby Generating H₂O₂from Peptone

SO-LAAO, a Novell-Amino Acid Oxidase That EnablesStreptococcus oligofermentansTo OutcompeteStreptococcus mutansby Generating H₂O₂from Peptone

Streptococcus oligofermentans inhibits Streptococcus mutans through conversion of lactic acid into inhibitory H₂O₂: a possible counteroffensive strategy for interspecies competition