Function of the Pyruvate Oxidase-Lactate Oxidase Cascade in Interspecies Competition between Streptococcus oligofermentans and Streptococcus mutans
Open Access
- 1 April 2012
- journal article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 78 (7), 2120-2127
- https://doi.org/10.1128/aem.07539-11
Abstract
Complex interspecies interactions occur constantly between oral commensals and the opportunistic pathogen Streptococcus mutans in dental plaque. Previously, we showed that oral commensal Streptococcus oligofermentans possesses multiple enzymes for H 2 O 2 production, especially lactate oxidase (Lox), allowing it to out-compete S. mutans . In this study, through extensive biochemical and genetic studies, we identified a pyruvate oxidase ( pox ) gene in S. oligofermentans . A pox deletion mutant completely lost Pox activity, while ectopically expressed pox restored activity. Pox was determined to produce most of the H 2 O 2 in the earlier growth phase and log phase, while Lox mainly contributed to H 2 O 2 production in stationary phase. Both pox and lox were expressed throughout the growth phase, while expression of the lox gene 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 H 2 O 2 can be attributed to differential gene expression and substrate availability. Interestingly, inactivation of pox causes a dramatic reduction in H 2 O 2 production from lactate, suggesting a synergistic action of the two oxidases in converting lactate into H 2 O 2 . In an in vitro two-species biofilm experiment, the pox mutant of S. oligofermentans failed to inhibit S. mutans even though lox was active. In summary, S. oligofermentans develops a Pox-Lox synergy strategy to maximize its H 2 O 2 formation so as to win the interspecies competition.Keywords
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