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A novel phosphotransferase system of Streptococcus mutans is responsible for transport of carbohydrates with ?-1,3 linkage.

ABSTRACT: The most common type of carbohydrate-transport system in Streptococcus mutans is the phosphoenolpyruvate-sugar phosphotransferase system (PTS). Fourteen PTS exist in S. mutans UA159. Several studies have shown that microorganisms growing in biofilms express different genes compared with their planktonic counterparts. In this study, we showed that one PTS of S. mutans was expressed in sucrose-grown biofilms. Furthermore, the same PTS was also responsible for the transport and metabolism of disaccharide nigerose (3-O-?-d-glucopyranosyl-d-glucose). Additionally, the results indicate that the studied PTS might be involved in the transport and metabolism of carbohydrates synthesized by glucosyltransferase B and glucosyltransferase C of S. mutans. To our knowledge, this is the first report that shows PTS transport of a disaccharide (and possibly extracellular oligosaccharides) with ?-1,3 linkage.

SUBMITTER: Ajdic D

PROVIDER: S-EPMC3593818 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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A novel phosphotransferase system of Streptococcus mutans is responsible for transport of carbohydrates with α-1,3 linkage.

Ajdic D D Chen Z Z

Molecular oral microbiology 20121101 2

The most common type of carbohydrate-transport system in Streptococcus mutans is the phosphoenolpyruvate-sugar phosphotransferase system (PTS). Fourteen PTS exist in S. mutans UA159. Several studies have shown that microorganisms growing in biofilms express different genes compared with their planktonic counterparts. In this study, we showed that one PTS of S. mutans was expressed in sucrose-grown biofilms. Furthermore, the same PTS was also responsible for the transport and metabolism of disacc ...[more]

PMID: 23193985

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Project description:BackgroundStreptococcus mutans is the primary etiological agent of human dental caries. It can metabolize a wide variety of carbohydrates and produce large amounts of organic acids that cause enamel demineralization. Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) plays an important role in carbohydrates uptake of S. mutans. The ptxA and ptxB genes in S. mutans encode putative enzyme IIA and enzyme IIB of the L-ascorbate-specific PTS. The aim of this study was to analyze the function of these proteins and understand the transcriptional regulatory mechanism.ResultsptxA (-), ptxB (-), as well as ptxA (-) , ptxB (-) double-deletion mutants all had more extended lag phase and lower growth yield than wild-type strain UA159 when grown in the medium using L-ascorbate as the sole carbon source. Acid production and acid killing assays showed that the absence of the ptxA and ptxB genes resulted in a reduction in the capacity for acidogenesis, and all three mutant strains did not survive an acid shock. According to biofilm and extracellular polysaccharides (EPS) formation analysis, all the mutant strains formed much less prolific biofilms with small amounts of EPS than wild-type UA159 when using L-ascorbate as the sole carbon source. Moreover, PCR analysis and quantitative real-time PCR revealed that sgaT, ptxA, ptxB, SMU.273, SMU.274 and SMU.275 appear to be parts of the same operon. The transcription levels of these genes were all elevated in the presence of L-ascorbate, and the expression of ptxA gene decreased significantly once ptxB gene was knockout.ConclusionsThe ptxA and ptxB genes are involved in the growth, aciduricity, acidogenesis, and formation of biofilms and EPS of S. mutans when L-ascorbate is the sole carbon source. In addition, the expression of ptxA is regulated by ptxB. ptxA, ptxB, and the upstream gene sgaT, the downstream genes SMU.273, SMU.274 and SMU.275 appear to be parts of the same operon, and L-ascorbate is a potential inducer of the operon.

Dataset Information

A novel phosphotransferase system of Streptococcus mutans is responsible for transport of carbohydrates with ?-1,3 linkage.

Publications

A novel phosphotransferase system of Streptococcus mutans is responsible for transport of carbohydrates with α-1,3 linkage.

Similar Datasets

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