Publications

• Two gene clusters coordinate galactose and lactose metabolism in Streptococcus gordonii.

  Zeng L., Martino N.C., Burne R.A.

  Streptococcus gordonii is an early colonizer of the human oral cavity and an abundant constituent of oral biofilms. Two tandemly arranged gene clusters, designated lac and gal, were identified in the S. gordonii DL1 genome, which encode genes of the tagatose pathway (lacABCD) and sugar phosphotran ... >> More

  Streptococcus gordonii is an early colonizer of the human oral cavity and an abundant constituent of oral biofilms. Two tandemly arranged gene clusters, designated lac and gal, were identified in the S. gordonii DL1 genome, which encode genes of the tagatose pathway (lacABCD) and sugar phosphotransferase system (PTS) enzyme II permeases. Genes encoding a predicted phospho-β-galactosidase (LacG), a DeoR family transcriptional regulator (LacR), and a transcriptional antiterminator (LacT) were also present in the clusters. Growth and PTS assays supported that the permease designated EII(Lac) transports lactose and galactose, whereas EII(Gal) transports galactose. The expression of the gene for EII(Gal) was markedly upregulated in cells growing on galactose. Using promoter-cat fusions, a role for LacR in the regulation of the expressions of both gene clusters was demonstrated, and the gal cluster was also shown to be sensitive to repression by CcpA. The deletion of lacT caused an inability to grow on lactose, apparently because of its role in the regulation of the expression of the genes for EII(Lac), but had little effect on galactose utilization. S. gordonii maintained a selective advantage over Streptococcus mutans in a mixed-species competition assay, associated with its possession of a high-affinity galactose PTS, although S. mutans could persist better at low pHs. Collectively, these results support the concept that the galactose and lactose systems of S. gordonii are subject to complex regulation and that a high-affinity galactose PTS may be advantageous when S. gordonii is competing against the caries pathogen S. mutans in oral biofilms. << Less

  Appl Environ Microbiol 78:5597-5605(2012) [PubMed] [EuropePMC]

• A galactose-specific sugar: phosphotransferase permease is prevalent in the non-core genome of Streptococcus mutans.

  Zeng L., Xue P., Stanhope M.J., Burne R.A.

  Three genes predicted to encode the A, B and C domains of a sugar : phosphotransferase system (PTS) permease specific for galactose\(EII(Gal) ) were identified in the genomes of 35 of 57 recently sequenced isolates of Streptococcus mutans, the primary etiological agent of human dental caries. Muta ... >> More

  Three genes predicted to encode the A, B and C domains of a sugar : phosphotransferase system (PTS) permease specific for galactose\(EII(Gal) ) were identified in the genomes of 35 of 57 recently sequenced isolates of Streptococcus mutans, the primary etiological agent of human dental caries. Mutants defective in the EII(Gal) complex were constructed in six of the isolates and showed markedly reduced growth rates on galactose-based medium relative to the parental strains. An EII(Gal) -deficient strain constructed using the invasive serotype f strain OMZ175 (OMZ/IIGal) expressed significantly lower PTS activity when galactose was present as the substrate. Galactose was shown to be an effective inducer of catabolite repression in OMZ175, but not in the EII(Gal) -deficient strain. In a mixed-species competition assay with galactose as the sole carbohydrate source, OMZ/IIGal was less effective than the parental strain at competing with the oral commensal bacterium Streptococcus gordonii, which has a high-affinity galactose transporter. Hence, a significant proportion of S. mutans strains encode a galactose PTS permease that could enhance the ability of these isolates to compete more effectively with commensal streptococci for galactose in salivary constituents and the diet. << Less

  Mol Oral Microbiol 28:292-301(2013) [PubMed] [EuropePMC]