The Pst system of Streptococcus mutans is important for phosphate transport and adhesion to abiotic surfaces

Authors

  • D.E. Luz,

    1.  Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil
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    • These authors contributed equally to the present study.

  • R.S.L. Nepomuceno,

    1.  Department of Parasitology, Biomedical Sciences Institute, University of São Paulo, São Paulo, Brazil
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    • These authors contributed equally to the present study.

  • B. Spira,

    1.  Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil
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  • R.C.C. Ferreira

    1.  Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, Brazil
    2.  Department of Parasitology, Biomedical Sciences Institute, University of São Paulo, São Paulo, Brazil
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Rita C.C. Ferreira, Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, Av. Prof. Lineu Prestes, 1374, São Paulo, 05508-00, Brazil Tel.: +55 11 30917408; fax: +55 11 30917354; E-mail: ritacafe@usp.br

Summary

The Pst system is a high-affinity inorganic phosphate transporter found in many bacterial species. Streptococcus mutans, the etiological agent of tooth decay, carries a single copy of the pst operon composed of six cistrons (pstS, pstC1, pstC, pstB, smu.1134 and phoU). Here, we show that deletion of pstS, encoding the phosphate-binding protein, reduces phosphate uptake and impairs cell growth, which can be restored upon enrichment of the medium with high concentrations of inorganic phosphate. The relevance of Pst for growth was also demonstrated in the wild-type strain treated with an anti-PstS antibody. Nevertheless, a reduced ability to bind to saliva-coated surfaces was observed, along with the reduction of extracellular polysaccharide production, although no difference on pH acidification was observed between mutant and wild-type strains. Taken together, the present data indicate that the S. mutans Pst system participates in phosphate uptake, cell growth and expression of virulence-associated traits.

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