Mechanism of adhesion maintenance by methionine sulphoxide reductase in Streptococcus gordonii

Y. Lei, Y. Zhang, B. D. Guenther, J. Kreth, M. C. Herzberg

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Methionine sulphoxide reductase maintains adhesin function during oxidative stress. Using Streptococcus gordonii as a model, we now show the mechanistic basis of adhesin maintenance provided by MsrA. In biofilms, S. gordonii selectively expresses the msrA gene. When the wild-type strain was grown with exogenous hydrogen peroxide (H2O2), msrA-specific mRNA expression significantly increased, while acid production was unaffected. In the presence of H2O2, a msrA-deletion mutant (ΔMsrA) showed a 6h delay in lag phase growth, a 30% lower yield of H2O2, significantly greater inhibition by H2O2 on agar plates (reversed by complementation), 30% less adhesion to saliva-coated hydroxyapatite, 87% less biofilm formation and an altered electrophoretic pattern of SspAB protein adhesins. Using mass spectrometry, methionine residues in the Met-rich central region of SspB were shown to be oxidized by H2O2 and reduced by MsrA. In intact wild-type cells, MsrA colocalized with a cell wall-staining dye, and MsrA was detected in both cell wall and cytosolic fractions. To maintain normal adhesion and biofilm function of S. gordonii in response to exogenous oxidants therefore msrA is upregulated, methionine oxidation of adhesins and perhaps other proteins is reversed, and adhesion and biofilm formation is maintained.

Original languageEnglish (US)
Pages (from-to)726-738
Number of pages13
JournalMolecular Microbiology
Volume80
Issue number3
DOIs
StatePublished - May 1 2011

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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