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Research Paper |
Department of Biology, Middlebury College, Middlebury, VT 05753, USA1
Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA2
Author for correspondence: Grace Spatafora. Tel: +1 802 443 5431. Fax: +1 802 443 2072. e-mail: spatafor{at}middlebury.edu
Streptococcus parasanguis is a primary colonizer of dental plaque and a major player in subacute bacterial endocarditis. In the present study, the authors report that an ORF (ORF3) located 77 bp downstream of the fimA operon on the S. parasanguis FW213 chromosome complements an Escherichia coli thiol peroxidase (tpx) mutation in glutamine synthetase (GS) protection assays and that GS is protected by the ORF3 gene product in S. parasanguis cell extracts. In addition, the putative streptococcal peroxidase (TpxSp) protects S. parasanguis from stress caused by H2O2 and is induced by oxygen, as revealed by Northern blot analysis. Taken collectively, these findings support a thiol-dependent antioxidant activity for Tpx in S. parasanguis.
Keywords: peroxidase, oral streptococci, oxidative stress
Abbreviations: GS, glutamine synthetase; MCO, metal-ion-catalysed oxidation; SOD, superoxide dismutase; TpxEc, periplasmic thiol peroxidase of Escherichia coli; TpxSp, putative streptococcal thiol peroxidase
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