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Published online ahead of print on 22 October 2009 as doi:10.1099/mic.0.031955-0
Microbiology (2009), DOI 10.1099/mic.0.031955-0
© 2009 Society for General Microbiology
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Microbiology 0 (2009), mic.0.031955; DOI  10.1099/mic.0.031955-0
© 2009 Society for General Microbiology

Characterization of a virulent and cell-wall-located deoxyribonuclease of Streptococcus pyogenes

Tadao Hasegawa1,3, Masaaki Minami1, Akira Okamoto2, Ichiro Tatsuno1, Masanori Isaka1 and Michio Ohta2

1 Nagoya City University Graduate School of Medical Sciences;
2 Nagoya University Graduate School of Medicine

We investigated culture supernatant proteins from the M1 serotype Streptococcus pyogenes by 2-dimensional gel electrophoresis and peptide mass mapping analysis, and we characterized the single protein spots. Among them, we analyzed the Spy0747 protein. This protein is homologous to the SsnA protein, which is a cell-wall-located DNase expressed in S. suis serotype 2. We designated the Spy0747 protein as SpnA. SpnA protein was also detected in the insoluble fraction of whole cell lysates using shotgun proteomic analysis and this result suggests that SpnA is also located in the cell wall. SpnA was expressed as a glutathione S-transferase-fusion protein in Escherichia coli. We confirmed that the recombinant protein had deoxyribonuclease activity that was dependent on Ca2+ and Mg2+ like SsnA. Blood bactericidal assays and mouse infection model experiments showed that the spnA knock-out strain was less virulent compared to the parental strain, thus suggesting that SpnA could play an important role in virulence. Using PCR, we found that the spnA gene was present in all clinical S. pyogenes strains examined in this study. Our results and the previous report that Spy0747 was identified as a surface-associated protein suggest that SpnA, an important cell-wall-located DNase, is involved in virulence that is generally produced in S. pyogenes.

3 E-mail: tadaoh{at}med.nagoya-cu.ac.jp






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