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Journal of Bacteriology, January 2006, p. 361-369, Vol. 188, No. 2
0021-9193/06/$08.00+0     doi:10.1128/JB.188.2.361-369.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Structure, Regulation, and Putative Function of the Arginine Deiminase System of Streptococcus suis

Petra Gruening, Marcus Fulde, Peter Valentin-Weigand, and Ralph Goethe*

Institut fuer Mikrobiologie, Zentrum fuer Infektionsmedizin, Stiftung Tieraerztliche Hochschule Hannover, Hannover, Germany

Received 10 June 2005/ Accepted 27 October 2005

Streptococcus suis is an important cause of infectious diseases in young pigs. Little is known about the virulence factors or protective antigens of S. suis. Recently, we have identified two proteins of the arginine deiminase system (ADS) of S. suis, which were temperature induced and expressed on the streptococcal surface (N. Winterhoff, R. Goethe, P. Gruening, M. Rohde, H. Kalisz, H. E. Smith, and P. Valentin-Weigand, J. Bacteriol. 184:6768-6776, 2002). In the present study, we analyzed the complete ADS of S. suis. Due to their homologies to the recently published S. gordonii ADS genes, the genes for arginine deiminase, ornithine carbamoyl-transferase, and carbamate kinase, which were previously designated adiS, octS, and ckS, respectively, were renamed arcA, arcB, and arcC, respectively. Our data revealed that arcA, arcB, and arcC of the S. suis ADS are transcribed from an operon (arcABC operon). Additionally, putative ADS-associated genes were cloned and sequenced which, however, did not belong to the arcABC operon. These were the flpS gene upstream of the arcABC operon with homology to the flp transcription regulator of S. gordonii and the arcD, arcT, arcH, and argR genes downstream of the arcABC operon with high homologies to a putative arginine-ornithine antiporter, a putative dipeptidase of S. gordonii, a putative ß-N-acetylhexosaminidase of S. pneumoniae, and a putative arginine repressor of S. gordonii, respectively. The transcriptional start point of the arcABC operon was determined, and promoter analysis provided evidence that multiple factors contribute to the regulation of the ADS. Thus, a putative binding site for a transcription regulator of the Crp/Fnr family, an ArgR-binding site, and two cis-acting catabolite response elements were identified in the promoter-operator region of the operon. Consistent with this, we could demonstrate that the ADS of S. suis is inducible by arginine and reduced O2 tension and subject to carbon catabolite repression. Furthermore, comparing an arcA knockout mutant in which expression of the three operon-encoded proteins was abolished with the parental wild-type strain showed that the arcABC operon of S. suis contributes to survival under acidic conditions.

* Corresponding author. Mailing address: Institut fuer Mikrobiologie, Zentrum fuer Infektionsmedizin, Tieraerztliche Hochschule Hannover, Bischofsholer Damm 15, 30173 Hannover, Germany. Phone: 49-511 8567625. Fax: 49-511 8567697. E-mail: ralph.goethe{at}tiho-hannover.de.

Journal of Bacteriology, January 2006, p. 361-369, Vol. 188, No. 2
0021-9193/06/$08.00+0     doi:10.1128/JB.188.2.361-369.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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