This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Winterhoff, N. Articles by Valentin-Weigand, P. Search for Related Content PubMed PubMed Citation Articles by Winterhoff, N. Articles by Valentin-Weigand, P. Pubmed/NCBI databases Protein Substance via MeSH

 Previous Article  |  Next Article 

Journal of Bacteriology, December 2002, p. 6768-6776, Vol. 184, No. 24
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.24.6768-6776.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of Two Temperature-Induced Surface-Associated Proteins of Streptococcus suis with High Homologies to Members of the Arginine Deiminase System of Streptococcus pyogenes

Nora Winterhoff,¹ Ralph Goethe,¹ Petra Gruening,¹ Manfred Rohde,² Henryk Kalisz,² Hilde E. Smith,³ and Peter Valentin-Weigand^1*

Institut fuer Mikrobiologie und Tierseuchen, Tieraerztliche Hochschule Hannover, Hannover,¹ Research Center for Biotechnology, Braunschweig, Germany,² Division of Infectious Diseases and Food Chain Quality, Institute for Animal Science and Health, Lelystad, The Netherlands³

Received 3 July 2002/ Accepted 11 September 2002

The present study was performed to identify stress-induced putative virulence proteins of Streptococcus suis. For this, protein expression patterns of streptococci grown at 32, 37, and 42°C were compared by one- and two-dimensional gel electrophoresis. Temperature shifts from 32 and 37 to 42°C induced expression of two cell wall-associated proteins with apparent molecular masses of approximately 47 and 53 kDa. Amino-terminal sequence analysis of the two proteins indicated homologies of the 47-kDa protein with an ornithine carbamoyltransferase (OCT) from Streptococcus pyogenes and of the 53-kDa protein with the streptococcal acid glycoprotein (SAGP) from S. pyogenes, an arginine deiminase (AD) recently proposed as a putative virulence factor. Cloning and sequencing the genes encoding the putative OCT and AD of S. suis, octS and adiS, respectively, revealed that they had 81.2 (octS) and 80.2% (adiS) identity with the respective genes of S. pyogenes. Both genes belong to the AD system, also found in other bacteria. Southern hybridization analysis demonstrated the presence of the adiS gene in all 42 serotype 2 and 9 S. suis strains tested. In 9 of these 42 strains, selected randomly, we confirmed expression of the AdiS protein, homologous to SAGP, by immunoblot analysis using a specific antiserum against the SAGP of S. pyogenes. In all strains AD activity was detected. Furthermore, by immunoelectron microscopy using the anti-S. pyogenes SAGP antiserum we were able to demonstrate that the AdiS protein is expressed on the streptococcal surface in association with the capsular polysaccharides but is not coexpressed with them.

---

* Corresponding author. Mailing address: Institut fuer Mikrobiologie und Tierseuchen, Tieraerztliche Hochschule Hannover, Bischofsholer Damm 15, 30171 Hannover, Germany. Phone: 49-511 953 7362. Fax: 49-511 953 7697. E-mail: peter.valentin{at}tiho-hannover.de.

---

Journal of Bacteriology, December 2002, p. 6768-6776, Vol. 184, No. 24
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.24.6768-6776.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Liu, Y., Dong, Y., Chen, Y.-Y. M., Burne, R. A. (2008). Environmental and Growth Phase Regulation of the Streptococcus gordonii Arginine Deiminase Genes. Appl. Environ. Microbiol. 74: 5023-5030 [Abstract] [Full Text]  
• Graveline, R., Segura, M., Radzioch, D., Gottschalk, M. (2007). TLR2-dependent recognition of Streptococcus suis is modulated by the presence of capsular polysaccharide which modifies macrophage responsiveness. Int Immunol 19: 375-389 [Abstract] [Full Text]  
• Severin, A., Nickbarg, E., Wooters, J., Quazi, S. A., Matsuka, Y. V., Murphy, E., Moutsatsos, I. K., Zagursky, R. J., Olmsted, S. B. (2007). Proteomic Analysis and Identification of Streptococcus pyogenes Surface-Associated Proteins. J. Bacteriol. 189: 1514-1522 [Abstract] [Full Text]  
• Baums, C. G., Verkuhlen, G. J., Rehm, T., Silva, L. M. G., Beyerbach, M., Pohlmeyer, K., Valentin-Weigand, P. (2007). Prevalence of Streptococcus suis Genotypes in Wild Boars of Northwestern Germany. Appl. Environ. Microbiol. 73: 711-717 [Abstract] [Full Text]  
• Gruening, P., Fulde, M., Valentin-Weigand, P., Goethe, R. (2006). Structure, Regulation, and Putative Function of the Arginine Deiminase System of Streptococcus suis. J. Bacteriol. 188: 361-369 [Abstract] [Full Text]  
• Heidt, M. C., Mohamed, W., Hain, T., Vogt, P. R., Chakraborty, T., Domann, E. (2005). Human Infective Endocarditis Caused by Streptococcus suis Serotype 2. J. Clin. Microbiol. 43: 4898-4901 [Abstract] [Full Text]  
• Cole, J. N., Ramirez, R. D., Currie, B. J., Cordwell, S. J., Djordjevic, S. P., Walker, M. J. (2005). Surface Analyses and Immune Reactivities of Major Cell Wall-Associated Proteins of Group A Streptococcus. Infect. Immun. 73: 3137-3146 [Abstract] [Full Text]  
• Chaussee, M. A., Callegari, E. A., Chaussee, M. S. (2004). Rgg Regulates Growth Phase-Dependent Expression of Proteins Associated with Secondary Metabolism and Stress in Streptococcus pyogenes. J. Bacteriol. 186: 7091-7099 [Abstract] [Full Text]  
• Cotter, P. D., Hill, C. (2003). Surviving the Acid Test: Responses of Gram-Positive Bacteria to Low pH. Microbiol. Mol. Biol. Rev. 67: 429-453 [Abstract] [Full Text]