ArticleJournal of bacteriology2006
Structure, regulation, and putative function of the arginine deiminase system of Streptococcus suis.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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57 citing papers in PubMed, 117 citations in OpenAlex.
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- Comparative analysis of composition and spatial variations in the foregut microbiota of male and female donkeys.Frontiers in microbiology · 2025Article
- Streptococcal arginine deiminase system defences macrophage bactericidal effect mediated by XRE family protein XtrSs.Virulence · 2024Article
- The ArgR-Regulated ADI Pathway Facilitates the Survival ofInternational journal of molecular sciences · 2024Article
- Acid-tolerant bacteria and prospects in industrial and environmental applications.Applied microbiology and biotechnology · 2023Review
- Transcriptomics in serum and culture medium reveal shared and differential gene regulation in pathogenic and commensalMicrobial genomics · 2023Article
- Role of Metabolic Adaptation ofPathogens (Basel, Switzerland) · 2023Review
- Virulence gene profile and antimicrobial resistance of non-typeable Streptococcus suis isolated from clinically healthy and diseased pigs from North East India.Folia microbiologica · 2022Article
- Screening for Virulence-Related Genes via a Transposon Mutant Library ofMicroorganisms · 2022Article
- The arginine deaminase system plays distinct roles in Borrelia burgdorferi and Borrelia hermsii.PLoS pathogens · 2022Article
- Comparative Proteomic Analysis Reveals Antibacterial Mechanism ofInfection and drug resistance · 2022Article
- Inactivation of theVirulence · 2020Article
- Transcriptomic Analysis ofGenes · 2020Article
- A critical review speculating on the protective efficacies of autogenousPorcine health management · 2020Review
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- MnmE, a Central tRNA-Modifying GTPase, Is Essential for the Growth, Pathogenicity, and Arginine Metabolism ofFrontiers in cellular and infection microbiology · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 beta-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.
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