CoChat
Sign Up
Cited by 70

The DOI matches its Crossref record.

ArgR is an essential local transcriptional regulator of the arcABC operon in Streptococcus suis and is crucial for biological fitness in an acidic environment

Fulde, Marcus, Willenborg, Joerg, de Greeff, Astrid, Benga, Laurentiu, Smith, Hilde E., Valentin-Weigand, Peter, Goethe, Ralph·2011·Microbiology
DOI 10.1099/mic.0.043067-0
Open this paper in CoChat — free account

Abstract

Streptococcus suis is one of the most important pathogens in pigs and can also cause severe infections in humans. Despite its clinical relevance, very little is known about the factors that contribute to its virulence. Recently, we identified a new putative virulence factor in S. suis, the arginine deiminase system (ADS), an arginine catabolic enzyme system encoded by the arcABC operon, which enables S. suis to survive in an acidic environment. In this study, we focused on ArgR, an ADS-associated regulator belonging to the ArgR/AhrC arginine repressor family. Using an argR knockout strain we were able to show that ArgR is essential for arcABC operon expression and necessary for the biological fitness of S. suis. By cDNA expression microarray analyses and quantitative real-time RT-PCR we found that the arcABC operon is the only gene cluster regulated by ArgR, which is in contrast to the situation in many other bacteria. Reporter gene analysis with gfp under the control of the arcABC promoter demonstrated that ArgR is able to activate the arcABC promoter. Electrophoretic mobility shift assays with fragments of the arcABC promoter and recombinant ArgR, and chromatin immunoprecipitation with antibodies directed against ArgR, revealed that ArgR interacts with the arcABC promoter in vitro and in vivo by binding to a region from −147 to −72 bp upstream of the transcriptional start point. Overall, our results show that in S. suis, ArgR is an essential, system-specific transcriptional regulator of the ADS that interacts directly with the arcABC promoter in vivo.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1099/mic.0.043067-0

Cites

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 52

  1. Arends, 1988, Meningitis caused by Streptococcus suis in humans, Rev Infect Dis, 10, 131, 10.1093/clinids/10.1.131 · DOI
  2. Barcelona-Andrés, 2002, Gene structure, organization, expression, and potential regulatory mechanisms of arginine catabolism in Enterococcus faecalis, J Bacteriol, 184, 6289, 10.1128/JB.184.22.6289-6300.2002 · DOI
  3. Benga, 2004, Non-encapsulated strains reveal novel insights in invasion and survival of Streptococcus suis in epithelial cells, Cell Microbiol, 6, 867, 10.1111/j.1462-5822.2004.00409.x · DOI
  4. Blakemore, 1976, Arginine catabolism by Treponema denticola, J Bacteriol, 128, 616, 10.1128/JB.128.2.616-622.1976 · DOI
  5. Braunstein, 1993, Transcriptional silencing in yeast is associated with reduced nucleosome acetylation, Genes Dev, 7, 592, 10.1101/gad.7.4.592 · DOI
  6. Broman, 1978, Oxygen and nitrate in utilization by Bacillus licheniformis of the arginase and arginine deiminase routes of arginine catabolism and other factors affecting their syntheses, J Bacteriol, 135, 920, 10.1128/JB.135.3.920-927.1978 · DOI
  7. Burne, 1989, Cloning and expression in Escherichia coli of the genes of the arginine deiminase system of Streptococcus sanguis NCTC 10904, Infect Immun, 57, 3540, 10.1128/IAI.57.11.3540-3548.1989 · DOI
  8. Caldara, 2006, The arginine regulon of Escherichia coli : whole-system transcriptome analysis discovers new genes and provides an integrated view of arginine regulation, Microbiology, 152, 3343, 10.1099/mic.0.29088-0 · DOI
  9. Champomier Vergès, M. C., Zuñiga, 1999, Relationships between arginine degradation, pH and survival in Lactobacillus sakei, FEMS Microbiol Lett, 180, 297, 10.1111/j.1574-6968.1999.tb08809.x · DOI
  10. Chanter, 1993, Meningitis in pigs caused by Streptococcus suis – a speculative review, Vet Microbiol, 36, 39, 10.1016/0378-1135(93)90127-S · DOI
  11. Chaussee, 2003, Rgg coordinates virulence factor synthesis and metabolism in Streptococcus pyogenes, J Bacteriol, 185, 6016, 10.1128/JB.185.20.6016-6024.2003 · DOI
  12. Cherney, 2008, Crystal structure of the arginine repressor protein in complex with the DNA operator from Mycobacterium tuberculosis, J Mol Biol, 384, 1330, 10.1016/j.jmb.2008.10.015 · DOI
  13. Clifton-Hadley, 1980, The carrier site and carrier rate of Streptococcus suis type II in pigs, Vet Rec, 107, 40, 10.1136/vr.107.2.40 · DOI
  14. Crow, 1982, Arginine metabolism in lactic streptococci, J Bacteriol, 150, 1024, 10.1128/JB.150.3.1024-1032.1982 · DOI
  15. Dong, 2004, Control of expression of the arginine deiminase operon of Streptococcus gordonii by CcpA and Flp, J Bacteriol, 186, 2511, 10.1128/JB.186.8.2511-2514.2004 · DOI
  16. Floderus, 1990, Arginine catabolism by strains of oral streptococci, APMIS, 98, 1045, 10.1111/j.1699-0463.1990.tb05033.x · DOI
  17. Gardan, 1995, Expression of the rocDEF operon involved in arginine catabolism in Bacillus subtilis, J Mol Biol, 249, 843, 10.1006/jmbi.1995.0342 · DOI
  18. Garnett, 2008, Structure and function of the arginine repressor–operator complex from Bacillus subtilis, J Mol Biol, 379, 284, 10.1016/j.jmb.2008.03.007 · DOI
  19. Gottschalk, 2010, Streptococcus suis : a new emerging or an old neglected zoonotic pathogen?, Future Microbiol, 5, 371, 10.2217/fmb.10.2 · DOI
  20. Grandori, 1995, The DNA-binding domain of the hexameric arginine repressor, J Mol Biol, 254, 150, 10.1006/jmbi.1995.0607 · DOI
  21. Gruening, 2006, Structure, regulation, and putative function of the arginine deiminase system of Streptococcus suis, J Bacteriol, 188, 361, 10.1128/JB.188.2.361-369.2006 · DOI
  22. Hashim, 2004, The arginine regulatory protein mediates repression by arginine of the operons encoding glutamate synthase and anabolic glutamate dehydrogenase in Pseudomonas aeruginosa, J Bacteriol, 186, 3848, 10.1128/JB.186.12.3848-3854.2004 · DOI
  23. Hernández-Flores, 2004, The global arginine regulator ArgR controls expression of argF in Pseudomonas syringae pv. phaseolicola but is not required for the synthesis of phaseolotoxin or for the regulated expression of argK, J Bacteriol, 186, 3653, 10.1128/JB.186.11.3653-3655.2004 · DOI
  24. Hoffmann, 2008, Transcriptional regulation of EGR-1 by the interleukin-1-JNK-MKK7-c-Jun pathway, J Biol Chem, 283, 12120, 10.1074/jbc.M800583200 · DOI
  25. Kiupakis, 2002, ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli, J Bacteriol, 184, 2940, 10.1128/JB.184.11.2940-2950.2002 · DOI
  26. Klingel, 1995, A binding-site for activation by the Bacillus subtilis AhrC protein, a repressor activator of arginine metabolism, Mol Gen Genet, 248, 329, 10.1007/BF02191600 · DOI
  27. Larsen, 2004, ArgR and AhrC are both required for regulation of arginine metabolism in Lactococcus lactis, J Bacteriol, 186, 1147, 10.1128/JB.186.4.1147-1157.2004 · DOI
  28. Larsen, 2005, Interaction between ArgR and AhrC controls regulation of arginine metabolism in Lactococcus lactis, J Biol Chem, 280, 19319, 10.1074/jbc.M413983200 · DOI
  29. Larsen, 2008, Transcriptome analysis of the Lactococcus lactis ArgR and AhrC regulons, Appl Environ Microbiol, 74, 4768, 10.1128/AEM.00117-08 · DOI
  30. Liu, 2008, Environmental and growth phase regulation of the Streptococcus gordonii arginine deiminase genes, Appl Environ Microbiol, 74, 5023, 10.1128/AEM.00556-08 · DOI
  31. Lu, 1999, Role of ArgR in activation of the ast operon, encoding enzymes of the arginine succinyltransferase pathway in Salmonella typhimurium, J Bacteriol, 181, 1934, 10.1128/JB.181.6.1934-1938.1999 · DOI
  32. Lu, 2004, Transcriptome analysis of the ArgR regulon in Pseudomonas aeruginosa, J Bacteriol, 186, 3855, 10.1128/JB.186.12.3855-3861.2004 · DOI
  33. Maas, 1994, The arginine repressor of Escherichia coli, Microbiol Rev, 58, 631, 10.1128/MMBR.58.4.631-640.1994 · DOI
  34. Maghnouj, 1998, The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis , and its activation by the arginine repressor argR, J Bacteriol, 180, 6468, 10.1128/JB.180.24.6468-6475.1998 · DOI
  35. Maghnouj, 2000, Regulation of anaerobic arginine catabolism in Bacillus licheniformis by a protein of the Crp/Fnr family, FEMS Microbiol Lett, 191, 227, 10.1111/j.1574-6968.2000.tb09344.x · DOI
  36. Makarova, 2001, Conservation of the binding site for the arginine repressor in all bacterial lineages, Genome Biol, 2, RESEARCH0013, 10.1186/gb-2001-2-4-research0013 · DOI
  37. Mercenier, 1980, Catabolism of l-arginine by Pseudomonas aeruginosa, J Gen Microbiol, 116, 381
  38. Münch, 2005, Virtual footprint and PRODORIC: an integrative framework for regulon prediction in prokaryotes, Bioinformatics, 21, 4187, 10.1093/bioinformatics/bti635 · DOI
  39. Park, 1997, Cloning and characterization of argR , a gene that participates in regulation of arginine biosynthesis and catabolism in Pseudomonas aeruginosa PAO1, J Bacteriol, 179, 5300, 10.1128/JB.179.17.5300-5308.1997 · DOI
  40. Rimmele, 1994, Trehalose-6-phosphate hydrolase of Escherichia coli, J Bacteriol, 176, 5654, 10.1128/JB.176.18.5654-5664.1994 · DOI
  41. Rosenkranz, 2003, Streptococcus suis meningitis and septicemia contracted from a wild boar in Germany, J Neurol, 250, 869, 10.1007/s00415-003-1103-3 · DOI
  42. Ryan, 2009, Molecular characterization of the arginine deiminase system in Listeria monocytogenes : regulation and role in acid tolerance, Environ Microbiol, 11, 432, 10.1111/j.1462-2920.2008.01782.x · DOI
  43. Sambrook, 1989, Molecular Cloning: a Laboratory Manual
  44. Saulnier, 2007, Identification of prebiotic fructooligosaccharide metabolism in Lactobacillus plantarum WCFS1 through microarrays, Appl Environ Microbiol, 73, 1753, 10.1128/AEM.01151-06 · DOI
  45. Smith, 1995, High-efficiency transformation and gene inactivation in Streptococcus suis type-2, Microbiology, 141, 181, 10.1099/00221287-141-1-181 · DOI
  46. Smith, 1999, Identification and characterization of the cps locus of Streptococcus suis serotype 2: the capsule protects against phagocytosis and is an important virulence factor, Infect Immun, 67, 1750, 10.1128/IAI.67.4.1750-1756.1999 · DOI
  47. van den Hoff, 1995, Evolutionary relationships of the carbamoylphosphate synthetase genes, J Mol Evol, 41, 813, 10.1007/BF00173161 · DOI
  48. Willemoës, 2005, Nucleoside triphosphate synthesis catalysed by adenylate kinase is ADP dependent, Arch Biochem Biophys, 444, 195, 10.1016/j.abb.2005.10.003 · DOI
  49. Winterhoff, 2002, 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, J Bacteriol, 184, 6768, 10.1128/JB.184.24.6768-6776.2002 · DOI
  50. Zeng, 2006, Characterization of cis -acting sites controlling arginine deiminase gene expression in Streptococcus gordonii, J Bacteriol, 188, 941, 10.1128/JB.188.3.941-949.2006 · DOI
  51. Zuñiga, 2002a, The product of arcR , the sixth gene of the arc operon of Lactobacillus sakei , is essential for expression of the arginine deiminase pathway, Appl Environ Microbiol, 68, 6051, 10.1128/AEM.68.12.6051-6058.2002 · DOI
  52. Zuñiga, 2002b, Evolution of arginine deiminase (ADI) pathway genes, Mol Phylogenet Evol, 25, 429, 10.1016/S1055-7903(02)00277-4 · DOI

Cited by

Sorted by citations

See all 70

Metadata

Authors
Fulde, M., Willenborg, J., de Greeff, A., Benga, L., Smith, H. E., Valentin-Weigand, P., & Goethe, R.
Affiliations
  • Institut für Mikrobiologie, Zentrum für Infektionsmedizin, Stiftung Tierärztliche Hochschule Hannover, 30173 Hannover, Germany
  • Animal Sciences Group (ASG), Wageningen UR, PO Box 65, 8200 AB Lelystad, The Netherlands
Venue
Microbiology
Publisher
Microbiology Society
Published
2011-02-01
Volume
157
Issue
2
Pages
572-582
ISSN
  • 1350-0872
  • 1465-2080
DOI
10.1099/mic.0.043067-0
Cited by
70
References
0
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: ArgR is an essential local transcriptional regulator of the arcABC operon in Streptococcus suis and is crucial for biological fitness in an acidic environment. https://app.cochat.ai/papers/10.1099/mic.0.043067-0
The paper
Fulde, M., Willenborg, J., de Greeff, A., Benga, L., Smith, H. E., Valentin-Weigand, P., & Goethe, R. (2011). ArgR is an essential local transcriptional regulator of the arcABC operon in Streptococcus suis and is crucial for biological fitness in an acidic environment. Microbiology. https://doi.org/10.1099/mic.0.043067-0