Characterization of the role of the divalent metal ion-dependent transcriptional repressor MntR in the virulence of Staphylococcus aureus

Infection and Immunity

Volumn 71, Issue 5, 2003, Pages 2584-2590

  Ando, Masaru ^a,e   Manabe, Yukari C ^a,b   Converse, Paul J ^b   Miyazaki, Eishi ^a,e   Harrison, Robert ^d   Murphy, John R ^c   Bishai, William R ^a,b  

^a JOHNS HOPKINS BLOOMBERG SCHOOL OF PUBLIC HEALTH   (United States)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d Advanced Microbial Solutions   (United States)

^e OITA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; BACTERIAL PROTEIN; DIPHTHERIA TOXIN; GENE PRODUCT; IRON; MANGANESE; METAL ION; MUTANT PROTEIN; PROTEIN DTXR; PROTEIN MNTR; PROTEIN SIRR; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BACTERIAL GENETICS; BACTERIAL STRAIN; BACTERIAL VIRULENCE; BACTERIUM ISOLATION; CONTROLLED STUDY; CORYNEBACTERIUM; DNA GEL BLOT ANALYSIS; GENE EXPRESSION; GENETIC CODE; GENETIC TRANSCRIPTION; IN VIVO STUDY; MALE; MOUSE; NONHUMAN; OPERATOR GENE; OPERON; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FAMILY; SEQUENCE HOMOLOGY; SKIN ABSCESS; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS EPIDERMIDIS; TRANSCRIPTION REGULATION; WILD TYPE;

ABSCESS; ANIMALS; BACTERIAL PROTEINS; BASE SEQUENCE; DNA-BINDING PROTEINS; IRON; MALE; MANGANESE; MICE; MICE, INBRED HRS; MOLECULAR SEQUENCE DATA; PROMOTER REGIONS (GENETICS); REPRESSOR PROTEINS; SKIN DISEASES, BACTERIAL; STAPHYLOCOCCUS AUREUS; VIRULENCE;

EID: 0037407505     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.71.5.2584-2590.2003     Document Type: Article

References (40)

1. Boyd, J., M. N. Oza, and J. R. Murphy. 1990. Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae. Proc. Natl. Acad. Sci. USA 87:5968-5972.
2. Bunce, C., L. Wheeler, G. Reed, J. Musser, and N. Barg. 1992. Murine model of cutaneous infection with gram-positive cocci. Infect. Immun. 60:2636-2640.
3. Burnette-Curley, D., V. Wells, H. Viscount, C. L. Munro, J. C. Fenno, P. Fives-Taylor, and F. L. Macrina. 1995. FimA, a major virulence factor associated with Streptococcus parasanguis endocarditis. Infect. Immun. 63:4669-4674.
4. Chan, P. F., S. J. Foster, E. Ingham, and M. O. Clements. 1998. The Staphylococcus aureus alternative sigma factor sigmaB controls the environmental stress response but not starvation survival or pathogenicity in a mouse abscess model. J. Bacteriol. 180:6082-6089.
5. Cohen, M. L. 1992. Epidemiology of drug resistance: implications for a post-antimicrobial era. Science 257:1050-1055.
6. Dussurget, O., M. Rodriguez, and I. Smith. 1996. An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response. Mol. Microbiol. 22:535-544.
7. Guerinot, M. L. 1994. Microbial iron transport. Annu. Rev. Microbiol. 48:743-772.
8. Gunter-Seeboth, K., and T. Schupp. 1995. Cloning and sequence analysis of the Corynebacterium diphtheriae dtxR homologue from Streptomyces lividans and S. pilosus encoding a putative iron repressor protein. Gene 166:117-119.
9. Hardham, J. M., L. V. Stamm, S. F. Porcella, J. G. Frye, N. Y. Barnes, J. K. Howell, S. L. Mueller, J. D. Radolf, G. M. Weinstock, and S. J. Norris. 1997. Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog. Gene 197:47-64.
10. Hayashi, S., and H. C. Wu. 1990. Lipoproteins in bacteria. J. Bioenerg. Biomembr. 22:451-471.
11. Hill, P. J., A. Cockayne, P. Landers, J. A. Morrissey, C. M. Sims, and P. Williams. 1998. SirR, a novel iron-dependent repressor in Staphylococcus epidermidis. Infect. Immun. 66:4123-4129.
12. Horsburgh, M. J., S. J. Wharton, A. G. Cox, E. Ingham, S. Peacock, and S. J. Foster. 2002. MntR modulates expression of the PerR regulon and superoxide resistance in Staphylococcus aureus through control of manganese uptake. Mol. Microbiol. 44:1269-1286.
13. Kitten, T., C. L. Munro, S. M. Michalek, and F. L. Macrina. 2000. Genetic characterization of a Streptococcus mutans Lra1 family operon and role in virulence. Infect. Immun. 68:4441-4451.
14. Lee, J. H., T. Wang, K. Ault, J. Liu, M. P. Schmitt, and R. K. Holmes. 1997. Identification and characterization of three new promoter/operators from Cocynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and iron. Infect. Immun. 65:4273-4280.
15. Lindsay, J. A., and T. V. Riley. 1994. Staphylococcal iron requirements, siderophore production, and iron-regulated protein expression. Infect. Immun. 62:2309-2314.
16. Lowy, F. D. 1998. Staphylococcus aureus infections. N. Engl. J. Med. 339:520-532.
17. Manabe, Y. C., B. J. Saviola, L. Sun, J. R. Murphy, and W. R. Bishai. 1999. Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor. Proc. Natl. Acad. Sci. USA 96:12844-12848.
18. Novick, R. P., I. Edelman, and S. Lofdahl. 1956. Small Staphylococcus aureus plasmids are transduced as linear multimers that are formed and resolved by replicative processes. J. Mol. Biol. 192:209-220.
19. Oguiza, J. A., X. Tao, A. T. Marcos, J. F. Martin, and J. R. Murphy. 1995. Molecular cloning, DNA sequence analysis, and characterization of the Corynebacterium diphtheriae dtxR homolog from Brevibacterium lactofennentum. J. Bacteriol. 177:465-467.
20. Pappenheimer, A. M., Jr. 1977. Diphtheria toxin. Annu. Rev. Biochem. 46:69-94.
21. Saraste, M., P. R. Sibbald, and A. Wittinghofer. 1990. The P-loop-a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15:430-434.
22. Schenk, S., and R. A. Laddaga. 1992. Improved method for electroporation of Staphylococcus aureus. FEMS Microbiol. Lett. 73:133-138.
23. Schindler, C. A., and V. T. Schuhardt. 1964. Lysostaphin: a new bacteriolytic agent for the staphylococcus. Proc. Natl. Acad. Sci. USA 51:414-421.
24. Schmitt, M. P. 1997. Transcription of the Corynebacterium diphtheriae hmuO gene is regulated by iron and heme. Infect. Immun. 65:4634-4641.
25. Schmitt, M. P. 1997. Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin. J. Bacteriol. 179:838-845.
26. Schmitt, M. P., and R. K. Holmes. 1994. Cloning, sequence, and footprint analysis of two promoter/operators from Cornebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and iron. J. Bacteriol. 176:1141-1149.
27. Schmitt, M. P., and R. K. Holmes. 1991. Iron-dependent regulation of diphtheria toxin and siderophore expression by the cloned Cornebacterium diphtheriae repressor gene dtxR in C. diphtheriae C7 strains. Infect. Immun. 59:1899-1904.
28. Schmitt, M. P., M. Predich, L. Doukhan, I. Smith, and R. K. Holmes. 1995. Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae. Infect. Immun. 63:4284-4289.
29. Schmitt, M. P., B. G. Talley, and R. K. Holmes. 1997. Characterization of lipoprotein IRP1 from Cornebacterium diphtheriae, which is regulated by the diphtheria toxin repressor (DtxR) and iron. Infect. Immun. 65:5364-5367.
30. Sheagren, J. N. 1984. Staphylococcus aureus. The persistent pathogen (first of two parts). N. Engl. J. Med. 310:1368-1373.
31. Sun, L., J. vanderSpek, and J. R. Murphy. 1998. Isolation and characterization of iron-independent positive dominant mutants of the diphtheria toxin repressor DtxR. Proc. Natl. Acad. Sci. USA 95:14985-14990.
32. Tai, S. P., A. E. Krafft, P. Nootheti, and R. K. Holmes. 1990. Coordinate regulation of siderophore and diphtheria toxin production by iron in Colynebacterium diphtheriae. Microb. Pathog. 9:267-273.
33. Tao, X., J. Boyd, and J. R. Murphy. 1992. Specific binding of the diphtheria tox regulatory element DtxR to the tox operator requires divalent heavy metal ions and a 9-base-pair interrupted palindromic sequence. Proc. Natl. Acad. Sci. USA 89:5897-5901.
34. Tao, X., and J. R. Murphy. 1993. Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR. Proc. Natl. Acad. Sci. USA 90:8524-8528.
35. Tao, X., H. Y. Zeng, and J. R. Murphy. 1993. Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers. Proc. Natl. Acad. Sci. USA 92:6803-6807.
36. Trivier, D., and R. J. Courcol. 1996. Iron depletion and virulence in Staphylococcus aureus. FEMS Microbiol. Lett. 141:117-127.
37. Twigg, P. D., G. Parthasarathy, L. Guerrero, T. M. Logan, and D. L. D. Caspar. 2001. Disordered to ordered folding in the regulation of diphtheria toxin repressor activity. Proc. Natl. Acad. Sci. USA 98:11259-11264.
38. Uchida, T., D. M. Gill, and A. M. Pappenheimer, Jr. 1971. Mutation in the structural gene for diphtheria toxin carried by temperate phage. Nat. New Biol. 233:8-11
39. van Schie, R. C., S. A. Marras, J. M. Conroy, N. J. Nowak, J. J. Catanese, and P. J. de Jong. 2000. Semiautomated clone verification by real-time PCR using molecular beacons. BioTechniques 29:1296-1306.
40. Wilkinson, B. J. 1997. Biology, p. 1-38. In K. B. Crossley and G. L. Archer (ed.), The staphylococci in human disease. Churchill Livingstone, New York, N.Y.