Quantitative proteomic view associated with resistance to clinically important antibiotics in Gram-positive bacteria: A systematic review

Frontiers in Microbiology

Volumn 6, Issue JUL, 2015, Pages

  Lee, Chang Ro ^a   Lee, Jung Hun ^a   Park, Kwang Seung ^a   Jeong, Byeong Chul ^a   Lee, Sang Hee ^a  

^a Myong Ji University   (South Korea)

Author keywords

Daptomycin resistance; Linezolid resistance; Methicillin resistance; Quantitative proteomics; Vancomycin resistance

Indexed keywords

COLD SHOCK PROTEIN; DAPTOMYCIN; LINEZOLID; METICILLIN; VANCOMYCIN;

ANTIBIOTIC RESISTANCE; BACTERIAL STRAIN; BACTERIAL VIRULENCE; DNA MICROARRAY; GRAM POSITIVE BACTERIUM; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; NONHUMAN; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEOMICS; REVIEW; SYSTEMATIC REVIEW; TRANSCRIPTOMICS; UPREGULATION; VANCOMYCIN RESISTANT ENTEROCOCCUS;

BACTERIA (MICROORGANISMS); ENTEROCOCCUS; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; POSIBACTERIA;

EID: 84938916902     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2015.00828     Document Type: Review

References (90)

1. Ament, P. W., Jamshed N., Horne J. P. (2002). Linezolid: its role in the treatment of gram-positive, drug572 resistant bacterial infections. Am. Fam. Physician. 65, 663-670.
2. Baltz, R. H. (2009). Daptomycin: mechanisms of action and resistance, and biosynthetic engineering. Curr. Opin. Chem. Biol. 13, 144-151. doi: 10.1016/j.cbpa.2009.02.031.
3. Berger-Bachi, B., Barberis-Maino L., Strassle A., Kayser F. H. (1989). FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: molecular cloning and characterization. Mol. Gen. Genet. 219, 263-269.
4. Bernardo, K., Pakulat N., Fleer S., Schnaith A., Utermohlen O., Krut O. et al. (2004). Subinhibitory concentrations of linezolid reduce Staphylococcus aureus virulence factor expression. Antimicrob. Agents Chemother. 48, 546-555.
5. Besier, S., Ludwig A., Zander J., Brade V., Wichelhaus T. A. (2008). Linezolid resistance in Staphylococcus aureus: gene dosage effect, stability, fitness costs, and cross-resistances. Antimicrob. Agents Chemother. 52, 1570-1572. doi: 10.1128/AAC.01098-07.
6. Bischoff, M., Berger-Bachi B. (2001). Teicoplanin stress-selected mutations increasing sB activity in Staphylococcus aureus. Antimicrob. Agents Chemother. 45, 1714-1720. doi: 10.1128/AAC.45.6.1714-1720.2001.
7. Boyle-Vavra, S., Yin S., Daum R. S. (2006). The VraS/VraR two-component regulatory system required for oxacillin resistance in community-acquired methicillin-resistant Staphylococcus aureus. FEMS Microbiol. Lett. 262, 163-171. doi: 10.1111/j.1574-6968.2006.00384.x.
8. Boyle-Vavra, S., Yin S., Jo D. S., Montgomery C. P., Daum R. S. (2013). VraT/YvqF is required for methicillin resistance and activation of the VraSR regulon in Staphylococcus aureus. Antimicrob. Agents Chemother. 57, 83-95. doi: 10.1128/AAC.01651-12.
9. Buntaran, L., Hatta M., Sultan A. R., Dwiyanti R., Sabir M. (2013). Sccmec type II gene is common among clinical isolates of methicillin-resistant Staphylococcus aureus in Jakarta, Indonesia. BMC Res. Notes. 6, 110. doi: 10.1186/1756-0500-6-110.
10. Byrgazov, K., Vesper O., Moll I. (2013). Ribosome heterogeneity: another level of complexity in bacterial translation regulation. Curr. Opin. Microbiol. 16, 133-139. doi: 10.1016/j.mib.2013.01.009.
11. Chambers, H. F. (1997). Methicillin resistance in staphylococci: molecular and biochemical basis and clinical implications. Clin. Microbiol. Rev. 10, 781-791.
12. Chen, H., Liu Y., Zhao C., Xiao D., Zhang J., Zhang F. et al. (2013). Comparative proteomics-based identification of genes associated with glycopeptide resistance in clinically derived heterogeneous vancomycin-intermediate Staphylococcus aureus strains. PLoS One. 8, e66880. doi: 10.1371/journal.pone.0066880.
13. Cordwell, S. J., Larsen M. R., Cole R. T., Walsh B. J. (2002). Comparative proteomics of Staphylococcus aureus and the response of methicillin-resistant and methicillin-sensitive strains to Triton X-100. Microbiology. 148, 2765-2781.
14. Cosgrove, K., Coutts G., Jonsson I. M., Tarkowski A., Kokai-Kun J. F., Mond J. J. et al. (2007). Catalase (KatA) and alkyl hydroperoxide reductase (AhpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence, and nasal colonization in Staphylococcus aureus. J. Bacteriol. 189, 1025-1035. doi: 10.1128/JB.01524-06.
15. Courvalin, P. (2005). Genetics of glycopeptide resistance in gram-positive pathogens. Int. J. Med. Microbiol. 294, 479-486. doi: 10.1016/j.ijmm.2004.10.002.
16. Cuaron, J. A., Dulal S., Song Y., Singh A. K., Montelongo C. E., Yu W. et al. (2013). Tea tree oil-induced transcriptional alterations in Staphylococcus aureus. Phytother. Res. 27, 390-396. doi: 10.1002/ptr.4738.
17. Cui, L., Lian J. Q., Neoh H. M., Reyes E., Hiramatsu K. (2005). DNA microarray-based identification of genes associated with glycopeptide resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 49, 3404-3413. doi: 10.1128/AAC.49.8.3404-3413.2005.
18. Delaune, A., Poupel O., Mallet A., Coic Y. M., Msadek T., Dubrac S. (2011). Peptidoglycan crosslinking relaxation plays an important role in Staphylococcus aureus WalKR-dependent cell viability. PLoS One. 6, e17054. doi: 10.1371/journal.pone.0017054.
19. Dengler, V., Meier P. S., Heusser R., Berger-Bachi B., McCallum N. (2011). Induction kinetics of the Staphylococcus aureus cell wall stress stimulon in response to different cell wall active antibiotics. BMC Microbiol. 11, 16. doi: 10.1186/1471-2180-11-16.
20. Drummelsmith, J., Winstall E., Bergeron M. G., Poirier G. G., Ouellette M. (2007). Comparative proteomics analyses reveal a potential biomarker for the detection of vancomycin-intermediate Staphylococcus aureus strains. J. Proteome Res. 6, 4690-4702. doi: 10.1021/pr070521m.
21. Enany, S., Yoshida Y., Yamamoto T. (2014). Exploring extra-cellular proteins in methicillin susceptible and methicillin resistant Staphylococcus aureus by liquid chromatography-tandem mass spectrometry. World J. Microbiol. Biotechnol. 30, 1269-1283. doi: 10.1007/s11274-013-1550-7.
22. Fan, X., Liu Y., Smith D., Konermann L., Siu K. W., Golemi-Kotra D. (2007). Diversity of penicillin-binding proteins. Resistance factor FmtA of Staphylococcus aureus. J. Biol. Chem. 282, 35143-35152. doi: 10.1074/jbc.M706296200.
23. Feng, J., Billal D. S., Lupien A., Racine G., Winstall E., Legare D. et al. (2011). Proteomic and transcriptomic analysis of linezolid resistance in Streptococcus pneumoniae. J. Proteome Res. 10, 4439-4452. doi: 10.1021/pr200221s.
24. Fischer, A., Yang S. J., Bayer A. S., Vaezzadeh A. R., Herzig S., Stenz L. et al. (2011). Daptomycin resistance mechanisms in clinically derived Staphylococcus aureus strains assessed by a combined transcriptomics and proteomics approach. J. Antimicrob. Chemother. 66, 1696-1711. doi: 10.1093/jac/dkr195.
25. Friedberg, E. C., Wagner R., Radman M. (2002). Specialized DNA polymerases, cellular survival, and the genesis of mutations. Science. 296, 1627-1630. doi: 10.1126/science.1070236.
26. Gardete, S., Wu S. W., Gill S., Tomasz A. (2006). Role of VraSR in antibiotic resistance and antibiotic-induced stress response in Staphylococcus aureus. Antimicrob. Agents Chemother. 50, 3424-3434. doi: 10.1128/AAC.00356-06.
27. Gov, Y., Borovok I., Korem M., Singh V. K., Jayaswal R. K., Wilkinson B. J. et al. (2004). Quorum sensing in Staphylococci is regulated via phosphorylation of three conserved histidine residues. J. Biol. Chem. 279, 14665-14672. doi: 10.1074/jbc.M311106200.
28. Hachmann, A. B., Angert E. R., Helmann J. D. (2009). Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin. Antimicrob. Agents Chemother. 53, 1598-1609. doi: 10.1128/AAC.01329-08.
29. Hanaki, H., Inaba Y., Sasaki K., Hiramatsu K. (1998). A novel method of detecting Staphylococcus aureus heterogeneously resistant to vancomycin (hetero-VRSA). Jpn. J. Antibiot. 51, 521-530.
30. Hao, H., Dai M., Wang Y., Huang L., Yuan Z. (2012). Key genetic elements and regulation systems in methicillin-resistant Staphylococcus aureus. Future Microbiol. 7, 1315-1329. doi: 10.2217/fmb.12.107.
31. Healy, V. L., Lessard I. A., Roper D. I., Knox J. R., Walsh C. T. (2000). Vancomycin resistance in enterococci: reprogramming of the D-Ala-D-Ala ligases in bacterial peptidoglycan biosynthesis. Chem. Biol. 7, R109-119.
32. Herrmann, D. J., Peppard W. J., Ledeboer N. A., Theesfeld M. L., Weigelt J. A., Buechel B. J. (2008). Linezolid for the treatment of drug-resistant infections. Expert Rev. Anti. Infect. Ther. 6, 825-848. doi: 10.1586/14787210.6.6.825.
33. Hessling, B., Bonn F., Otto A., Herbst F. A., Rappen G. M., Bernhardt J. et al. (2013). Global proteome analysis of vancomycin stress in Staphylococcus aureus. Int. J. Med. Microbiol. 303, 624-634. doi: 10.1016/j.ijmm.2013.08.014.
34. Hobbs, J. K., Miller K., O'Neill A. J., Chopra I. (2008). Consequences of daptomycin-mediated membrane damage in Staphylococcus aureus. J. Antimicrob. Chemother. 62, 1003-1008. doi: 10.1093/jac/dkn321.
35. Howden, B. P., Grayson M. L. (2006). Dumb and dumber-the potential waste of a useful antistaphylococcal agent: emerging fusidic acid resistance in Staphylococcus aureus. Clin. Infect. Dis. 42, 394-400. doi: 10.1086/499365.
36. Ippolito, J. A., Kanyo Z. F., Wang D., Franceschi F. J., Moore P. B., Steitz T. A. et al. (2008). Crystal structure of the oxazolidinone antibiotic linezolid bound to the 50S ribosomal subunit. J. Med. Chem. 51, 3353-3356. doi: 10.1021/jm800379d.
37. Joly, N., Engl C., Jovanovic G., Huvet M., Toni T., Sheng X. et al. (2010). Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. FEMS Microbiol. Rev. 34, 797-827. doi: 10.1111/j.1574-6976.2010.00240.x.
38. Jones, T., Yeaman M. R., Sakoulas G., Yang S. J., Proctor R. A., Sahl H. G. et al. (2008). Failures in clinical treatment of Staphylococcus aureus Infection with daptomycin are associated with alterations in surface charge, membrane phospholipid asymmetry, and drug binding. Antimicrob. Agents Chemother. 52, 269-278. doi: 10.1128/AAC.00719-07.
39. Jordan, S., Junker A., Helmann J. D., Mascher T. (2006). Regulation of LiaRS-dependent gene expression in bacillus subtilis: identification of inhibitor proteins, regulator binding sites, and target genes of a conserved cell envelope stress-sensing two-component system. J. Bacteriol. 188, 5153-5166. doi: 10.1128/JB.00310-06.
40. Jousselin, A., Renzoni A., Andrey D. O., Monod A., Lew D. P., Kelley W. L. (2012). The posttranslocational chaperone lipoprotein PrsA is involved in both glycopeptide and oxacillin resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 56, 3629-3640. doi: 10.1128/AAC.06264-11.
41. Katayama, Y., Zhang H. Z., Chambers H. F. (2004). PBP 2a mutations producing very-high-level resistance to ß-lactams. Antimicrob. Agents Chemother. 48, 453-459.
42. Koripella, R. K., Chen Y., Peisker K., Koh C. S., Selmer M., Sanyal S. (2012). Mechanism of elongation factor-G726 mediated fusidic acid resistance and fitness compensation in Staphylococcus aureus. J. Biol. Chem. 287, 30257-30267. doi: 10.1074/jbc.M112.378521.
43. Kuroda, M., Kuroda H., Oshima T., Takeuchi F., Mori H., Hiramatsu K. (2003). Two-component system VraSR positively modulates the regulation of cell-wall biosynthesis pathway in Staphylococcus aureus. Mol. Microbiol. 49, 807-821.
44. Kuroda, M., Kuwahara-Arai K., Hiramatsu K. (2000). Identification of the up-and down-regulated genes in vancomycin-resistant Staphylococcus aureus strains Mu3 and Mu50 by cDNA differential hybridization method. Biochem. Biophys. Res. Commun. 269, 485-490. doi: 10.1006/bbrc.2000.2277.
45. Lee, C. R., Cho I. H., Jeong B. C., Lee S. H. (2013). Strategies to minimize antibiotic resistance. Int. J. Environ. Res. Public Health. 10, 4274-4305. doi: 10.3390/ijerph10094274.
46. Lee, J. H., Bae I. K., Lee S. H. (2012). New definitions of extended-spectrum ß-lactamase conferring worldwide emerging antibiotic resistance. Med. Res. Rev. 32, 216-232. doi: 10.1002/med.20210.
47. Levine, D. P. (2006). Vancomycin: a history. Clin. Infect. Dis. 42 Suppl 1, S5-12. doi: 10.1086/491709.
48. Long, K. S., Vester B. (2012). Resistance to linezolid caused by modifications at its binding site on the ribosome. Antimicrob. Agents Chemother. 56, 603-612. doi: 10.1128/AAC.05702-11.
49. Lorenz, U., Lorenz B., Schmitter T., Streker K., Erck C., Wehland J. et al. (2011). Functional antibodies targeting IsaA of Staphylococcus aureus augment host immune response and open new perspectives for antibacterial therapy. Antimicrob. Agents Chemother. 55, 165-173. doi: 10.1128/AAC.01144-10.
50. Marcone, G. L., Beltrametti F., Binda E., Carrano L., Foulston L., Hesketh A. et al. (2010). Novel mechanism of glycopeptide resistance in the A40926 producer Nonomuraea sp. ATCC 39727. Antimicrob. Agents Chemother. 54, 2465-2472. doi: 10.1128/AAC.00106-10.
51. Matsuno, K., Sonenshein A. L. (1999). Role of SpoVG in asymmetric septation in Bacillus subtilis. J. Bacteriol. 181, 3392-3401.
52. McAleese, F., Wu S. W., Sieradzki K., Dunman P., Murphy E., Projan S. et al. (2006). Overexpression of genes of the cell wall stimulon in clinical isolates of Staphylococcus aureus exhibiting vancomycin-intermediate-S. aureus-type resistance to vancomycin. J. Bacteriol. 188, 1120-1133. doi: 10.1128/JB.188.3.1120-1133.2006.
53. Mehta, S., Cuirolo A. X., Plata K. B., Riosa S., Silverman J. A., Rubio A. et al. (2012). VraSR two-component regulatory system contributes to mprF-mediated decreased susceptibility to daptomycin in in vivo-selected clinical strains of methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 56, 92-102. doi: 10.1128/AAC.00432-10.
54. Mendes, R. E., Deshpande L. M., Jones R. N. (2014). Linezolid update: stable in vitro activity following more than a decade of clinical use and summary of associated resistance mechanisms. Drug Resist. Updat. 17, 1-12. doi: 10.1016/j.drup.2014.04.002.
55. Miao, V., Coeffet-Legal M. F., Brian P., Brost R., Penn J., Whiting A. et al. (2005). Daptomycin biosynthesis in Streptomyces roseosporus: cloning and analysis of the gene cluster and revision of peptide stereochemistry. Microbiology. 151, 1507-1523. doi: 10.1099/mic.0.27757-0.
56. Mishra, N. N., Yang S. J., Sawa A., Rubio A., Nast C. C., Yeaman M. R. et al. (2009). Analysis of cell membrane characteristics of in vitro-selected daptomycin-resistant strains of methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 53, 2312-2318. doi: 10.1128/AAC.01682-08.
57. Moher, D., Liberati A., Tetzlaff J., Altman D. G., Group P. (2009). Preferred reporting items for systematic reviews and meta-analyses: the PRISMA statement. PLoS Med. 6, e1000097. doi: 10.1371/journal.pmed.1000097.
58. Mongodin, E., Finan J., Climo M. W., Rosato A., Gill S., Archer G. L. (2003). Microarray transcription analysis of clinical Staphylococcus aureus isolates resistant to vancomycin. J. Bacteriol. 185, 4638-4643.
59. Muthaiyan, A., Silverman J. A., Jayaswal R. K., Wilkinson B. J. (2008). Transcriptional profiling reveals that daptomycin induces the Staphylococcus aureus cell wall stress stimulon and genes responsive to membrane depolarization. Antimicrob. Agents Chemother. 52, 980-990. doi: 10.1128/AAC.01121-07.
60. Napolitano, R., Janel-Bintz R., Wagner J., Fuchs R. P. (2000). All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis. EMBO J. 19, 6259-6265. doi: 10.1093/emboj/19.22.6259.
61. Newsom, S. W. (2004). MRSA-past, present, future. J. R. Soc. Med. 97, 509-510. doi: 10.1258/jrsm.97.11.509.
62. Perry, S. E., Edwards D. H. (2004). Identification of a polar targeting determinant for Bacillus subtilis DivIVA. Mol. Microbiol. 54, 1237-1249. doi: 10.1111/j.1365-2958.2004.04363.x.
63. Pieper, R., Gatlin-Bunai C. L., Mongodin E. F., Parmar P. P., Huang S. T., Clark D. J. et al. (2006). Comparative proteomic analysis of Staphylococcus aureus strains with differences in resistance to the cell wall-targeting antibiotic vancomycin. Proteomics. 6, 4246-4258. doi: 10.1002/pmic.200500764.
64. Pietiainen, M., Francois P., Hyyrylainen H. L., Tangomo M., Sass V., Sahl H. G. et al. (2009). Transcriptome analysis of the responses of Staphylococcus aureus to antimicrobial peptides and characterization of the roles of vraDE and vraSR in antimicrobial resistance. BMC Genomics. 10, 429. doi: 10.1186/1471-2164-10-429.
65. Pogliano, J., Pogliano N., Silverman J. A. (2012). Daptomycin-mediated reorganization of membrane architecture causes mislocalization of essential cell division proteins. J. Bacteriol. 194, 4494-4504. doi: 10.1128/JB.00011-12.
66. Radhouani, H., Pinto L., Poeta P., Igrejas G. (2012). After genomics, what proteomics tools could help us understand the antimicrobial resistance of Escherichia coli? J. Proteomics. 75, 2773-2789. doi: 10.1016/j.jprot.2011.12.035.
67. Ramos, S., Chafsey I., Silva N., Hebraud M., Santos H., Capelo-Martinez J. L. et al. (2015). Effect of vancomycin on the proteome of the multiresistant Enterococcus faecium SU18 strain. J. Proteomics. 113, 378-387. doi: 10.1016/j.jprot.2014.10.012.
68. Reyes, J., Panesso D., Tran T. T., Mishra N. N., Cruz M. R., Munita J. M. et al. (2015). A liaR Deletion Restores Susceptibility to Daptomycin and Antimicrobial Peptides in Multidrug-Resistant Enterococcus faecalis. J. Infect. Dis. 211, 1317-1325. doi: 10.1093/infdis/jiu602.
69. Rogers, P. D., Liu T. T., Barker K. S., Hilliard G. M., English B. K., Thornton J. et al. (2007). Gene expression profiling of the response of Streptococcus pneumoniae to penicillin. J. Antimicrob. Chemother. 59, 616-626. doi: 10.1093/jac/dkl560.
70. Sasindran, S. J., Saikolappan S., Dhandayuthapani S. (2007). Methionine sulfoxide reductases and virulence of bacterial pathogens. Future Microbiol. 2, 619-630. doi: 10.2217/17460913.2.6.619.
71. Sass, P., Jansen A., Szekat C., Sass V., Sahl H. G., Bierbaum G. (2008). The lantibiotic mersacidin is a strong inducer of the cell wall stress response of Staphylococcus aureus. BMC Microbiol. 8, 186. doi: 10.1186/1471-2180-8-186.
72. Scherl, A., Francois P., Charbonnier Y., Deshusses J. M., Koessler T., Huyghe A. et al. (2006). Exploring glycopeptide-resistance in Staphylococcus aureus: a combined proteomics and transcriptomics approach for the identification of resistance-related markers. BMC Genomics. 7, 296. doi: 10.1186/1471-2164-7-296.
73. Schulthess, B., Bloes D. A., Berger-Bachi B. (2012). Opposing roles of sB and sB-controlled SpoVG in the global regulation of esxA in Staphylococcus aureus. BMC Microbiol. 12, 17. doi: 10.1186/1471-2180-12-17.
74. Schulthess, B., Meier S., Homerova D., Goerke C., Wolz C., Kormanec J. et al. (2009). Functional characterization of the sB-dependent yabJ-spoVG operon in Staphylococcus aureus: role in methicillin and glycopeptide resistance. Antimicrob. Agents Chemother. 53, 1832-1839. doi: 10.1128/AAC.01255-08.
75. Schumacher, A., Trittler R., Bohnert J. A., Kummerer K., Pages J. M., Kern W. V. (2007). Intracellular accumulation of linezolid in Escherichia coli, Citrobacter freundii and Enterobacter aerogenes: role of enhanced efflux pump activity and inactivation. J. Antimicrob. Chemother. 59, 1261-1264. doi: 10.1093/jac/dkl380.
76. Seidl, K., Stucki M., Ruegg M., Goerke C., Wolz C., Harris L. et al. (2006). Staphylococcus aureus CcpA affects virulence determinant production and antibiotic resistance. Antimicrob. Agents Chemother. 50, 1183-1194. doi: 10.1128/AAC.50.4.1183-1194.2006.
77. Sobral, R. G., Jones A. E., Des Etages S. G., Dougherty T. J., Peitzsch R. M., Gaasterland T. et al. (2007). Extensive and genome-wide changes in the transcription profile of Staphylococcus aureus induced by modulating the transcription of the cell wall synthesis gene murF. J. Bacteriol. 189, 2376-2391. doi: 10.1128/JB.01439-06.
78. Song, Y., Rubio A., Jayaswal R. K., Silverman J. A., Wilkinson B. J. (2013). Additional routes to Staphylococcus aureus daptomycin resistance as revealed by comparative genome sequencing, transcriptional profiling, and phenotypic studies. PLoS One. 8, e58469. doi: 10.1371/journal.pone.0058469.
79. Stülke, J., Hillen W. (2000). Regulation of carbon catabolism in Bacillus species. Annu. Rev. Microbiol. 54, 849-880. doi: 10.1146/annurev.micro.54.1.849.
80. Stapleton, M. R., Horsburgh M. J., Hayhurst E. J., Wright L., Jonsson I. M., Tarkowski A. et al. (2007). Characterization of IsaA and SceD, two putative lytic transglycosylases of Staphylococcus aureus. J. Bacteriol. 189, 7316-7325. doi: 10.1128/JB.00734-07.
81. Swaney, S. M., Aoki H., Ganoza M. C., Shinabarger D. L. (1998). The oxazolidinone linezolid inhibits initiation of protein synthesis in bacteria. Antimicrob. Agents Chemother. 42, 3251-3255.
82. Tettelin, H., Nelson K. E., Paulsen I. T., Eisen J. A., Read T. D., Peterson S. et al. (2001). Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science. 293, 498-506. doi: 10.1126/science.1061217.
83. Utaida, S., Dunman P. M., Macapagal D., Murphy E., Projan S. J., Singh V. K. et al. (2003). Genome-wide transcriptional profiling of the response of Staphylococcus aureus to cell-wall-active antibiotics reveals a cell880 wall-stress stimulon. Microbiology. 149, 2719-2732.
84. van der Voort, M., Kuipers O. P., Buist G., de Vos W. M., Abee T. (2008). Assessment of CcpA-mediated catabolite control of gene expression in Bacillus cereus ATCC 14579. BMC Microbiol. 8, 62. doi: 10.1186/1471-2180-8-62.
85. Wang, X., He X., Jiang Z., Wang J., Chen X., Liu D. et al. (2010). Proteomic analysis of the Enterococcus faecalis V583 strain and clinical isolate V309 under vancomycin treatment. J. Proteome Res. 9, 1772-1785. doi: 10.1021/pr901216e.
86. Wecke, T., Zuhlke D., Mader U., Jordan S., Voigt B., Pelzer S. et al. (2009). Daptomycin versus Friulimicin B: in891 depth profiling of Bacillus subtilis cell envelope stress responses. Antimicrob. Agents Chemother. 53, 1619-1623. doi: 10.1128/AAC.01046-08.
87. Wilson, D. N., Schluenzen F., Harms J. M., Starosta A. L., Connell S. R., Fucini P. (2008). The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning. Proc. Natl. Acad. Sci. USA. 105, 13339-13344. doi: 10.1073/pnas.0804276105.
88. Winkler, M. E., Hoch J. A. (2008). Essentiality, bypass, and targeting of the YycFG (VicRK) two-component regulatory system in gram-positive bacteria. J. Bacteriol. 190, 2645-2648. doi: 10.1128/JB.01682-07.
89. Woodford, N. (1998). Glycopeptide-resistant enterococci: a decade of experience. J. Med. Microbiol. 47, 849-862.
90. Yin, S., Daum R. S., Boyle-Vavra S. (2006). VraSR two-component regulatory system and its role in induction of pbp2 and vraSR expression by cell wall antimicrobials in Staphylococcus aureus. Antimicrob. Agents Chemother. 50, 336-343. doi: 10.1128/AAC.50.1.336-343.2006.