Pseudomonas aeruginosa lifestyle: A paradigm for adaptation, survival, and persistence

Frontiers in Cellular and Infection Microbiology

Volumn 7, Issue FEB, 2017, Pages

  Moradali, M Fata ^a,b   Ghods, Shirin ^a   Rehm, Bernd H A ^a  

^a MASSEY UNIVERSITY   (New Zealand)

^b UNIVERSITY OF FLORIDA COLLEGE OF DENTISTRY   (United States)

Author keywords

Antibiotic resistance; Biofilm; Persistence; Pseudomonas aeruginosa; Virulence

Indexed keywords

ALDEHYDE; ALKALINE PROTEINASE; AMINOGLYCOSIDE ANTIBIOTIC AGENT; BACTERIAL TOXIN; CARBAPENEM; CEPHALOSPORIN; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; ELASTASE; EXOPOLYSACCHARIDE; GAMMA INTERFERON; HYDROGEN CYANIDE; LACTONE; LECTIN; PEPTIDES AND PROTEINS; PHENAZINE; PYOCYANINE; QUINOLINE DERIVED ANTIINFECTIVE AGENT; QUINOLONE; RHAMNOLIPID;

ADAPTIVE RADIATION; ANTIBIOTIC RESISTANCE; BACTERIAL MUTATION; BACTERIAL SURVIVAL; BACTERIAL TRANSMISSION; BACTERIAL VIRULENCE; CELL AGGREGATION; CELL DENSITY; CELL MOTILITY; CELLULAR STRESS RESPONSE; CYSTIC FIBROSIS; ENZYME ACTIVITY; EVOLUTIONARY ADAPTATION; GENE EXPRESSION; HOSPITAL INFECTION; HUMAN; HYPOXIA; IMMUNE RESPONSE; NONHUMAN; PATHOGENESIS; PHENOTYPE; PLASMID; PSEUDOMONAS AERUGINOSA; REVIEW; SIGNAL TRANSDUCTION; SYSTEMIC ACQUIRED RESISTANCE; UPREGULATION; ADAPTATION; GENETIC VARIATION; MICROBIAL VIABILITY; PHYSIOLOGICAL STRESS; PHYSIOLOGY;

ADAPTATION, BIOLOGICAL; ADAPTATION, PHYSIOLOGICAL; GENETIC VARIATION; MICROBIAL VIABILITY; PHENOTYPE; PSEUDOMONAS AERUGINOSA; STRESS, PHYSIOLOGICAL;

EID: 85014708437     PISSN: None     EISSN: 22352988     Source Type: Journal    
DOI: 10.3389/fcimb.2017.00039     Document Type: Review

References (340)

1. Aendekerk, S., Diggle, S. P., Song, Z., Høiby, N., Cornelis, P., Williams, P., et al. (2005). The MexGHI-OpmD multidrug efflux pump controls growth, antibiotic susceptibility and virulence in Pseudomonas aeruginosa via 4-quinolone-dependent cell-to-cell communication. Microbiology 151(Pt 4), 1113-1125. doi: 10.1099/mic.0.27631-0
2. Alcalde-Rico, M., Hernando-Amado, S., Blanco, P., and Martínez, J. L. (2016). Multidrug efflux pumps at the crossroad between antibiotic resistance and bacterial virulence. Front. Microbiol. 7:1483. doi: 10.3389/fmicb.2016.01483
3. Alhede, M., Bjarnsholt, T., Jensen, P. Ø., Phipps, R. K., Moser, C., Christophersen, L., et al. (2009). Pseudomonas aeruginosa recognizes and responds aggressively to the presence of polymorphonuclear leukocytes. Microbiology 155(Pt 11), 3500-3508. doi: 10.1099/mic.0.031443-0
4. Allesen-Holm, M., Barken, K. B., Yang, L., Klausen, M., Webb, J. S., Kjelleberg, S., et al. (2006). A characterization of DNA release in Pseudomonas aeruginosa cultures and biofilms. Mol. Microbiol. 59, 1114-1128. doi: 10.1111/j.1365-2958.2005.05008.x
5. Alvarez-Ortega, C., and Harwood, C. S. (2007). Responses of Pseudomonas aeruginosa to low oxygen indicate that growth in the cystic fibrosis lung is by aerobic respiration. Mol. Microbiol. 65, 153-165. doi: 10.1111/j.1365-2958.2007.05772.x
6. Amato, S. M., Fazen, C. H., Henry, T. C., Mok, W. W., Orman, M. A., Sandvik, E. L., et al. (2014). The role of metabolism in bacterial persistence. Front. Microbiol. 5:70. doi: 10.3389/fmicb.2014.00070
7. Amato, S. M., Orman, M. A., and Brynildsen, M. P. (2013). Metabolic control of persister formation in Escherichia coli. Mol. Cell 50, 475-487. doi: 10.1016/j.molcel.2013.04.002
8. Amiel, E., Lovewell, R. R., O'Toole, G. A., Hogan, D. A., and Berwin, B. (2010). Pseudomonas aeruginosa evasion of phagocytosis is mediated by loss of swimming motility and is independent of flagellum expression. Infect. Immun. 78, 2937-2945. doi: 10.1128/IAI.00144-10
9. Avrain, L., Mertens, P., and Van Bambeke, F. (2013). RND efflux pumps in P. aeruginosa: an underestimated resistance mechanism. Antibiot. Susceptibility 26321, 26-28. Available online at: http://www.uclouvain.be/cps/ucl/doc/ir-ldri/images/Avrain-2013-1.pdf
10. Ayers, M., Sampaleanu, L. M., Tammam, S., Koo, J., Harvey, H., Howell, P. L., et al. (2009). PilM/N/O/P proteins form an inner membrane complex that affects the stability of the pseudomonas aeruginosa type iv pilus secretin. J. Mol. Biol. 394, 128-142. doi: 10.1016/j.jmb.2009.09.034
11. Bains, M., Fernández, L., and Hancock, R. E. (2012). Phosphate starvation promotes swarming motility and cytotoxicity of Pseudomonas aeruginosa. Appl. Environ. Microbiol. 78, 6762-6768. doi: 10.1128/AEM.01015-12
12. Bajolet-Laudinat, O., Girod-de Bentzmann, S., Tournier, J. M., Madoulet, C., Plotkowski, M. C., Chippaux, C., et al. (1994). Cytotoxicity of Pseudomonas aeruginosa internal lectin PA-I to respiratory epithelial cells in primary culture. Infect. Immun. 62, 4481-4487.
13. Balasubramanian, D., Kong, K. F., Jayawardena, S. R., Leal, S. M., Sautter, R. T., and Mathee, K. (2011). Co-regulation of β-lactam resistance, alginate production and quorum sensing in Pseudomonas aeruginosa. J. Med. Microbiol. 60(Pt 2), 147-156. doi: 10.1099/jmm.0.021600-0
14. Balasubramanian, D., Kumari, H., Jaric, M., Fernandez, M., Turner, K. H., Dove, S. L., et al. (2014). Deep sequencing analyses expands the Pseudomonas aeruginosa AmpR regulon to include small RNA-mediated regulation of iron acquisition, heat shock and oxidative stress response. Nucleic Acids Res. 42, 979-998. doi: 10.1093/nar/gkt942
15. Balasubramanian, D., Kumari, H., and Mathee, K. (2015). Pseudomonas aeruginosa AmpR: an acute-chronic switch regulator. Pathog. Dis. 73, 1-14. doi: 10.1111/2049-632X.12208
16. Balasubramanian, D., Schneper, L., Merighi, M., Smith, R., Narasimhan, G., Lory, S., et al. (2012). The regulatory repertoire of Pseudomonas aeruginosa AmpC ss-lactamase regulator AmpR includes virulence genes. PLoS ONE 7:e34067. doi: 10.1371/journal.pone.0034067
17. Banerjee, G., and Ray, A. K. (2016). The talking language in some major Gram-negative bacteria. Arch. Microbiol. 198, 489-499. doi: 10.1007/s00203-016-1220-x
18. Baraquet, C., Murakami, K., Parsek, M. R., and Harwood, C. S. (2012). The FleQ protein from Pseudomonas aeruginosa functions as both a repressor and an activator to control gene expression from the pel operon promoter in response to c-di-GMP. Nucleic Acids Res. 40, 7207-7218. doi: 10.1093/nar/gks384
19. Barclay, M. L., Begg, E. J., and Chambers, S. T. (1992). Adaptive resistance following single doses of gentamicin in a dynamic in vitro model. Antimicrob. Agents Chemother. 36, 1951-1957. doi: 10.1128/AAC.36.9.1951
20. Barken, K. B., Pamp, S. J., Yang, L., Gjermansen, M., Bertrand, J. J., Klausen, M., et al. (2008). Roles of type IV pili, flagellum-mediated motility and extracellular DNA in the formation of mature multicellular structures in Pseudomonas aeruginosa biofilms. Environ. Microbiol. 10, 2331-2343. doi: 10.1111/j.1462-2920.2008.01658.x
21. Barker, A. P., Vasil, A. I., Filloux, A., Ball, G., Wilderman, P. J., and Vasil, M. L. (2004). A novel extracellular phospholipase C of Pseudomonas aeruginosa is required for phospholipid chemotaxis. Mol. Microbiol. 53, 1089-1098. doi: 10.1111/j.1365-2958.2004.04189.x
22. Barr, H. L., Halliday, N., Cámara, M., Barrett, D. A., Williams, P., Forrester, D. L., et al. (2015). Pseudomonas aeruginosa quorum sensing molecules correlate with clinical status in cystic fibrosis. Eur. Respir. J. 46, 1046-1054. doi: 10.1183/09031936.00225214
23. Barrow, K., and Kwon, D. H. (2009). Alterations in two-component regulatory systems of phoPQ and pmrAB are associated with polymyxin B resistance in clinical isolates of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 53, 5150-5154. doi: 10.1128/AAC.00893-09
24. Baumgart, A. M., Molinari, M. A., and Silveira, A. C. (2010). Prevalence of carbapenem resistant Pseudomonas aeruginosa and Acinetobacter baumannii in high complexity hospital. Braz. J. Infect. Dis. 14, 433-436. doi: 10.1590/S1413-86702010000500002
25. Bennett, P. M. (2008). Plasmid encoded antibiotic resistance: acquisition and transfer of antibiotic resistance genes in bacteria. Br. J. Pharmacol. 153(Suppl. 1), S347-357. doi: 10.1038/sj.bjp.0707607
26. Berrazeg, M., Jeannot, K., Ntsogo Enguene, V. Y., Broutin, I., Loeffert, S., Fournier, D., et al. (2015). Mutations in β-lactamase AmpC increase resistance of Pseudomonas aeruginosa isolates to antipseudomonal cephalosporins. Antimicrob. Agents Chemother. 59, 6248-6255. doi: 10.1128/AAC.00825-15
27. Bhaya, D., Davison, M., and Barrangou, R. (2011). CRISPR-Cas systems in bacteria and archaea: versatile small RNAs for adaptive defense and regulation. Annu. Rev. Genet. 45, 273-297. doi: 10.1146/annurev-genet-110410-132430
28. Billings, N., Millan, M., Caldara, M., Rusconi, R., Tarasova, Y., Stocker, R., et al. (2013). The extracellular matrix component Psl provides fast-acting antibiotic defense in Pseudomonas aeruginosa biofilms. PLoS Pathog. 9:e1003526. doi: 10.1371/journal.ppat.1003526
29. Bjarnsholt, T., Jensen, P. Ø., Jakobsen, T. H., Phipps, R., Nielsen, A. K., Rybtke, M. T., et al. (2010). Quorum sensing and virulence of Pseudomonas aeruginosa during lung infection of cystic fibrosis patients. PLoS ONE 5:e10115. doi: 10.1371/journal.pone.0010115
30. Blair, J. M., Webber, M. A., Baylay, A. J., Ogbolu, D. O., and Piddock, L. J. (2015). Molecular mechanisms of antibiotic resistance. Nat. Rev. Microbiol. 13, 42-51. doi: 10.1038/nrmicro3380
31. Blanka, A., Düvel, J., Dotsch, A., Klinkert, B., Abraham, W. R., Kaever, V., et al. (2015). Constitutive production of c-di-GMP is associated with mutations in a variant of Pseudomonas aeruginosa with altered membrane composition. Sci. Signal. 8:ra36. doi: 10.1126/scisignal.2005943
32. Blumer, C., and Haas, D. (2000). Mechanism, regulation, and ecological role of bacterial cyanide biosynthesis. Arch. Microbiol. 173, 170-177. doi: 10.1007/s002039900127
33. Boehm, A., Kaiser, M., Li, H., Spangler, C., Kasper, C. A., Ackermann, M., et al. (2010). Second messenger-mediated adjustment of bacterial swimming velocity. Cell 141, 107-116. doi: 10.1016/j.cell.2010.01.018
34. Boes, N., Schreiber, K., and Schobert, M. (2008). SpoT-triggered stringent response controls usp gene expression in Pseudomonas aeruginosa. J. Bacteriol. 190, 7189-7199. doi: 10.1128/JB.00600-08
35. Boles, B. R., and Singh, P. K. (2008). Endogenous oxidative stress produces diversity and adaptability in biofilm communities. Proc. Natl. Acad. Sci. U.S.A. 105, 12503-12508. doi: 10.1073/pnas.0801499105
36. Boles, B. R., Thoendel, M., and Singh, P. K. (2005). Rhamnolipids mediate detachment of Pseudomonas aeruginosa from biofilms. Mol. Microbiol. 57, 1210-1223. doi: 10.1111/j.1365-2958.2005.04743.x
37. Bondy-Denomy, J., and Davidson, A. R. (2014). To acquire or resist: the complex biological effects of CRISPR-Cas systems. Trends Microbiol. 22, 218-225. doi: 10.1016/j.tim.2014.01.007
38. Bondy-Denomy, J., Garcia, B., Strum, S., Du, M. J., Rollins, M. F., Hidalgo-Reyes, Y., et al. (2015). Multiple mechanisms for CRISPR-Cas inhibition by anti-CRISPR proteins. Nature 526, 136-139. doi: 10.1038/nature15254
39. Bondy-Denomy, J., Pawluk, A., Maxwell, K. L., and Davidson, A. R. (2013). Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system. Nature 493, 429-432. doi: 10.1038/nature11723
40. Breidenstein, E. B. M., Janot, L., Strehmel, J., Fernandez, L., Taylor, P. K., Kukavica-Ibrulj, I., et al. (2012). The Lon protease is essential for full virulence in Pseudomonas aeruginosa. PLoS ONE 7:e49123. doi: 10.1371/journal.pone.0049123
41. Bremer, H., and Dennis, P. P. (2008). Modulation of chemical composition and other parameters of the cell at different exponential growth rates. EcoSal Plus 3, 1-49. doi: 10.1128/ecosal.5.2.3
42. Britigan, B. E., Roeder, T. L., Rasmussen, G. T., Shasby, D. M., McCormick, M. L., and Cox, C. D. (1992). Interaction of the Pseudomonas aeruginosa secretory products pyocyanin and pyochelin generates hydroxyl radical and causes synergistic damage to endothelial cells-Implications for Pseudomonas associated tissue injury. J. Clin. Invest. 90, 2187-2196. doi: 10.1172/JCI116104
43. Brouns, S. J., Jore, M. M., Lundgren, M., Westra, E. R., Slijkhuis, R. J., Snijders, A. P., et al. (2008). Small CRISPR RNAs guide antiviral defense in prokaryotes. Science 321, 960-964. doi: 10.1126/science.1159689
44. Budzik, J. M., Rosche, W. A., Rietsch, A., and O'Toole, G. A. (2004). Isolation and characterization of a generalized transducing phage for Pseudomonas aeruginosa strains PAO1 and PA14. J. Bacteriol. 186, 3270-3273. doi: 10.1128/JB.186.10.3270-3273.2004
45. Burrows, L. L. (2012). Pseudomonas aeruginosa twitching motility: type IV pili in action. Annu. Rev. Microbiol. 66, 493-520. doi: 10.1146/annurev-micro-092611-150055
46. Byrd, M. S., Sadovskaya, I., Vinogradov, E., Lu, H., Sprinkle, A. B., Richardson, S. H., et al. (2009). Genetic and biochemical analyses of the Pseudomonas aeruginosa Psl exopolysaccharide reveal overlapping roles for polysaccharide synthesis enzymes in Psl and LPS production. Mol. Microbiol. 73, 622-638. doi: 10.1111/j.1365-2958.2009.06795.x
47. Cady, K. C., Bondy-Denomy, J., Heussler, G. E., Davidson, A. R., and O'Toole, G. A. (2012). The CRISPR/Cas adaptive immune system of Pseudomonas aeruginosa mediates resistance to naturally occurring and engineered phages. J. Bacteriol. 194, 5728-5738. doi: 10.1128/JB.01184-12
48. Cady, K. C., White, A. S., Hammond, J. H., Abendroth, M. D., Karthikeyan, R. S., Lalitha, P., et al. (2011). Prevalence, conservation and functional analysis of Yersinia and Escherichia CRISPR regions in clinical Pseudomonas aeruginosa isolates. Microbiology 157(Pt 2), 430-437. doi: 10.1099/mic.0.045732-0
49. Cai, Z., Liu, Y., Chen, Y., Yam, J. K., Chew, S. C., Chua, S. L., et al. (2015). RpoN regulates virulence factors of Pseudomonas aeruginosa via modulating the PqsR quorum sensing regulator. Int. J. Mol. Sci. 16, 28311-28319. doi: 10.3390/ijms161226103
50. Cardo, D., Horan, T., Andrus, M., Dembinski, M., Edwards, J., Peavy, G., et al. (2004). National nosocomial infections surveillance (NNIS) system report, data summary from January 1992 through June 2004, issued October 2004. Am. J. Infect. Control 32, 470-485. doi: 10.1016/j.ajic.2004.10.001
51. Castric, P. (1994). Influence of oxygen on the Pseudomonas aeruginosa hydrogen cyanide synthase. Curr. Microbiol. 29, 19-21. doi: 10.1007/BF01570186
52. Castric, P. A. (1975). Hydrogen cyanide, a secondary metabolite of Pseudomonas aeruginosa. Can. J. Microbiol. 21, 613-618. doi: 10.1139/m75-088
53. Castric, P. A. (1983). Hydrogen cyanide production by Pseudomonas aeruginosa at reduced oxygen levels. Can. J. Microbiol. 29, 1344-1349. doi: 10.1139/m83-209
54. Chemani, C., Imberty, A., de Bentzmann, S., Pierre, M., Wimmerová, M., Guery, B. P., et al. (2009). Role of LecA and LecB lectins in Pseudomonas aeruginosa-induced lung injury and effect of carbohydrate ligands. Infect. Immun. 77, 2065-2075. doi: 10.1128/IAI.01204-08
55. Chen, L., Zou, Y., She, P., and Wu, Y. (2015). Composition, function, and regulation of T6SS in Pseudomonas aeruginosa. Microbiol. Res. 172, 19-25. doi: 10.1016/j.micres.2015.01.004
56. Choi, Y., Park, H. Y., Park, S. J., Park, S. J., Kim, S. K., Ha, C., et al. (2011). Growth phase-differential quorum sensing regulation of anthranilate metabolism in Pseudomonas aeruginosa. Mol. Cells 32, 57-65. doi: 10.1007/s10059-011-2322-6
57. Christensen, S. K., Mikkelsen, M., Pedersen, K., and Gerdes, K. (2001). RelE, a global inhibitor of translation, is activated during nutritional stress. Proc. Natl. Acad. Sci. U.S.A. 98, 14328-14333. doi: 10.1073/pnas.251327898
58. Christensen-Dalsgaard, M., Jørgensen, M. G., and Gerdes, K. (2010). Three new RelE-homologous mRNA interferases of Escherichia coli differentially induced by environmental stresses. Mol. Microbiol. 75, 333-348. doi: 10.1111/j.1365-2958.2009.06969.x
59. Chrzanowski, L., Lawniczak, L., and Czaczyk, K. (2012). Why do microorganisms produce rhamnolipids? World J. Microb. Biot. 28, 401-419. doi: 10.1007/s11274-011-0854-8
60. Chugani, S., and Greenberg, E. P. (2007). The influence of human respiratory epithelia on Pseudomonas aeruginosa gene expression. Microb. Pathog. 42, 29-35. doi: 10.1016/j.micpath.2006.10.004
61. Ciofu, O., Mandsberg, L. F., Bjarnsholt, T., Wassermann, T., and Hoiby, N. (2010). Genetic adaptation of Pseudomonas aeruginosa during chronic lung infection of patients with cystic fibrosis: strong and weak mutators with heterogeneous genetic backgrounds emerge in mucA and/or lasR mutants. Microbiology 156, 1108-1119. doi: 10.1099/mic.0.033993-0
62. Colvin, K. M., Gordon, V. D., Murakami, K., Borlee, B. R., Wozniak, D. J., Wong, G. C. L., et al. (2011). The Pel polysaccharide can serve a structural and protective role in the biofilm matrix of Pseudomonas aeruginosa. PLoS Pathog. 7:e1001264. doi: 10.1371/journal.ppat.1001264
63. Colvin, K. M., Irie, Y., Tart, C. S., Urbano, R., Whitney, J. C., Ryder, C., et al. (2012). The Pel and Psl polysaccharides provide Pseudomonas aeruginosa structural redundancy within the biofilm matrix. Environ. Microbiol. 14, 1913-1928. doi: 10.1111/j.1462-2920.2011.02657.x
64. Daddaoua, A., Fillet, S., Fernández, M., Udaondo, Z., Krell, T., and Ramos, J. L. (2012). Genes for carbon metabolism and the ToxA virulence factor in Pseudomonas aeruginosa are regulated through molecular interactions of PtxR and PtxS. PLoS ONE 7:e39390. doi: 10.1371/journal.pone.0039390
65. Dalebroux, Z. D., and Swanson, M. S. (2012). ppGpp: magic beyond RNA polymerase. Nat. Rev. Microbiol. 10, 203-212. doi: 10.1038/nrmicro2720
66. D'Argenio, D. A., Wu, M., Hoffman, L. R., Kulasekara, H. D., Déziel, E., Smith, E. E., et al. (2007). Growth phenotypes of Pseudomonas aeruginosa lasR mutants adapted to the airways of cystic fibrosis patients. Mol. Microbiol. 64, 512-533. doi: 10.1111/j.1365-2958.2007.05678.x
67. da Silva, L. V. R. F., Ferreira, F. D., Reis, F. J. C., de Britto, M. C. A., Levy, C. E., Clark, O., et al. (2013). Pseudomonas aeruginosa infection in patients with cystic fibrosis: scientific evidence regarding clinical impact, diagnosis, and treatment. J. Bras. Pneumol. 39, 495-512. doi: 10.1590/S1806-37132013000400015
68. Das, T., Kutty, S. K., Kumar, N., and Manefield, M. (2013). Pyocyanin facilitates extracellular DNA binding to Pseudomonas aeruginosa influencing cell surface properties and aggregation. PLoS ONE 8:e58299. doi: 10.1371/journal.pone.0058299
69. Das, T., Kutty, S. K., Tavallaie, R., Ibugo, A. I., Panchompoo, J., Sehar, S., et al. (2015). Phenazine virulence factor binding to extracellular DNA is important for Pseudomonas aeruginosa biofilm formation. Sci. Rep. 5:8398. doi: 10.1038/srep08398
70. Davey, M. E., Caiazza, N. C., and O'Toole, G. A. (2003). Rhamnolipid surfactant production affects biofilm architecture in Pseudomonas aeruginosa PAO1. J. Bacteriol. 185, 1027-1036. doi: 10.1128/JB.185.3.1027-1036.2003
71. Davies, J., and Davies, D. (2010). Origins and evolution of antibiotic resistance. Microbiol. Mol. Biol. Rev. 74, 417-433. doi: 10.1128/MMBR.00016-10
72. Davies, J. E. (1997). Origins, acquisition and dissemination of antibiotic resistance determinants. Ciba Found. Symp. 207, 15-27; discussion 27-35.
73. Deveau, H., Garneau, J. E., and Moineau, S. (2010). CRISPR/Cas system and its role in phage-bacteria interactions. Annu. Rev. Microbiol. 64, 475-493. doi: 10.1146/annurev.micro.112408.134123
74. Diaz Caballero, J., Clark, S. T., Coburn, B., Zhang, Y., Wang, P. W., Donaldson, S. L., et al. (2015). Selective sweeps and parallel pathoadaptation drive Pseudomonas aeruginosa evolution in the cystic fibrosis lung. MBio 6, e00981-e00915. doi: 10.1128/mBio.00981-15
75. Diggle, S. P., Stacey, R. E., Dodd, C., Cámara, M., Williams, P., and Winzer, K. (2006). The galactophilic lectin, LecA, contributes to biofilm development in Pseudomonas aeruginosa. Environ. Microbiol. 8, 1095-1104. doi: 10.1111/j.1462-2920.2006.001001.x
76. Diggle, S. P., Winzer, K., Lazdunski, A., Williams, P., and Cámara, M. (2002). Advancing the quorum in Pseudomonas aeruginosa: mvat and the regulation of N-acylhomoserine lactone production and virulence gene expression. J. Bacteriol. 184, 2576-2586. doi: 10.1128/JB.184.10.2576-2586.2002
77. Döring, G., Conway, S. P., Heijerman, H. G., Hodson, M. E., Høiby, N., Smyth, A., et al. (2000). Antibiotic therapy against Pseudomonas aeruginosa in cystic fibrosis: a European consensus. Eur. Respir. J. 16, 749-767. doi: 10.1034/j.1399-3003.2000.16d30.x
78. Driffield, K., Miller, K., Bostock, J. M., O'Neill, A. J., and Chopra, I. (2008). Increased mutability of Pseudomonas aeruginosa in biofilms. J. Antimicrob. Chemother. 61, 1053-1056. doi: 10.1093/jac/dkn044
79. Durfee, T., Hansen, A. M., Zhi, H., Blattner, F. R., and Jin, D. J. (2008). Transcription profiling of the stringent response in Escherichia coli. J. Bacteriol. 190, 1084-1096. doi: 10.1128/JB.01092-07
80. Dusane, D. H., Zinjarde, S. S., Venugopalan, V. P., McLean, R. J., Weber, M. M., and Rahman, P. K. (2010). Quorum sensing: implications on rhamnolipid biosurfactant production. Biotechnol. Genet. Eng. Rev. 27, 159-184. doi: 10.1080/02648725.2010.10648149
81. El Amin, N., Giske, C. G., Jalal, S., Keijser, B., Kronvall, G., and Wretlind, B. (2005). Carbapenem resistance mechanisms in Pseudomonas aeruginosa: alterations of porin OprD and efflux proteins do not fully explain resistance patterns observed in clinical isolates. APMIS 113, 187-196. doi: 10.1111/j.1600-0463.2005.apm1130306.x
82. Epp, S. F., Köhler, T., Plésiat, P., Michéa-Hamzehpour, M., Frey, J., and Pechère, J. C. (2001). C-terminal region of Pseudomonas aeruginosa outer membrane porin OprD modulates susceptibility to meropenem. Antimicrob. Agents Chemother. 45, 1780-1787. doi: 10.1128/AAC.45.6.1780-1787.2001
83. Erickson, D. L., Lines, J. L., Pesci, E. C., Venturi, V., and Storey, D. G. (2004). Pseudomonas aeruginosa relA contributes to virulence in Drosophila melanogaster. Infect. Immun. 72, 5638-5645. doi: 10.1128/IAI.72.10.5638-5645.2004
84. Eurosurveillance Editorial Team (2013). CDC publishes report on antibiotic resistance threats in the United States for the first time. Eurosurveillance 18:5. Available online at: http://www.ecdc.europa.eu/en/activities/sciadvice/_layouts/forms/Review_DispForm.aspx?List=a3216f4c-f040-4f51-9f77-a96046dbfd72&ID=752&RootFolder=%2Fen%2Factivities%2Fsciadvice%2FLists%2FECDC%20Reviews&Web=0be238ef-4498-4962-8826-2e082a1f1639
85. Eymann, C., Homuth, G., Scharf, C., and Hecker, M. (2002). Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis. J. Bacteriol. 184, 2500-2520. doi: 10.1128/JB.184.9.2500-2520.2002
86. Falagas, M. E., and Kasiakou, S. K. (2005). Colistin: the revival of polymyxins for the management of multidrug-resistant gram-negative bacterial infections. Clin. Infect. Dis. 40, 1333-1341. doi: 10.1086/429323
87. Fasani, R. A., and Savageau, M. A. (2015). Unrelated toxin-antitoxin systems cooperate to induce persistence. J. R. Soc. Interface 12:20150130. doi: 10.1098/rsif.2015.0130
88. Feng, L., Xiang, Q., Ai, Q., Wang, Z., Zhang, Y., and Lu, Q. (2016). Effects of quorum sensing systems on regulatory T cells in catheter-related Pseudomonas aeruginosa biofilm infection rat models. Mediators Inflamm. 2016:4012912. doi: 10.1155/2016/4012912
89. Fernández, L., Breidenstein, E. B., and Hancock, R. E. (2011). Creeping baselines and adaptive resistance to antibiotics. Drug Resist. Updat. 14, 1-21. doi: 10.1016/j.drup.2011.01.001
90. Fernández, L., Gooderham, W. J., Bains, M., McPhee, J. B., Wiegand, I., and Hancock, R. E. (2010). Adaptive resistance to the "last hope" antibiotics polymyxin B and colistin in Pseudomonas aeruginosa is mediated by the novel two-component regulatory system ParR-ParS. Antimicrob. Agents Chemother. 54, 3372-3382. doi: 10.1128/AAC.00242-10
91. Fernández, L., Jenssen, H., Bains, M., Wiegand, I., Gooderham, W. J., and Hancock, R. E. (2012). The two-component system CprRS senses cationic peptides and triggers adaptive resistance in Pseudomonas aeruginosa independently of ParRS. Antimicrob. Agents Chemother. 56, 6212-6222. doi: 10.1128/AAC.01530-12
92. Fernández-García, L., Blasco, L., Lopez, M., Bou, G., García-Contreras, R., Wood, T., et al. (2016). Toxin-antitoxin systems in clinical pathogens. Toxins (Basel). 8:227. doi: 10.3390/toxins8070227
93. Flemming, H. C., and Wingender, J. (2010). The biofilm matrix. Nat. Rev. Microbiol. 8, 623-633. doi: 10.1038/nrmicro2415
94. Flume, P. A., and Van Devanter, D. R. (2012). State of progress in treating cystic fibrosis respiratory disease. BMC Med. 10:88. doi: 10.1186/1741-7015-10-88
95. Folkesson, A., Jelsbak, L., Yang, L., Johansen, H. K., Ciofu, O., Høiby, N., et al. (2012). Adaptation of Pseudomonas aeruginosa to the cystic fibrosis airway: an evolutionary perspective. Nat. Rev. Microbiol. 10, 841-851. doi: 10.1038/nrmicro2907
96. Franklin, M. J., Nivens, D. E., Weadge, J. T., and Howell, P. L. (2011). Biosynthesis of the Pseudomonas aeruginosa extracellular polysaccharides, alginate, Pel, and Psl. Front. Microbiol. 2:167. doi: 10.3389/fmicb.2011.00167
97. Fraud, S., Campigotto, A. J., Chen, Z., and Poole, K. (2008). MexCD-OprJ multidrug efflux system of Pseudomonas aeruginosa: involvement in chlorhexidine resistance and induction by membrane-damaging agents dependent upon the AlgU stress response sigma factor. Antimicrob. Agents Chemother. 52, 4478-4482. doi: 10.1128/AAC.01072-08
98. Frimmersdorf, E., Horatzek, S., Pelnikevich, A., Wiehlmann, L., and Schomburg, D. (2010). How Pseudomonas aeruginosa adapts to various environments: a metabolomic approach. Environ. Microbiol. 12, 1734-1747. doi: 10.1111/j.1462-2920.2010.02253.x
99. Frisk, A., Schurr, J. R., Wang, G., Bertucci, D. C., Marrero, L., Hwang, S. H., et al. (2004). Transcriptome analysis of Pseudomonas aeruginosa after interaction with human airway epithelial cells. Infect. Immun. 72, 5433-5438. doi: 10.1128/IAI.72.9.5433-5438.2004
100. Fujimura, T., Anan, N., Sugimori, G., Watanabe, T., Jinushi, Y., Yoshida, I., et al. (2009). Susceptibility of Pseudomonas aeruginosa clinical isolates in Japan to doripenem and other antipseudomonal agents. Int. J. Antimicrob. Agents 34, 523-528. doi: 10.1016/j.ijantimicag.2009.07.008
101. Fung, D. K., Chan, E. W., Chin, M. L., and Chan, R. C. (2010). Delineation of a bacterial starvation stress response network which can mediate antibiotic tolerance development. Antimicrob. Agents Chemother. 54, 1082-1093. doi: 10.1128/AAC.01218-09
102. Furukawa, S., Kuchma, S. L., and O'Toole, G. A. (2006). Keeping their options open: acute versus persistent infections. J. Bacteriol. 188, 1211-1217. doi: 10.1128/JB.188.4.1211-1217.2006
103. García-Contreras, R. (2016). Is quorum sensing interference a viable alternative to treat Pseudomonas aeruginosa infections? Front. Microbiol. 7:1454. doi: 10.3389/fmicb.2016.01454
104. García-Contreras, R., Nuñez-López, L., Jasso-Chávez, R., Kwan, B. W., Belmont, J. A., Rangel-Vega, A., et al. (2015). Quorum sensing enhancement of the stress response promotes resistance to quorum quenching and prevents social cheating. ISME J. 9, 115-125. doi: 10.1038/ismej.2014.98
105. García-García, J. D., Sánchez-Thomas, R., and Moreno-Sánchez, R. (2016). Bio-recovery of non-essential heavy metals by intra-and extracellular mechanisms in free-living microorganisms. Biotechnol. Adv. 34, 859-873. doi: 10.1016/j.biotechadv.2016.05.003
106. Garneau, J. E., Dupuis, M. È., Villion, M., Romero, D. A., Barrangou, R., Boyaval, P., et al. (2010). The CRISPR/Cas bacterial immune system cleaves bacteriophage and plasmid DNA. Nature 468, 67-71. doi: 10.1038/nature09523
107. Gellatly, S. L., and Hancock, R. E. W. (2013). Pseudomonas aeruginosa: new insights into pathogenesis and host defenses. Pathog. Dis. 67, 159-173. doi: 10.1111/2049-632X.12033
108. Ghafoor, A., Hay, I. D., and Rehm, B. H. (2011). Role of exopolysaccharides in Pseudomonas aeruginosa biofilm formation and architecture. Appl. Environ. Microbiol. 77, 5238-5246. doi: 10.1128/AEM.00637-11
109. Glick, J., and Garber, N. (1983). The intracellular localization of Pseudomonas aeruginosa lectins. J. Gen. Microbiol. 129, 3085-3090. doi: 10.1099/00221287-129-10-3085
110. Gloag, E. S., Turnbull, L., Huang, A., Vallotton, P., Wang, H., Nolan, L. M., et al. (2013). Self-organization of bacterial biofilms is facilitated by extracellular DNA. Proc. Natl. Acad. Sci. U.S.A. 110, 11541-11546. doi: 10.1073/pnas.1218898110
111. González, J. E., and Keshavan, N. D. (2006). Messing with bacterial quorum sensing. Microbiol. Mol. Biol. Rev. 70, 859-875. doi: 10.1128/MMBR.00002-06
112. González-Valdez, A., Servín-González, L., Juarez, K., Hernandez-Aligio, A., and Soberón-Chávez, G. (2014). The effect of specific rhlA-las-box mutations on DNA binding and gene activation by Pseudomonas aeruginosa quorum-sensing transcriptional regulators RhlR and LasR. FEMS Microbiol. Lett. 356, 217-225. doi: 10.1111/1574-6968.12505
113. Grote, J., Krysciak, D., and Streit, W. R. (2015). Phenotypic heterogeneity, a phenomenon that may explain why quorum sensing does not always result in truly homogenous cell behavior. Appl. Environ. Microbiol. 81, 5280-5289. doi: 10.1128/AEM.00900-15
114. Gupta, K., Liao, J., Petrova, O. E., Cherny, K. E., and Sauer, K. (2014). Elevated levels of the second messenger c-di-GMP contribute to antimicrobial resistance of Pseudomonas aeruginosa. Mol. Microbiol. 92, 488-506. doi: 10.1111/mmi.12587
115. Gutiérrez, O., Juan, C., Cercenado, E., Navarro, F., Bouza, E., Coll, P., et al. (2007). Molecular epidemiology and mechanisms of carbapenem resistance in Pseudomonas aeruginosa isolates from Spanish hospitals. Antimicrob. Agents Chemother. 51, 4329-4335. doi: 10.1128/AAC.00810-07
116. Gutu, A. D., Sgambati, N., Strasbourger, P., Brannon, M. K., Jacobs, M. A., Haugen, E., et al. (2013). Polymyxin resistance of Pseudomonas aeruginosa phoQ mutants is dependent on additional two-component regulatory systems. Antimicrob. Agents Chemother. 57, 2204-2215. doi: 10.1128/AAC.02353-12
117. Guzzo, J., Pages, J. M., Duong, F., Lazdunski, A., and Murgier, M. (1991). Pseudomonas aeruginosa alkaline protease: evidence for secretion genes and study of secretion mechanism. J. Bacteriol. 173, 5290-5297. doi: 10.1128/jb.173.17.5290-5297.1991
118. Hall, S., McDermott, C., Anoopkumar-Dukie, S., McFarland, A. J., Forbes, A., Perkins, A. V, et al. (2016). Cellular effects of pyocyanin, a secreted virulence factor of Pseudomonas aeruginosa. Toxins (Basel). 8:236. doi: 10.3390/toxins8080236
119. Hammond, J. H., Dolben, E. F., Smith, T. J., Bhuju, S., and Hogan, D. A. (2015). Links between Anr and quorum sensing in Pseudomonas aeruginosa biofilms. J. Bacteriol. 197, 2810-2820. doi: 10.1128/JB.00182-15
120. Hancock, R. E. W., and Speert, D. P. (2000). Antibiotic resistance in Pseudomonas aeruginosa: mechanisms and impact on treatment. Drug Resist Updat. 3, 247-255. doi: 10.1054/drup.2000.0152
121. Hannauer, M., Braud, A., Hoegy, F., Ronot, P., Boos, A., and Schalk, I. J. (2012). The PvdRT-OpmQ efflux pump controls the metal selectivity of the iron uptake pathway mediated by the siderophore pyoverdine in Pseudomonas aeruginosa. Environ. Microbiol. 14, 1696-1708. doi: 10.1111/j.1462-2920.2011.02674.x
122. Hassett, D. J. (1996). Anaerobic production of alginate by Pseudomonas aeruginosa: alginate restricts diffusion of oxygen. J. Bacteriol. 178, 7322-7325. doi: 10.1128/jb.178.24.7322-7325.1996
123. Hassett, D. J., Sutton, M. D., Schurr, M. J., Herr, A. B., Caldwell, C. C., and Matu, J. O. (2009). Pseudomonas aeruginosa hypoxic or anaerobic biofilm infections within cystic fibrosis airways. Trends Microbiol. 17, 130-138. doi: 10.1016/j.tim.2008.12.003
124. Häussler, S., Tümmler, B., Weissbrodt, H., Rohde, M., and Steinmetz, I. (1999). Small-colony variants of Pseudomonas aeruginosa in cystic fibrosis. Clin. Infect. Dis. 29, 621-625. doi: 10.1086/598644
125. Häussler, S., Ziegler, I., Löttel, A., von Götz, F., Rohde, M., Wehmhöhner, D., et al. (2003). Highly adherent small-colony variants of Pseudomonas aeruginosa in cystic fibrosis lung infection. J. Med. Microbiol. 52(Pt 4), 295-301. doi: 10.1099/jmm.0.05069-0
126. Hay, I. D., Gatland, K., Campisano, A., Jordens, J. Z., and Rehm, B. H. (2009a). Impact of alginate overproduction on attachment and biofilm architecture of a supermucoid Pseudomonas aeruginosa strain. Appl. Environ. Microbiol. 75, 6022-6025. doi: 10.1128/AEM.01078-09
127. Hay, I. D., Remminghorst, U., and Rehm, B. H. (2009b). MucR, a novel membrane-associated regulator of alginate biosynthesis in Pseudomonas aeruginosa. Appl. Environ. Microbiol. 75, 1110-1120. doi: 10.1128/AEM.02416-08
128. Hay, I. D., Ur Rehman, Z., Ghafoor, A., and Rehm, B. H. (2010). Bacterial biosynthesis of alginates. J. Chem. Techn. Biotechnol. 85, 752-759. doi: 10.1002/jctb.2372
129. Hay, I. D., Ur Rehman, Z., Moradali, M. F., Wang, Y., and Rehm, B. H. (2013). Microbial alginate production, modification and its applications. Microb. Biotechnol. 6, 637-650. doi: 10.1111/1751-7915.12076
130. Hay, T., Fraud, S., Lau, C. H., Gilmour, C., and Poole, K. (2013). Antibiotic inducibility of the MexXY multidrug efflux operon of Pseudomonas aeruginosa: involvement of the MexZ anti-repressor ArmZ. PLoS ONE 8:e56858. doi: 10.1371/journal.pone.0056858
131. Henrichfreise, B., Wiegand, I., Pfister, W., and Wiedemann, B. (2007). Resistance mechanisms of multiresistant Pseudomonas aeruginosa strains from Germany and correlation with hypermutation. Antimicrob. Agents Chemother. 51, 4062-4070. doi: 10.1128/AAC.00148-07
132. Hershberger, C. D., Ye, R. W., Parsek, M. R., Xie, Z. D., and Chakrabarty, A. M. (1995). The algT (algU) gene of Pseudomonas aeruginosa, a key regulator involved in alginate biosynthesis, encodes an alternative sigma factor (sigma E). Proc. Natl. Acad. Sci. U.S.A. 92, 7941-7945. doi: 10.1073/pnas.92.17.7941
133. Hesketh, A., Chen, W. J., Ryding, J., Chang, S., and Bibb, M. (2007). The global role of ppGpp synthesis in morphological differentiation and antibiotic production in Streptomyces coelicolor A3(2). Genome Biol. 8:R161. doi: 10.1186/gb-2007-8-8-r161
134. Hickman, J. W., Tifrea, D. F., and Harwood, C. S. (2005). A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels. Proc. Natl. Acad. Sci. U.S.A. 102, 14422-14427. doi: 10.1073/pnas.0507170102
135. Higgins, P. G., Fluit, A. C., Milatovic, D., Verhoef, J., and Schmitz, F. J. (2003). Mutations in GyrA, ParC, MexR and NfxB in clinical isolates of Pseudomonas aeruginosa. Int. J. Antimicrob. Agents 21, 409-413. doi: 10.1016/S0924-8579(03)00009-8
136. Hirai, K., Suzue, S., Irikura, T., Iyobe, S., and Mitsuhashi, S. (1987). Mutations producing resistance to norfloxacin in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 31, 582-586. doi: 10.1128/AAC.31.4.582
137. Hoffman, L. R., Kulasekara, H. D., Emerson, J., Houston, L. S., Burns, J. L., Ramsey, B. W., et al. (2009). Pseudomonas aeruginosa lasR mutants are associated with cystic fibrosis lung disease progression. J. Cyst. Fibros. 8, 66-70. doi: 10.1016/j.jcf.2008.09.006
138. Hoffman, L. R., Richardson, A. R., Houston, L. S., Kulasekara, H. D., Martens-Habbena, W., Klausen, M., et al. (2010). Nutrient availability as a mechanism for selection of antibiotic tolerant Pseudomonas aeruginosa within the CF airway. PLoS Pathog. 6:e1000712. doi: 10.1371/journal.ppat.1000712
139. Hogardt, M., and Heesemann, J. (2010). Adaptation of Pseudomonas aeruginosa during persistence in the cystic fibrosis lung. Int. J. Med. Microbiol. 300, 557-562. doi: 10.1016/j.ijmm.2010.08.008
140. Hoge, R., Pelzer, A., Rosenau, F., and Wilhelm, S. (2010). Weapons of a pathogen: proteases and their role in virulence of Pseudomonas aeruginosa. Current research, technology and education topics in applied microbiology and microbial biotechnology 2, 383-395.
141. Hong, D. J., Bae, I. K., Jang, I. H., Jeong, S. H., Kang, H. K., and Lee, K. (2015). Epidemiology and characteristics of metallo-β-lactamase-producing Pseudomonas aeruginosa. Infect Chemother. 47, 81-97. doi: 10.3947/ic.2015.47.2.81
142. Imperi, F., Tiburzi, F., Fimia, G. M., and Visca, P. (2010). Transcriptional control of the pvdS iron starvation sigma factor gene by the master regulator of sulfur metabolism CysB in Pseudomonas aeruginosa. Environ. Microbiol. 12, 1630-1642. doi: 10.1111/j.1462-2920.2010.02210.x
143. Irie, Y., Starkey, M., Edwards, A. N., Wozniak, D. J., Romeo, T., and Parsek, M. R. (2010). Pseudomonas aeruginosa biofilm matrix polysaccharide Psl is regulated transcriptionally by RpoS and post-transcriptionally by RsmA. Mol. Microbiol. 78, 158-172. doi: 10.1111/j.1365-2958.2010.07320.x
144. Jaffar-Bandjee, M. C., Lazdunski, A., Bally, M., Carrere, J., Chazalette, J. P., and Galabert, C. (1995). Production of elastase, exotoxin A, and alkaline protease in sputa during pulmonary exacerbation of cystic fibrosis in patients chronically infected by Pseudomonas aeruginosa. J. Clin. Microbiol. 33, 924-929.
145. Jeannot, K., Elsen, S., Kohler, T., Attree, I., van Delden, C., and Plésiat, P. (2008). Resistance and virulence of Pseudomonas aeruginosa clinical strains overproducing the MexCD-OprJ efflux pump. Antimicrob. Agents Chemother. 52, 2455-2462. doi: 10.1128/AAC.01107-07
146. Jennings, L. K., Storek, K. M., Ledvina, H. E., Coulon, C., Marmont, L. S., Sadovskaya, I., et al. (2015). Pel is a cationic exopolysaccharide that cross-links extracellular DNA in the Pseudomonas aeruginosa biofilm matrix. Proc. Natl. Acad. Sci. U.S.A. 112, 11353-11358. doi: 10.1073/pnas.1503058112
147. Jensen, P. Ø., Bjarnsholt, T., Phipps, R., Rasmussen, T. B., Calum, H., Christoffersen, L., et al. (2007). Rapid necrotic killing of polymorphonuclear leukocytes is caused by quorum-sensing-controlled production of rhamnolipid by Pseudomonas aeruginosa. Microbiology 153(Pt 5), 1329-1338. doi: 10.1099/mic.0.2006/003863-0
148. Jimenez, P. N., Koch, G., Thompson, J. A., Xavier, K. B., Cool, R. H., and Quax, W. J. (2012). The multiple signaling systems regulating virulence in Pseudomonas aeruginosa. Microbiol. Mol. Biol. Rev. 76, 46-65. doi: 10.1128/MMBR.05007-11
149. Jiricny, N., Molin, S., Foster, K., Diggle, S. P., Scanlan, P. D., Ghoul, M., et al. (2014). Loss of social behaviours in populations of Pseudomonas aeruginosa infecting lungs of patients with cystic fibrosis. PLoS ONE 9:e83124. doi: 10.1371/journal.pone.0083124
150. Johnson, A. P., and Woodford, N. (2013). Global spread of antibiotic resistance: the example of New Delhi metallo-β-lactamase (NDM)-mediated carbapenem resistance. J Med. Microbiol. 62(Pt 4), 499-513. doi: 10.1099/jmm.0.052555-0
151. Jones, P., Palser, S. C., Pravle, A. P., Hurley, M. N., and Smyth, A. R. (2016). WS20.1 Secular trends in Pseudomonas aeruginosa acquisition in the United Kingdom: a registry study. J. Cyst. Fibros 15(Suppl. 1), S31. doi: 10.1016/S1569-1993(16)30169-2
152. Juan, C., Macia, M. D., Gutierrez, O., Vidal, C., Perez, J. L., and Oliver, A. (2005). Molecular mechanisms of β-lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains. Antimicrob. Agents Chemother. 49, 4733-4738. doi: 10.1128/AAC.49.11.4733-4738.2005
153. Jyot, J., and Ramphal, R. (2008). "Flagella and pili of Pseudomonas aeruginosa," in Pseudomonas: Model Organism, Pathogen, Cell Factory, ed B. H. A. Rehm (Weinheim: Wiley-VCH Verlag GmbH & Co. KGaA), 85-108.
154. Kao, C. Y., Chen, S. S., Hung, K. H., Wu, H. M., Hsueh, P. R., Yan, J. J., et al. (2016). Overproduction of active efflux pump and variations of OprD dominate in imipenem-resistant Pseudomonas aeruginosa isolated from patients with bloodstream infections in Taiwan. BMC Microbiol. 16:107. doi: 10.1186/s12866-016-0719-2
155. Karatuna, O., and Yagci, A. (2010). Analysis of quorum sensing-dependent virulence factor production and its relationship with antimicrobial susceptibility in Pseudomonas aeruginosa respiratory isolates. Clin. Microbiol. Infect. 16, 1770-1775. doi: 10.1111/j.1469-0691.2010.03177.x
156. Karlowsky, J. A., Hoban, D. J., Zelenitsky, S. A., and Zhanel, G. G. (1997). Altered denA and anr gene expression in aminoglycoside adaptive resistance in Pseudomonas aeruginosa. J. Antimicrob. Chemother. 40, 371-376. doi: 10.1093/jac/40.3.371
157. Kenward, M. A., Brown, M. R., Hesslewood, S. R., and Dillon, C. (1978). Influence of R-plasmid RP1 of Pseudomonas aeruginosa on cell wall composition, drug resistance, and sensitivity to cold shock. Antimicrob. Agents Chemother. 13, 446-453. doi: 10.1128/AAC.13.3.446
158. Kessler, E., Safrin, M., Abrams, W. R., Rosenbloom, J., and Ohman, D. E. (1997). Inhibitors and specificity of Pseudomonas aeruginosa LasA. J. Biol. Chem. 272, 9884-9889. doi: 10.1074/jbc.272.15.9884
159. Khaledi, A., Schniederjans, M., Pohl, S., Rainer, R., Bodenhofer, U., Xia, B., et al. (2016). Transcriptome profiling of antimicrobial resistance in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 60, 4722-4733. doi: 10.1128/AAC.00075-16
160. Khan, T. Z., Wagener, J. S., Bost, T., Martinez, J., Accurso, F. J., and Riches, D. W. H. (1995). Early pulmonary inflammation in infants with cystic fibrosis. Am. J. Resp. Crit. Care 151, 1075-1082.
161. Kim, E. J., Sabra, W., and Zeng, A. P. (2003). Iron deficiency leads to inhibition of oxygen transfer and enhanced formation of virulence factors in cultures of Pseudomonas aeruginosa PAO1. Microbiology 149(Pt 9), 2627-2634. doi: 10.1099/mic.0.26276-0
162. Kim, H. Y., Schlictman, D., Shankar, S., Xie, Z., Chakrabarty, A. M., and Kornberg, A. (1998). Alginate, inorganic polyphosphate, GTP and ppGpp synthesis co-regulated in Pseudomonas aeruginosa: implications for stationary phase survival and synthesis of RNA/DNA precursors. Mol. Microbiol. 27, 717-725. doi: 10.1046/j.1365-2958.1998.00702.x
163. Kirisits, M. J., Prost, L., Starkey, M., and Parsek, M. R. (2005). Characterization of colony morphology variants isolated from Pseudomonas aeruginosa biofilms. Appl. Environ. Microbiol. 71, 4809-4821. doi: 10.1128/AEM.71.8.4809-4821.2005
164. Kohanski, M. A., Dwyer, D. J., Wierzbowski, J., Cottarel, G., and Collins, J. J. (2008). Mistranslation of membrane proteins and two-component system activation trigger antibiotic-mediated cell death. Cell 135, 679-690. doi: 10.1016/j.cell.2008.09.038
165. Köhler, T., Michéa-Hamzehpour, M., Henze, U., Gotoh, N., Curty, L. K., and Pechère, J. C. (1997). Characterization of MexE-MexF-OprN, a positively regulated multidrug efflux system of Pseudomonas aeruginosa. Mol. Microbiol. 23, 345-354. doi: 10.1046/j.1365-2958.1997.2281594.x
166. Köhler, T., van Delden, C., Curty, L. K., Hamzehpour, M. M., and Pechere, J. C. (2001). Overexpression of the MexEF-OprN multidrug efflux system affects cell-to-cell signaling in Pseudomonas aeruginosa. J. Bacteriol. 183, 5213-5222. doi: 10.1128/JB.183.18.5213-5222.2001
167. Kong, K.-F., Jayawardena, S. R., Indulkar, S. D., del Puerto, A., Koh, C.-L., Høiby, N., et al. (2005). Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB β-lactamases, proteases, quorum sensing, and other virulence factors. Antimicrob. Agents Chemother. 49, 4567-4575. doi: 10.1128/AAC.49.11.4567-4575.2005
168. Kung, V. L., Ozer, E. A., and Hauser, A. R. (2010). The accessory genome of Pseudomonas aeruginosa. Microbiol. Mol. Biol. Rev. 74, 621-641. doi: 10.1128/MMBR.00027-10
169. Kuroda, A., Nomura, K., Ohtomo, R., Kato, J., Ikeda, T., Takiguchi, N., et al. (2001). Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli. Science 293, 705-708. doi: 10.1126/science.1061315
170. Laarman, A. J., Bardoel, B. W., Ruyken, M., Fernie, J., Milder, F. J., van Strijp, J. A., et al. (2012). Pseudomonas aeruginosa alkaline protease blocks complement activation via the classical and lectin pathways. J. Immunol. 188, 386-393. doi: 10.4049/jimmunol.1102162
171. LaFayette, S. L., Houle, D., Beaudoin, T., Wojewodka, G., Radzioch, D., Hoffman, L. R., et al. (2015). Cystic fibrosis-adapted Pseudomonas aeruginosa quorum sensing lasR mutants cause hyperinflammatory responses. Sci. Adv. 1:e1500199. doi: 10.1126/sciadv.1500199
172. Lamarche, M. G., and Déziel, E. (2011). MexEF-OprN efflux pump exports the Pseudomonas quinolone signal (PQS) precursor HHQ (4-hydroxy-2-heptylquinoline). PLoS ONE 6:e24310. doi: 10.1371/journal.pone.0024310
173. Lambert, M. L., Suetens, C., Savey, A., Palomar, M., Hiesmayr, M., Morales, I., et al. (2011). Clinical outcomes of health-care-associated infections and antimicrobial resistance in patients admitted to European intensive-care units: a cohort study. Lancet Infect. Dis. 11, 30-38. doi: 10.1016/S1473-3099(10)70258-9
174. Lapouge, K., Schubert, M., Allain, F. H., and Haas, D. (2008). Gac/Rsm signal transduction pathway of gamma-proteobacteria: from RNA recognition to regulation of social behaviour. Mol. Microbiol. 67, 241-253. doi: 10.1111/j.1365-2958.2007.06042.x
175. LaSarre, B., and Federle, M. J. (2013). Exploiting quorum sensing to confuse bacterial pathogens. Microbiol. Mol. Biol. Rev. 77, 73-111. doi: 10.1128/MMBR.00046-12
176. Lau, C. H., Hughes, D., and Poole, K. (2014). MexY-promoted aminoglycoside resistance in Pseudomonas aeruginosa: involvement of a putative proximal binding pocket in aminoglycoside recognition. Mbio 5:e01068. doi: 10.1128/mBio.01068-14
177. Laughlin, R. S., Musch, M. W., Hollbrook, C. J., Rocha, F. M., Chang, E. B., and Alverdy, J. C. (2000). The key role of Pseudomonas aeruginosa PA-I lectin on experimental gut-derived sepsis. Ann. Surg. 232, 133-142. doi: 10.1097/00000658-200007000-00019
178. Lee, J. K., Lee, Y. S., Park, Y. K., and Kim, B. S. (2005). Alterations in the GyrA and GyrB subunits of topoisomerase II and the ParC and ParE subunits of topoisomerase IV in ciprofloxacin-resistant clinical isolates of Pseudomonas aeruginosa. Int. J. Antimicrob. Agents 25, 290-295. doi: 10.1016/j.ijantimicag.2004.11.012
179. Lee, J., Wu, J., Deng, Y., Wang, J., Wang, C., Wang, J., et al. (2013). A cell-cell communication signal integrates quorum sensing and stress response. Nat. Chem. Biol. 9, 339-343. doi: 10.1038/nchembio.1225
180. Lee, J. Y., Park, Y. K., Chung, E. S., Na, I. Y., and Ko, K. S. (2016). Evolved resistance to colistin and its loss due to genetic reversion in Pseudomonas aeruginosa. Sci. Rep. 6:25543. doi: 10.1038/srep25543
181. Lee, J., and Zhang, L. (2015). The hierarchy quorum sensing network in Pseudomonas aeruginosa. Protein Cell 6, 26-41. doi: 10.1007/s13238-014-0100-x
182. Leid, J. G. (2009). Bacterial biofilms resist key host defenses. Microbe 4, 66-70.
183. Lenney, W., and Gilchrist, F. J. (2011). Pseudomonas aeruginosa and cyanide production. Eur. Respir. J. 37, 482-483. doi: 10.1183/09031936.00122810
184. Lewis, K. (2007). Persister cells, dormancy and infectious disease. Nat. Rev. Microbiol. 5, 48-56. doi: 10.1038/nrmicro1557
185. Lewis, K. (2008). Multidrug tolerance of biofilms and persister cells. Curr. Top. Microbiol. Immunol. 322, 107-131. doi: 10.1007/978-3-540-75418-3_6
186. Li, G., Shen, M., Lu, S., Le, S., Tan, Y., Wang, J., et al. (2016). Identification and characterization of the HicAB toxin-antitoxin system in the opportunistic pathogen Pseudomonas aeruginosa. Toxins (Basel). 8:113. doi: 10.3390/toxins8040113
187. Li, M., Long, Y., Liu, Y., Liu, Y., Chen, R., Shi, J., et al. (2016). HigB of Pseudomonas aeruginosa enhances killing of phagocytes by up-regulating the type III secretion system in ciprofloxacin induced persister cells. Front. Cell. Infect. Microbiol. 6:125. doi: 10.3389/fcimb.2016.00125
188. Li, X. Z., Plésiat, P., and Nikaido, H. (2015). The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria. Clin. Microbiol. Rev. 28, 337-418. doi: 10.1128/CMR.00117-14
189. Li, Y. Q., Du, X. L., Lu, Z. J., Wu, D. Q., Zhao, Y. L., Ren, B., et al. (2011). Regulatory feedback loop of two phz gene clusters through 5'-untranslated regions in Pseudomonas sp M18. PLoS ONE 6:e19413. doi: 10.1371/journal.pone.0019413
190. Lister, P. D., Wolter, D. J., and Hanson, N. D. (2009). Antibacterial-resistant Pseudomonas aeruginosa: clinical impact and complex regulation of chromosomally encoded resistance mechanisms. Clin. Microbiol. Rev. 22, 582-610. doi: 10.1128/CMR.00040-09
191. Liu, Y. Y., Wang, Y., Walsh, T. R., Yi, L. X., Zhang, R., Spencer, J., et al. (2016). Emergence of plasmid-mediated colistin resistance mechanism MCR-1 in animals and human beings in China: a microbiological and molecular biological study. Lancet Infect. Dis. 16, 161-168. doi: 10.1016/S1473-3099(15)00424-7
192. Llanes, C., Kohler, T., Patry, I., Dehecq, B., van Delden, C., and Plésiat, P. (2011). Role of the MexEF-OprN efflux system in low-level resistance of Pseudomonas aeruginosa to ciprofloxacin. Antimicrob. Agents Chemother. 55, 5676-5684. doi: 10.1128/AAC.00101-11
193. Long, J., Zaborina, O., Holbrook, C., Zaborin, A., and Alverdy, J. (2008). Depletion of intestinal phosphate after operative injury activates the virulence of P. aeruginosa causing lethal gut-derived sepsis. Surgery 144, 189-197. doi: 10.1016/j.surg.2008.03.045
194. Louwen, R., Staals, R. H. J., Endtz, H. P., van Baarlen, P., and van der Oost, J. (2014). The role of CRISPR-Cas systems in virulence of pathogenic bacteria. Microbiol. Mol. Biol. Rev. 78, 74-88. doi: 10.1128/MMBR.00039-13
195. Ma, L., Conover, M., Lu, H., Parsek, M. R., Bayles, K., and Wozniak, D. J. (2009). Assembly and development of the Pseudomonas aeruginosa biofilm matrix. PLoS Pathog. 5:e1000354. doi: 10.1371/journal.ppat.1000354
196. MacDougall, C., Harpe, S. E., Powell, J. P., Johnson, C. K., Edmond, M. B., and Polk, R. E. (2005). Pseudomonas aeruginosa, Staphylococcus aureus, and fluoroquinolone use. Emerging Infect. Dis. 11, 1197-1204. doi: 10.3201/eid1108.050116
197. Mahenthiralingam, E., Campbell, M. E., and Speert, D. P. (1994). Nonmotility and phagocytic resistance of Pseudomonas aeruginosa isolates from chronically colonized patients with cystic fibrosis. Infect. Immun. 62, 596-605.
198. Maisonneuve, E., Castro-Camargo, M., and Gerdes, K. (2013). (p)ppGpp controls bacterial persistence by stochastic induction of toxin-antitoxin activity. Cell 154, 1140-1150. doi: 10.1016/j.cell.2013.07.048
199. Makarova, K. S., Haft, D. H., Barrangou, R., Brouns, S. J. J., Charpentier, E., Horvath, P., et al. (2011). Evolution and classification of the CRISPR-Cas systems. Nat. Rev. Microbiol. 9, 467-477. doi: 10.1038/nrmicro2577
200. Malone, J. G. (2015). Role of small colony variants in persistence of Pseudomonas aeruginosa infections in cystic fibrosis lungs. Infect. Drug Resist. 8, 237-247. doi: 10.2147/IDR.S68214
201. Malone, J. G., Jaeger, T., Manfredi, P., Dötsch, A., Blanka, A., Bos, R., et al. (2012). The YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airways. PLoS Pathog. 8:e1002760. doi: 10.1371/journal.ppat.1002760
202. Mann, E. E., and Wozniak, D. J. (2012). Pseudomonas biofilm matrix composition and niche biology. FEMS Microbiol. Rev. 36, 893-916. doi: 10.1111/j.1574-6976.2011.00322.x
203. Marr, A. K., Overhage, J., Bains, M., and Hancock, R. E. W. (2007). The Lon protease of Pseudomonas aeruginosa is induced by aminoglycosides and is involved in biofilm formation and motility. Microbiology 153(Pt 2), 474-482. doi: 10.1099/mic.0.2006/002519-0
204. Martinez, J. L., Sánchez, M. B., Martínez-Solano, L., Hernandez, A., Garmendia, L., Fajardo, A., et al. (2009). Functional role of bacterial multidrug efflux pumps in microbial natural ecosystems. FEMS Microbiol. Rev. 33, 430-449. doi: 10.1111/j.1574-6976.2008.00157.x
205. Marvig, R. L., Sommer, L. M., Molin, S., and Johansen, H. K. (2015). Convergent evolution and adaptation of Pseudomonas aeruginosa within patients with cystic fibrosis. Nat. Genet. 47, 57-64. doi: 10.1038/ng.3148
206. Maseda, H., Saito, K., Nakajima, A., and Nakae, T. (2000). Variation of the mexT gene, a regulator of the MexEF-oprN efflux pump expression in wild-type strains of Pseudomonas aeruginosa. FEMS Microbiol. Lett. 192, 107-112. doi: 10.1111/j.1574-6968.2000.tb09367.x
207. Maseda, H., Uwate, M., and Nakae, T. (2010). Transcriptional regulation of the MexEF-oprN multidrug efflux pump operon by MexT and an unidentified repressor in nfxC-type mutant of Pseudomonas aeruginosa. FEMS Microbiol. Lett. 311, 36-43. doi: 10.1111/j.1574-6968.2010.02063.x
208. Mashburn, L. M., and Whiteley, M. (2005). Membrane vesicles traffic signals and facilitate group activities in a prokaryote. Nature 437, 422-425. doi: 10.1038/nature03925
209. Mataseje, L. F., Peirano, G., Church, D. L., Conly, J., Mulvey, M., and Pitout, J. D. (2016). Colistin-nonsusceptible Pseudomonas aeruginosa sequence type 654 with blaNDM-1 arrives in North America. Antimicrob. Agents Chemother. 60, 1794-1800. doi: 10.1128/AAC.02591-15
210. Mathee, K., Ciofu, O., Sternberg, C., Lindum, P. W., Campbell, J. I, Jensen, P., et al. (1999). Mucoid conversion of Pseudomonas aeruginosa by hydrogen peroxide: a mechanism for virulence activation in the cystic fibrosis lung. Microbiology 145(Pt 6), 1349-1357. doi: 10.1099/13500872-145-6-1349
211. Mathee, K., Narasimhan, G., Valdes, C., Qiu, X., Matewish, J. M., Koehrsen, M., et al. (2008). Dynamics of Pseudomonas aeruginosa genome evolution. Proc. Natl. Acad. Sci. U.S.A. 105, 3100-3105. doi: 10.1073/pnas.0711982105
212. Matsuo, Y., Eda, S., Gotoh, N., Yoshihara, E., and Nakae, T. (2004). MexZ-mediated regulation of MexXY multidrug efflux pump expression in Pseudomonas aeruginosa by binding on the mexZ-mexX intergenic DNA. FEMS Microbiol. Lett. 238, 23-28. doi: 10.1016/j.femsle.2004.07.010
213. Maxwell, K. L. (2016). Phages fight back: inactivation of the CRISPR-Cas bacterial immune system by anti-CRISPR proteins. PLoS Pathog. 12:e1005282. doi: 10.1371/journal.ppat.1005282
214. McDaniel, C. T., Panmanee, W., and Hassett, D. J. (2015). "An overview of infections in cystic fibrosis airways and the role of environmental conditions on Pseudomonas aeruginosa biofilm formation and viability," in Cystic Fibrosis in the Light of New Research, ed D. Wat (InTech), 171-198.
215. Meletis, G., and Bagkeri, M. (2013). "Pseudomonas aeruginosa: multi-drug-resistance development and treatment options," in Infection Control, ed S. Basak (InTech), 33-56.
216. Michalska, M., and Wolf, P. (2015). Pseudomonas Exotoxin A: optimized by evolution for effective killing. Front. Microbiol. 6:963. doi: 10.3389/fmicb.2015.00963
217. Mishra, M., Byrd, M. S., Sergeant, S., Azad, A. K., Parsek, M. R., McPhail, L., et al. (2012). Pseudomonas aeruginosa Psl polysaccharide reduces neutrophil phagocytosis and the oxidative response by limiting complement-mediated opsonization. Cell. Microbiol. 14, 95-106. doi: 10.1111/j.1462-5822.2011.01704.x
218. Mojica, F. J., Díez-Villaseñor, C., García-Martínez, J., and Almendros, C. (2009). Short motif sequences determine the targets of the prokaryotic CRISPR defence system. Microbiology 155(Pt 3), 733-740. doi: 10.1099/mic.0.023960-0
219. Moradali, M. F., Donati, I., Sims, I. M., Ghods, S., and Rehm, B. H. (2015). Alginate polymerization and modification are linked in Pseudomonas aeruginosa. MBio 6, e00453-e00415. doi: 10.1128/mBio.00453-15
220. Moscoso, J. A., Mikkelsen, H., Heeb, S., Williams, P., and Filloux, A. (2011). The Pseudomonas aeruginosa sensor RetS switches type III and type VI secretion via c-di-GMP signalling. Environ. Microbiol. 13, 3128-3138. doi: 10.1111/j.1462-2920.2011.02595.x
221. Moskowitz, S. M., Brannon, M. K., Dasgupta, N., Pier, M., Sgambati, N., Miller, A. K., et al. (2012). PmrB mutations promote polymyxin resistance of Pseudomonas aeruginosa isolated from colistin-treated cystic fibrosis patients. Antimicrob. Agents Chemother. 56, 1019-1030. doi: 10.1128/AAC.05829-11
222. Mouneimné, H., Robert, J., Jarlier, V., and Cambau, E. (1999). Type II topoisomerase mutations in ciprofloxacin-resistant strains of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 43, 62-66.
223. Mulcahy, H., Charron-Mazenod, L., and Lewenza, S. (2008). Extracellular DNA chelates cations and induces antibiotic resistance in Pseudomonas aeruginosa biofilms. PLoS Pathog. 4:e1000213. doi: 10.1371/journal.ppat.1000213
224. Mulcahy, L. R., Burns, J. L., Lory, S., and Lewis, K. (2010). Emergence of Pseudomonas aeruginosa strains producing high levels of persister cells in patients with cystic fibrosis. J. Bacteriol. 192, 6191-6199. doi: 10.1128/JB.01651-09
225. Nathwani, D., Raman, G., Sulham, K., Gavaghan, M., and Menon, V. (2014). Clinical and economic consequences of hospital-acquired resistant and multidrug-resistant Pseudomonas aeruginosa infections: a systematic review and meta-analysis. Antimicrob. Resist. Infect. Control 3:32. doi: 10.1186/2047-2994-3-32
226. Nelson, L. K., D'Amours, G. H., Sproule-Willoughby, K. M., Morck, D. W., and Ceri, H. (2009). Pseudomonas aeruginosa las and rhl quorum-sensing systems are important for infection and inflammation in a rat prostatitis model. Microbiology 155(Pt 8), 2612-2619. doi: 10.1099/mic.0.028464-0
227. Nguyen, A. T., Jones, J. W., Camara, M., Williams, P., Kane, M. A., and Oglesby-Sherrouse, A. G. (2016). Cystic fibrosis isolates of Pseudomonas aeruginosa retain iron-regulated antimicrobial activity against Staphylococcus aureus through the action of multiple alkylquinolones. Front. Microbiol. 7:1171. doi: 10.3389/fmicb.2016.01171
228. Nguyen, A. T., Jones, J. W., Ruge, M. A., Kane, M. A., and Oglesby-Sherrouse, A. G. (2015). Iron depletion enhances production of antimicrobials by Pseudomonas aeruginosa. J. Bacteriol. 197, 2265-2275. doi: 10.1128/JB.00072-15
229. Nguyen, D., Joshi-Datar, A., Lepine, F., Bauerle, E., Olakanmi, O., Beer, K., et al. (2011). Active starvation responses mediate antibiotic tolerance in biofilms and nutrient-limited bacteria. Science 334, 982-986. doi: 10.1126/science.1211037
230. Ochs, M. M., McCusker, M. P., Bains, M., and Hancock, R. E. (1999). Negative regulation of the Pseudomonas aeruginosa outer membrane porin OprD selective for imipenem and basic amino acids. Antimicrob. Agents Chemother. 43, 1085-1090.
231. Oldak, E., and Trafny, E. A. (2005). Secretion of proteases by Pseudomonas aeruginosa biofilms exposed to ciprofloxacin. Antimicrob. Agents Chemother. 49, 3281-3288. doi: 10.1128/AAC.49.8.3281-3288.2005
232. Oliver, A., Cantón, R., Campo, P., Baquero, F., and Blázquez, J. (2000). High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection. Science 288, 1251-1253. doi: 10.1126/science.288.5469.1251
233. Oliver, A., and Mena, A. (2010). Bacterial hypermutation in cystic fibrosis, not only for antibiotic resistance. Clin. Microbiol. Infect. 16, 798-808. doi: 10.1111/j.1469-0691.2010.03250.x
234. Oliver, A., Mulet, X., López-Causapé, C., and Juan, C. (2015). The increasing threat of Pseudomonas aeruginosa high-risk clones. Drug Resist. Updat. 21-22, 41-59. doi: 10.1016/j.drup.2015.08.002
235. Olsen, I. (2015). Biofilm-specific antibiotic tolerance and resistance. Eur. J. Clin. Microbiol. Infect. Dis. 34, 877-886. doi: 10.1007/s10096-015-2323-z
236. Overhage, J., Schemionek, M., Webb, J. S., and Rehm, B. H. (2005). Expression of the psl operon in Pseudomonas aeruginosa PAO1 biofilms: PslA performs an essential function in biofilm formation. Appl. Environ. Microbiol. 71, 4407-4413. doi: 10.1128/AEM.71.8.4407-4413.2005
237. Ozer, E. A., Allen, J. P., and Hauser, A. R. (2014). Characterization of the core and accessory genomes of Pseudomonas aeruginosa using bioinformatic tools Spine and AGEnt. BMC Genomics 15:737. doi: 10.1186/1471-2164-15-737
238. Pagedar, A., Singh, J., and Batish, V. K. (2011). Efflux mediated adaptive and cross resistance to ciprofloxacin and benzalkonium chloride in Pseudomonas aeruginosa of dairy origin. J. Basic Microbiol. 51, 289-295. doi: 10.1002/jobm.201000292
239. Palmer, K. L., and Whiteley, M. (2011). DMS3-42: the secret to CRISPR-dependent biofilm inhibition in Pseudomonas aeruginosa. J. Bacteriol. 193, 3431-3432. doi: 10.1128/JB.05066-11
240. Pandey, D. P., and Gerdes, K. (2005). Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Res. 33, 966-976. doi: 10.1093/nar/gki201
241. Papenfort, K., and Bassler, B. L. (2016). Quorum sensing signal-response systems in Gram-negative bacteria. Nat. Rev. Microbiol. 14, 576-588. doi: 10.1038/nrmicro.2016.89
242. Paterson, D. L., and Bonomo, R. A. (2005). Extended-spectrum β-lactamases: a clinical update. Clin. Microbiol. Rev. 18, 657-686. doi: 10.1128/CMR.18.4.657-686.2005
243. Paul, K., Nieto, V., Carlquist, W. C., Blair, D. F., and Harshey, R. M. (2010). The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism. Mol. Cell 38, 128-139. doi: 10.1016/j.molcel.2010.03.001
244. Pawluk, A., Bondy-Denomy, J., Cheung, V. H. W., Maxwell, K. L., and Davidson, A. R. (2014). A new group of phage Anti-CRISPR genes inhibits the type I-E CRISPR-Cas system of Pseudomonas aeruginosa. MBio 5:e00896-14. doi: 10.1128/mBio.00896-14
245. Pessi, G., and Haas, D. (2000). Transcriptional control of the hydrogen cyanide biosynthetic genes hcnABC by the anaerobic regulator ANR and the quorum-sensing regulators LasR and RhlR in Pseudomonas aeruginosa. J. Bacteriol. 182, 6940-6949. doi: 10.1128/JB.182.24.6940-6949.2000
246. Petrova, O. E., and Sauer, K. (2009). A novel signaling network essential for regulating Pseudomonas aeruginosa biofilm development. PLoS Pathog. 5:e1000668. doi: 10.1371/journal.ppat.1000668
247. Pillar, C. M., and Hobden, J. A. (2002). Pseudomonas aeruginosa exotoxin A and keratitis in mice. Invest. Ophthalmol. Vis. Sci. 43, 1437-1444. Available online at: http://iovs.arvojournals.org/article.aspx?articleid=2123690
248. Poole, K. (2005). Aminoglycoside resistance in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 49, 479-487. doi: 10.1128/AAC.49.2.479-487.2005
249. Poole, K. (2011). Pseudomonas aeruginosa: resistance to the max. Front. Microbiol. 2:65. doi: 10.3389/fmicb.2011.00065
250. Poole, K. (2012). Stress responses as determinants of antimicrobial resistance in Gram-negative bacteria. Trends Microbiol. 20, 227-234. doi: 10.1016/j.tim.2012.02.004
251. Porter, S. L., Wadhams, G. H., and Armitage, J. P. (2011). Signal processing in complex chemotaxis pathways. Nat. Rev. Microbiol. 9, 153-165. doi: 10.1038/nrmicro2505
252. Potron, A., Poirel, L., and Nordmann, P. (2015). Emerging broad-spectrum resistance in Pseudomonas aeruginosa and Acinetobacter baumannii: mechanisms and epidemiology. Int. J. Antimicrob. Agents 45, 568-585. doi: 10.1016/j.ijantimicag.2015.03.001
253. Potrykus, K., and Cashel, M. (2008). (p)ppGpp: still magical? Annu. Rev. Microbiol. 62, 35-51. doi: 10.1146/annurev.micro.62.081307.162903
254. Pourmand, M., Sadighian, H., and Naderi, M. (2015). Relation between expression of the las quorum-sensing system in clinical isolates of Pseudomonas aeruginosa and expression of efflux pump and ampC. J. Med. Bacteriol. 2, 32-40. Available online at: http://tums.ac.ir/1393/04/18/Sadighian.pdf-mpourmand-2014-07-09-06-33.pdf
255. Quale, J., Bratu, S., Gupta, J., and Landman, D. (2006). Interplay of efflux system, ampC, and oprD expression in carbapenem resistance of Pseudomonas aeruginosa clinical isolates. Antimicrob. Agents Chemother. 50, 1633-1641. doi: 10.1128/AAC.50.5.1633-1641.2006
256. Ramisetty, B. C. M., Ghosh, D., Chowdhury, M. R., and Santhosh, R. S. (2016). What is the link between stringent response, endoribonuclease encoding Type II Toxin-Antitoxin systems and persistence? bioRxiv. Front. Microbiol. 7:1882. doi: 10.1101/069831
257. Ramisse, F., van Delden, C., Gidenne, S., Cavallo, J., and Hernandez, E. (2000). Decreased virulence of a strain of Pseudomonas aeruginosa O12 overexpressing a chromosomal type 1 β-lactamase could be due to reduced expression of cell-to-cell signaling dependent virulence factors. FEMS Immunol. Med. Microbiol. 28, 241-245. doi: 10.1111/j.1574-695X.2000.tb01483.x
258. Rasamiravaka, T., and El Jaziri, M. (2016). Quorum-sensing mechanisms and bacterial response to antibiotics in P. aeruginosa. Curr Microbiol. doi: 10.1007/s00284-016-1101-1
259. Rau, M. H., Hansen, S. K., Johansen, H. K., Thomsen, L. E., Workman, C. T., Nielsen, K. F., et al. (2010). Early adaptive developments of Pseudomonas aeruginosa after the transition from life in the environment to persistent colonization in the airways of human cystic fibrosis hosts. Environ. Microbiol. 12, 1643-1658. doi: 10.1111/j.1462-2920.2010.02211.x
260. Rehm, B. H., Grabert, E., Hein, J., and Winkler, U. K. (1994). Antibody response of rabbits and cystic fibrosis patients to an alginate-specific outer membrane protein of a mucoid strain of Pseudomonas aeruginosa. Microb. Pathog. 16, 43-51. doi: 10.1006/mpat.1994.1004
261. Remminghorst, U., and Rehm, B. H. (2006). Alg44, a unique protein required for alginate biosynthesis in Pseudomonas aeruginosa. FEBS Lett. 580, 3883-3888. doi: 10.1016/j.febslet.2006.05.077
262. Rocker, A., and Meinhart, A. (2016). Type II toxin: antitoxin systems. More than small selfish entities? Curr. Genet. 62, 287-290. doi: 10.1007/s00294-015-0541-7
263. Rojas Murcia, N., Lee, X., Waridel, P., Maspoli, A., Imker, H. J., Chai, T., et al. (2015). The Pseudomonas aeruginosa antimetabolite L-2-amino-4-methoxy-trans-3-butenoic acid (AMB) is made from glutamate and two alanine residues via a thiotemplate-linked tripeptide precursor. Front. Microbiol. 6:170. doi: 10.3389/fmicb.2015.00170
264. Römling, U., and Balsalobre, C. (2012). Biofilm infections, their resilience to therapy and innovative treatment strategies. J. Intern. Med. 272, 541-561. doi: 10.1111/joim.12004
265. Römling, U., Galperin, M. Y., and Gomelsky, M. (2013). Cyclic di-GMP: the first 25 years of a universal bacterial second messenger. Microbiol. Mol. Biol. Rev. 77, 1-52. doi: 10.1128/MMBR.00043-12
266. Rosenfeld, M., Gibson, R. L., McNamara, S., Emerson, J., Burns, J. L., Castile, R., et al. (2001). Early pulmonary infection, inflammation, and clinical outcomes in infants with cystic fibrosis. Pediatr. Pulmonol. 32, 356-366. doi: 10.1002/ppul.1144
267. Rosenthal, V. D., Al-Abdely, H. M., El-Kholy, A. A., AlKhawaja, S. A. A., Leblebicioglu, H., Mehta, Y., et al. (2016). International nosocomial infection control consortium report, data summary of 50 countries for 2010-2015: device-associated module. Am. J. Infect. Control. 44, 1495-1504. doi: 10.1016/j.ajic.2016.08.007
268. Russotto, V., Cortegiani, A., Raineri, S. M., and Giarratano, A. (2015). Bacterial contamination of inanimate surfaces and equipment in the intensive care unit. J. Intensive Care 3, 54. doi: 10.1186/s40560-015-0120-5
269. Ryan, R. P., Fouhy, Y., Lucey, J. F., and Dow, J. M. (2006). Cyclic di-GMP signaling in bacteria: recent advances and new puzzles. J. Bacteriol. 188, 8327-8334. doi: 10.1128/JB.01079-06
270. Sampathkumar, G., Khakimova, M., Chan, T., and Nguyen, D. (2016). "The stringent response and antioxidant defences in Pseudomonas aeruginosa," in Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria, ed F. J. de Bruijn (Hoboken, NJ: John Wiley & Sons, Inc.), 500-506.
271. Schafhauser, J., Lepine, F., McKay, G., Ahlgren, H. G., Khakimova, M., and Nguyen, D. (2014). The stringent response modulates 4-hydroxy-2-alkylquinoline biosynthesis and quorum-sensing hierarchy in Pseudomonas aeruginosa. J. Bacteriol. 196, 1641-1650. doi: 10.1128/JB.01086-13
272. Schalk, I. J., and Guillon, L. (2013). Pyoverdine biosynthesis and secretion in Pseudomonas aeruginosa: implications for metal homeostasis. Environ. Microbiol. 15, 1661-1673. doi: 10.1111/1462-2920.12013
273. Schmiel, D. H., and Miller, V. L. (1999). Bacterial phospholipases and pathogenesis. Microbes Infect 1, 1103-1112. doi: 10.1016/S1286-4579(99)00205-1
274. Schneider, M., Mühlemann, K., Droz, S., Couzinet, S., Casaulta, C., and Zimmerli, S. (2008). Clinical characteristics associated with isolation of small-colony variants of Staphylococcus aureus and Pseudomonas aeruginosa from respiratory secretions of patients with cystic fibrosis. J. Clin. Microbiol. 46, 1832-1834. doi: 10.1128/JCM.00361-08
275. Schroder, K., Hertzog, P. J., Ravasi, T., and Hume, D. A. (2004). Interferon-gamma: an overview of signals, mechanisms and functions. J. Leukoc. Biol. 75, 163-189. doi: 10.1189/jlb.0603252
276. Schurr, M. J., Yu, H., Martinez-Salazar, J. M., Boucher, J. C., and Deretic, V. (1996). Control of AlgU, a member of the sigma E-like family of stress sigma factors, by the negative regulators MucA and MucB and Pseudomonas aeruginosa conversion to mucoidy in cystic fibrosis. J. Bacteriol. 178, 4997-5004. doi: 10.1128/jb.178.16.4997-5004.1996
277. Shih, P. C., and Huang, C. T. (2002). Effects of quorum-sensing deficiency on Pseudomonas aeruginosa biofilm formation and antibiotic resistance. J. Antimicrob. Chemother. 49, 309-314. doi: 10.1093/jac/49.2.309
278. Slater, H., Crow, M., Everson, L., and Salmond, G. P. (2003). Phosphate availability regulates biosynthesis of two antibiotics, prodigiosin and carbapenem, in Serratia via both quorum-sensing-dependent and-independent pathways. Mol. Microbiol. 47, 303-320. doi: 10.1046/j.1365-2958.2003.03295.x
279. Sobel, M. L., Hocquet, D., Cao, L., Plesiat, P., and Poole, K. (2005). Mutations in PA3574 (nalD) lead to increased MexAB-OprM expression and multidrug resistance in laboratory and clinical isolates of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 49, 1782-1786. doi: 10.1128/AAC.49.5.1782-1786.2005
280. Starkey, M., Hickman, J. H., Ma, L. Y., Zhang, N., De Long, S., Hinz, A., et al. (2009). Pseudomonas aeruginosa rugose small-colony variants have adaptations that likely promote persistence in the cystic fibrosis lung. J. Bacteriol. 191, 3492-3503. doi: 10.1128/JB.00119-09
281. Stover, C. K., Pham, X. Q., Erwin, A. L., Mizoguchi, S. D., Warrener, P., Hickey, M. J., et al. (2000). Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 406, 959-964. doi: 10.1038/35023079
282. Strateva, T., and Yordanov, D. (2009). Pseudomonas aeruginosa-a phenomenon of bacterial resistance. J. Med. Microbiol. 58, 1133-1148. doi: 10.1099/jmm.0.009142-0
283. Strempel, N., Neidig, A., Nusser, M., Geffers, R., Vieillard, J., Lesouhaitier, O., et al. (2013). Human host defense peptide LL-37 stimulates virulence factor production and adaptive resistance in Pseudomonas aeruginosa. PLoS ONE 8:e82240. doi: 10.1371/journal.pone.0082240
284. Sullivan, R., Schaus, D., John, M., and Delport, J. A. (2016). Extended spectrum beta-lactamases: a minireview of clinical relevant groups. J. Med. Microb. Diagn. 4:203. doi: 10.4172/2161-0703.1000203
285. Sun, J., Deng, Z., and Yan, A. (2014). Bacterial multidrug efflux pumps: mechanisms, physiology and pharmacological exploitations. Biochem. Biophys. Res. Commun. 453, 254-267. doi: 10.1016/j.bbrc.2014.05.090
286. Sun, S., Zhou, L., Jin, K., Jiang, H., and He, Y. W. (2016). Quorum sensing systems differentially regulate the production of phenazine-1-carboxylic acid in the rhizobacterium Pseudomonas aeruginosa PA1201. Sci. Rep. 6:30352. doi: 10.1038/srep30352
287. Tamber, S., and Hancock, R. E. (2003). On the mechanism of solute uptake in Pseudomonas. Front. Biosci. 8:s472-s483. doi: 10.2741/1075
288. Tian, Z. X., Mac Aogain, M., O'Connor, H. F., Fargier, E., Mooij, M. J., Adams, C., et al. (2009). MexT modulates virulence determinants in Pseudomonas aeruginosa independent of the MexEF-OprN efflux pump. Microb. Pathog. 47, 237-241. doi: 10.1016/j.micpath.2009.08.003
289. Tielen, P., Strathmann, M., Jaeger, K. E., Flemming, H. C., and Wingender, J. (2005). Alginate acetylation influences initial surface colonization by mucoid Pseudomonas aeruginosa. Microbiol. Res. 160, 165-176. doi: 10.1016/j.micres.2004.11.003
290. Toder, D. S., Ferrell, S. J., Nezezon, J. L., Rust, L., and Iglewski, B. H. (1994). lasA and lasB genes of Pseudomonas aeruginosa-Analysis of transcription and gene product activity. Infect. Immun. 62, 1320-1327.
291. Toder, D. S., Gambello, M. J., and Iglewski, B. H. (1991). Pseudomonas aeruginosa LasA: a second elastase under the transcriptional control of lasR. Mol. Microbiol. 5, 2003-2010. doi: 10.1111/j.1365-2958.1991.tb00822.x
292. Trejo-Hernández, A., Andrade-Domínguez, A., Herníndez, M., and Encarnación, S. (2014). Interspecies competition triggers virulence and mutability in Candida albicans-Pseudomonas aeruginosa mixed biofilms. ISME J. 8, 1974-1988. doi: 10.1038/ismej.2014.53
293. Trias, J., and Nikaido, H. (1990). Outer membrane protein D2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 34, 52-57. doi: 10.1128/AAC.34.1.52
294. Trubiano, J. A., and Padiglione, A. A. (2015). Nosocomial infections in the intensive care unit. Anaesth. Intensive Care 16, 598-602. doi: 10.1016/j.mpaic.2015.09.010
295. Turner, K. H., Everett, J., Trivedi, U., Rumbaugh, K. P., and Whiteley, M. (2014). Requirements for Pseudomonas aeruginosa acute burn and chronic surgical wound infection. PLoS Genet. 10:e1004518. doi: 10.1371/journal.pgen.1004518
296. Ueda, A., and Wood, T. K. (2009). Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885). PLoS Pathog. 5:e1000483. doi: 10.1371/journal.ppat.1000483
297. Ueda, A., and Wood, T. K. (2010). Tyrosine phosphatase TpbA of Pseudomonas aeruginosa controls extracellular DNA via cyclic diguanylic acid concentrations. Environ. Microbiol. 2, 449-455. doi: 10.1111/j.1758-2229.2010.00171.x
298. Umadevi, S., Joseph, N. M., Kumari, K., Easow, J. M., Kumar, S., Stephen, S., et al. (2011). Detection of extended spectrum beta lactamases, ampc beta-lactamases and metallobetalactamases in clinical isolates of ceftazidime resistant Pseudomonas aeruginosa. Braz. J. Microbiol. 42, 1284-1288. doi: 10.1590/S1517-83822011000400006
299. Valentini, M., and Filloux, A. (2016). Biofilms and cyclic di-GMP (c-di-GMP) signaling: lessons from Pseudomonas aeruginosa and other bacteria. J. Biol. Chem. 291, 12547-12555. doi: 10.1074/jbc.R115.711507
300. van Belkum, A., Soriaga, L. B., LaFave, M. C., Akella, S., Veyrieras, J. B., Barbu, E. M., et al. (2015). Phylogenetic distribution of CRISPR-Cas systems in antibiotic-resistant Pseudomonas aeruginosa. MBio 6:e01796-15. doi: 10.1128/mBio.01796-15
301. van Delden, C., Comte, R., and Bally, A. M. (2001). Stringent response activates quorum sensing and modulates cell density-dependent gene expression in Pseudomonas aeruginosa. J. Bacteriol. 183, 5376-5384. doi: 10.1128/JB.183.18.5376-5384.2001
302. Van Delden, C., and Iglewski, B. H. (1998). Cell-to-cell signaling and Pseudomonas aeruginosa infections. Emerg. Infect. Dis. 4, 551-560. doi: 10.3201/eid0404.980405
303. Van Gennip, M., Christensen, L. D., Alhede, M., Phipps, R., Jensen, P. Ø., Christophersen, L., et al. (2009). Inactivation of the rhlA gene in Pseudomonas aeruginosa prevents rhamnolipid production, disabling the protection against polymorphonuclear leukocytes. APMIS 117, 537-546. doi: 10.1111/j.1600-0463.2009.02466.x
304. Van Melderen, L. (2010). Toxin-antitoxin systems: why so many, what for? Curr. Opin. Microbiol. 13, 781-785. doi: 10.1016/j.mib.2010.10.006
305. Varga, J. J., Barbier, M., Mulet, X., Bielecki, P., Bartell, J. A., Owings, J. P., et al. (2015). Genotypic and phenotypic analyses of a Pseudomonas aeruginosa chronic bronchiectasis isolate reveal differences from cystic fibrosis and laboratory strains. BMC Genomics 16:883. doi: 10.1186/s12864-015-2069-0
306. Venter, H., Mowla, R., Ohene-Agyei, T., and Ma, S. (2015). RND-type drug e fflux pumps from Gram-negative bacteria: molecular mechanism and inhibition. Front. Microbiol. 6:377. doi: 10.3389/fmicb.2015.00377
307. Venturi, V. (2006). Regulation of quorum sensing in Pseudomonas. FEMS Microbiol. Rev. 30, 274-291. doi: 10.1111/j.1574-6976.2005.00012.x
308. Viducic, D., Ono, T., Murakami, K., Susilowati, H., Kayama, S., Hirota, K., et al. (2006). Functional analysis of spoT, relA and dksA genes on quinolone tolerance in Pseudomonas aeruginosa under nongrowing condition. Microbiol. Immunol. 50, 349-357. doi: 10.1111/j.1348-0421.2006.tb03793.x
309. Visca, P., Imperi, F., and Lamont, I. L. (2007). Pyoverdine siderophores: from biogenesis to biosignificance. Trends Microbiol. 15, 22-30. doi: 10.1016/j.tim.2006.11.004
310. Vogt, S. L., Green, C., Stevens, K. M., Day, B., Erickson, D. L., Woods, D. E., et al. (2011). The stringent response is essential for Pseudomonas aeruginosa virulence in the rat lung agar bead and Drosophila melanogaster feeding models of infection. Infect. Immun. 79, 4094-4104. doi: 10.1128/IAI.00193-11
311. Wagner, V. E., Bushnell, D., Passador, L., Brooks, A. I, and Iglewski, B. H. (2003). Microarray analysis of Pseudomonas aeruginosa quorum-sensing regulons: effects of growth phase and environment. J. Bacteriol. 185, 2080-2095. doi: 10.1128/JB.185.7.2080-2095.2003
312. Wang, H., Tu, F., Gui, Z., Lu, X., and Chu, W. (2013). Antibiotic resistance profiles and quorum sensing-dependent virulence factors in clinical isolates of Pseudomonas aeruginosa. Indian J. Microbiol. 53, 163-167. doi: 10.1007/s12088-013-0370-7
313. Wang, S., Parsek, M. R., Wozniak, D. J., and Ma, L. Z. (2013). A spider web strategy of type IV pili-mediated migration to build a fibre-like Psl polysaccharide matrix in Pseudomonas aeruginosa biofilms. Environ. Microbiol. 15, 2238-2253. doi: 10.1111/1462-2920.12095
314. Wang, X., and Wood, T. K. (2011). Toxin-antitoxin systems influence biofilm and persister cell formation and the general stress response. Appl. Environ. Microbiol. 77, 5577-5583. doi: 10.1128/AEM.05068-11
315. Wang, X. X., Lord, D. M., Cheng, H. Y., Osbourne, D. O., Hong, S. H., Sanchez-Torres, V., et al. (2012). A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS. Nat. Chem. Biol. 8, 855-861. doi: 10.1038/nchembio.1062
316. Wang, Y., Hay, I. D., Rehman, Z. U., and Rehm, B. H. (2015). Membrane-anchored MucR mediates nitrate-dependent regulation of alginate production in Pseudomonas aeruginosa. Appl. Microbiol. Biotechnol. 99, 7253-7265. doi: 10.1007/s00253-015-6591-4
317. Wei, Q., Tarighi, S., Dotsch, A., Haussler, S., Müsken, M., Wright, V. J., et al. (2011). Phenotypic and genome-wide analysis of an antibiotic-resistant small colony variant (SCV) of Pseudomonas aeruginosa. PLoS ONE 6:e29276. doi: 10.1371/journal.pone.0029276
318. Wen, Y. R., Behiels, E., and Devreese, B. (2014). Toxin-Antitoxin systems: their role in persistence, biofilm formation, and pathogenicity. Pathog. Dis. 70, 240-249. doi: 10.1111/2049-632X.12145
319. Whiteley, M., Lee, K. M., and Greenberg, E. P. (1999). Identification of genes controlled by quorum sensing in Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. U.S.A. 96, 13904-13909. doi: 10.1073/pnas.96.24.13904
320. Williams, J. J., Halvorsen, E. M., Dwyer, E. M., DiFazio, R. M., and Hergenrother, P. J. (2011). Toxin-antitoxin (TA) systems are prevalent and transcribed in clinical isolates of Pseudomonas aeruginosa and methicillin-resistant Staphylococcus aureus. FEMS Microbiol. Lett. 322, 41-50. doi: 10.1111/j.1574-6968.2011.02330.x
321. Williams, P., and Camara, M. (2009). Quorum sensing and environmental adaptation in Pseudomonas aeruginosa: a tale of regulatory networks and multifunctional signal molecules. Curr. Opin. Microbiol. 12, 182-191. doi: 10.1016/j.mib.2009.01.005
322. Winstanley, C., O'Brien, S., and Brockhurst, M. A. (2016). Pseudomonas aeruginosa evolutionary adaptation and diversification in cystic fibrosis chronic lung infections. Trends Microbiol. 24, 327-337. doi: 10.1016/j.tim.2016.01.008
323. Wittgens, A., Tiso, T., Arndt, T. T., Wenk, P., Hemmerich, J., Müller, C., et al. (2011). Growth independent rhamnolipid production from glucose using the non-pathogenic Pseudomonas putida KT2440. Microb. Cell Fact. 10:80. doi: 10.1186/1475-2859-10-80
324. Wong, A., Rodrigue, N., and Kassen, R. (2012). Genomics of adaptation during experimental evolution of the opportunistic pathogen Pseudomonas aeruginosa. PLoS Genet. 8:e1002928. doi: 10.1371/journal.pgen.1002928
325. Wood, T. L., and Wood, T. K. (2016). The HigB/HigA toxin/antitoxin system of Pseudomonas aeruginosa influences the virulence factors pyochelin, pyocyanin, and biofilm formation. Microbiologyopen 5, 499-511. doi: 10.1002/mbo3.346
326. Workentine, M. L., Sibley, C. D., Glezerson, B., Purighalla, S., Norgaard-Gron, J. C., Parkins, M. D., et al. (2013). Phenotypic heterogeneity of Pseudomonas aeruginosa populations in a cystic fibrosis patient. PLoS ONE 8:e60225. doi: 10.1371/journal.pone.0060225
327. Worlitzsch, D., Tarran, R., Ulrich, M., Schwab, U., Cekici, A., Meyer, K. C., et al. (2002). Effects of reduced mucus oxygen concentration in airway Pseudomonas infections of cystic fibrosis patients. J. Clin. Invest. 109, 317-325. doi: 10.1172/JCI0213870
328. van't Wout, E. F. A., van Schadewijk, A., van Boxtel, R., Dalton, L. E., Clarke, H. J., Tommassen, J., et al. (2015). Virulence factors of Pseudomonas aeruginosa induce both the unfolded protein and integrated stress responses in airway epithelial cells. PLoS Pathog. 11:e1004946. doi: 10.1371/journal.ppat.1004946
329. Wu, J., Long, Q., and Xie, J. (2010). (p)ppGpp and drug resistance. J. Cell. Physiol. 224, 300-304. doi: 10.1002/jcp.22158
330. Wu, L., Estrada, O., Zaborina, O., Bains, M., Shen, L., Kohler, J. E., et al. (2005). Recognition of host immune activation by Pseudomonas aeruginosa. Science 309, 774-777. doi: 10.1126/science.1112422
331. Xiong, Y. Q., Caillon, J., Drugeon, H., Potel, G., and Baron, D. (1996). Influence of pH on adaptive resistance of Pseudomonas aeruginosa to aminoglycosides and their postantibiotic effects. Antimicrob. Agents Chemother. 40, 35-39.
332. Ye, L., Cornelis, P., Guillemyn, K., Ballet, S., and Hammerich, O. (2014). Structure revision of N-mercapto-4-formylcarbostyril produced by Pseudomonas fluorescens G308 to 2-(2-hydroxyphenyl)thiazole-4-carbaldehyde [aeruginaldehyde]. Nat. Prod. Commun. 9, 789-794.
333. Yoon, S. S., Hennigan, R. F., Hilliard, G. M., Ochsner, U. A., Parvatiyar, K., Kamani, M. C., et al. (2002). Pseudomonas aeruginosa anaerobic respiration in biofilms: relationships to cystic fibrosis pathogenesis. Dev. Cell 3, 593-603. doi: 10.1016/S1534-5807(02)00295-2
334. Zaborin, A., Romanowski, K., Gerdes, S., Holbrook, C., Lepine, F., Long, J., et al. (2009). Red death in Caenorhabditis elegans caused by Pseudomonas aeruginosa PAO1. Proc. Natl. Acad. Sci. U.S.A. 106, 6327-6332. doi: 10.1073/pnas.0813199106
335. Zegans, M. E., Wagner, J. C., Cady, K. C., Murphy, D. M., Hammond, J. H., and O'Toole, G. A. (2009). Interaction between bacteriophage DMS3 and host CRISPR region inhibits group behaviors of Pseudomonas aeruginosa. J. Bacteriol. 191, 210-219. doi: 10.1128/JB.00797-08
336. Zegans, M. E., Wozniak, D., Griffin, E., Toutain-Kidd, C. M., Hammond, J. H., Garfoot, A., et al. (2012). Pseudomonas aeruginosa exopolysaccharide Psl promotes resistance to the biofilm inhibitor polysorbate 80. Antimicrob. Agents Chemother. 56, 4112-4122. doi: 10.1128/AAC.00373-12
337. Zhang, L., Li, X. Z., and Poole, K. (2001). Fluoroquinolone susceptibilities of efflux-mediated multidrug-resistant Pseudomonas aeruginosa, Stenotrophomonas maltophilia and Burkholderia cepacia. J. Antimicrob. Chemother. 48, 549-552. doi: 10.1093/jac/48.4.549
338. Zhao, J., Jiang, H., Cheng, W., Wu, J., Wang, J., and Dong, L. (2015). The role of quorum sensing system in antimicrobial induced ampC expression in Pseudomonas aeruginosa biofilm. J. Basic Microbiol. 55, 671-678. doi: 10.1002/jobm.201300987
339. Zhao, K., Tseng, B. S., Beckerman, B., Jin, F., Gibiansky, M. L., Harrison, J. J., et al. (2013). Psl trails guide exploration and microcolony formation in Pseudomonas aeruginosa biofilms. Nature 497, 388-391. doi: 10.1038/nature12155
340. Zhu, K., and Rock, C. O. (2008). RhlA converts β-hydroxyacyl-acyl carrier protein intermediates in fatty acid synthesis to the β-hydroxydecanoyl-β-hydroxydecanoate component of rhamnolipids in Pseudomonas aeruginosa. J. Bacteriol. 190, 3147-3154. doi: 10.1128/JB.00080-08