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The Scientific World Journal
Volume 2012, Article ID 402919, 18 pages
http://dx.doi.org/10.1100/2012/402919
Research Article

Vesiculation from Pseudomonas aeruginosa under SOS

1Department of Biology, The University of Texas at San Antonio, One UTSA Circle, San Antonio, TX 78249, USA
2Pediatric Biochemistry Laboratory, The University of Texas at San Antonio, San Antonio, TX 78249, USA
3Department of Biology, The University of Texas at San Antonio, San Antonio, TX 78249, USA
4Department of Chemistry, The University of Texas at San Antonio, San Antonio, TX 78249, USA
5RCMI Proteomics, The University of Texas at San Antonio, San Antonio, TX 78249, USA
6Protein Biomarkers Cores, The University of Texas at San Antonio, San Antonio, TX 78249, USA
7Center for Research and Training in the Sciences, The University of Texas at San Antonio, San Antonio, TX 78249, USA
8Division of Hematology and Medical Oncology, Department of Medicine, Cancer Therapy and Research Center, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA

Received 3 October 2011; Accepted 23 October 2011

Academic Editor: Paul Cos

Copyright © 2012 Reshma Maredia et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. M. D. Obritsch, D. N. Fish, R. MacLaren, and R. Jung, “Nosocomial infections due to multidrug-resistant Pseudomonas aeruginosa: epidemiology and treatment options,” Pharmacotherapy, vol. 25, no. 10, pp. 1353–1364, 2005. View at Publisher · View at Google Scholar · View at Scopus
  2. J. W. Costerton, P. S. Stewart, and E. P. Greenberg, “Bacterial biofilms: a common cause of persistent infections,” Science, vol. 284, no. 5418, pp. 1318–1322, 1999. View at Publisher · View at Google Scholar · View at Scopus
  3. R. M. Donlan and J. W. Costerton, “Biofilms: survival mechanisms of clinically relevant microorganisms,” Clinical Microbiology Reviews, vol. 15, no. 2, pp. 167–193, 2002. View at Publisher · View at Google Scholar · View at Scopus
  4. P. Bielecki, J. Glik, M. Kawecki, and V. A. P. M. dos Santos, “Towards understanding Pseudomonas aeruginosa burn wound infections by profiling gene expression,” Biotechnology Letters, vol. 30, no. 5, pp. 777–790, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. J. H. Calhoun, C. K. Murray, and M. M. Manring, “Multidrug-resistant organisms in military wounds from Iraq and Afghanistan,” Clinical Orthopaedics and Related Research, vol. 466, no. 6, pp. 1356–1362, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. T. J. Beveridge, “Structures of Gram-negative cell walls and their derived membrane vesicles,” Journal of Bacteriology, vol. 181, no. 16, pp. 4725–4733, 1999. View at Google Scholar · View at Scopus
  7. D. Mayrand and D. Grenier, “Biological activities of outer membrane vesicles,” Canadian Journal of Microbiology, vol. 35, no. 6, pp. 607–613, 1989. View at Google Scholar · View at Scopus
  8. J. M. Bomberger, D. P. MacEachran, B. A. Coutermarsh, S. Ye, G. A. O'Toole, and B. A. Stanton, “Long-distance delivery of bacterial virulence factors by pseudomonas aeruginosa outer membrane vesicles,” PLoS Pathogens, vol. 5, no. 4, Article ID e1000382, 2009. View at Publisher · View at Google Scholar · View at Scopus
  9. N. Katsui, T. Tsuchido, R. Hiramatsu, S. Fujikawa, M. Takano, and I. Shibasaki, “Heat-induced blebbing and vesiculation of the outer membrane of Escherichia coli,” Journal of Bacteriology, vol. 151, no. 3, pp. 1523–1531, 1982. View at Google Scholar
  10. H. Nikaido, “Isolation of outer membranes,” Methods in Enzymology, vol. 235, pp. 225–234, 1994. View at Publisher · View at Google Scholar · View at Scopus
  11. S. S. Thompson, Y. M. Naidu, and J. J. Pestka, “Ultrastructural localization of an extracellular protease in Pseudomonas fragi by using the peroxidase-antiperoxidase reaction,” Applied and Environmental Microbiology, vol. 50, no. 4, pp. 1038–1042, 1985. View at Google Scholar · View at Scopus
  12. T. Kogoma, T. A. Torrey, and M. J. Connaughton, “Induction of UV-resistant DNA replication in Escherichia coli: induced stable DNA replication as an SOS function,” Molecular and General Genetics, vol. 176, no. 1, pp. 1–9, 1979. View at Google Scholar · View at Scopus
  13. H. I. Miller, M. Kirk, and H. Echols, “SOS induction and autoregulation of the himA gene for site-specific recombination in Escherichia coli,” Proceedings of the National Academy of Sciences of the United States of America, vol. 78, no. 11, pp. 6754–6758, 1981. View at Google Scholar · View at Scopus
  14. S. Dutta, K. I. Iida, A. Takade, Y. Meno, G. B. Nair, and S. I. Yoshida, “Release of Shiga toxin by membrane vesicles in Shigella dysenteriae serotype 1 strains and in vitro effects of antimicrobials on toxin production and release,” Microbiology and Immunology, vol. 48, no. 12, pp. 965–969, 2004. View at Google Scholar · View at Scopus
  15. P. L. Wagner, J. Livny, M. N. Neely, D. W. K. Acheson, D. I. Friedman, and M. K. Waldor, “Bacteriophage control of Shiga toxin 1 production and release by Escherichia coli,” Molecular Microbiology, vol. 44, no. 4, pp. 957–970, 2002. View at Publisher · View at Google Scholar · View at Scopus
  16. A. J. McBroom and M. J. Kuehn, “Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response,” Molecular Microbiology, vol. 63, no. 2, pp. 545–558, 2007. View at Publisher · View at Google Scholar · View at Scopus
  17. G. C. Walker, “Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli,” Microbiological Reviews, vol. 48, no. 1, pp. 60–93, 1984. View at Google Scholar · View at Scopus
  18. J. Courcelle, A. Khodursky, B. Peter, P. O. Brown, and P. C. Hanawalt, “Comparative gene expression profiles following UV exposure in wild-type and SOS-deficient Escherichia coli,” Genetics, vol. 158, no. 1, pp. 41–64, 2001. View at Google Scholar
  19. A. R. F. de Henestrosa, T. Ogi, S. Aoyagi et al., “Identification of additional genes belonging to the LexA regulon in Escherichia coli,” Molecular Microbiology, vol. 35, no. 6, pp. 1560–1572, 2000. View at Publisher · View at Google Scholar · View at Scopus
  20. P. P. Khil and R. D. Camerini-Otero, “Over 1000 genes are involved in the DNA damage response of Escherichia coli,” Molecular Microbiology, vol. 44, no. 1, pp. 89–105, 2002. View at Publisher · View at Google Scholar · View at Scopus
  21. R. T. Cirz, B. M. O'Neill, J. A. Hammond, S. R. Head, and F. E. Romesberg, “Defining the Pseudomonas aeruginosa SOS response and its role in the global response to the antibiotic ciprofloxacin,” Journal of Bacteriology, vol. 188, no. 20, pp. 7101–7110, 2006. View at Publisher · View at Google Scholar · View at Scopus
  22. K. Drlica and X. Zhao, “DNA gyrase, topoisomerase IV, and the 4-quinolones,” Microbiology and Molecular Biology Reviews, vol. 61, no. 3, pp. 377–392, 1997. View at Google Scholar · View at Scopus
  23. P. M. Hawkey, “Mechanisms of quinolone action and microbial response,” Journal of Antimicrobial Chemotherapy, vol. 51, no. 1, pp. 29–35, 2003. View at Publisher · View at Google Scholar · View at Scopus
  24. M. Sassanfar and J. W. Roberts, “Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication,” Journal of Molecular Biology, vol. 212, no. 1, pp. 79–96, 1990. View at Publisher · View at Google Scholar · View at Scopus
  25. J. W. Little, “Mechanism of specific LexA cleavage: autodigestion and the role of RecA coprotease,” Biochimie, vol. 73, no. 4, pp. 411–421, 1991. View at Publisher · View at Google Scholar · View at Scopus
  26. M. M. Cox, “A broadening view of recombinational DNA repair in bacteria,” Genes to Cells, vol. 3, no. 2, pp. 65–78, 1998. View at Publisher · View at Google Scholar · View at Scopus
  27. D. J. Sherratt, “Bacterial chromosome dynamics,” Science, vol. 301, no. 5634, pp. 780–785, 2003. View at Publisher · View at Google Scholar · View at Scopus
  28. B. L. Deatherage, J. C. Lara, T. Bergsbaken, S. L. R. Barrett, S. Lara, and B. T. Cookson, “Biogenesis of bacterial membrane vesicles,” Molecular Microbiology, vol. 72, no. 6, pp. 1395–1407, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. T. Dörr, K. Lewis, and M. Vulić, “SOS response induces persistence to fluoroquinolones in Escherichia coli,” PLoS Genetics, vol. 5, no. 12, Article ID e1000760, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. H. Gotoh, Y. Zhang, S. F. Dallo, S. Hong, N. Kasaraneni, and T. Weitao, “Pseudomonas aeruginosa, under DNA replication inhibition, tends to form biofilms via Arr,” Research in Microbiology, vol. 159, no. 4, pp. 294–302, 2008. View at Publisher · View at Google Scholar · View at Scopus
  31. T. Weitao, K. Nordström, and S. Dasgupta, “Mutual suppression of mukB and seqA phenotypes might arise from their opposing influences on the Escherichia coli nucleoid structure,” Molecular Microbiology, vol. 34, no. 1, pp. 157–168, 1999. View at Publisher · View at Google Scholar · View at Scopus
  32. R. C. Alaniz, B. L. Deatherage, J. C. Lara, and B. T. Cookson, “Membrane vesicles are immunogenic facsimiles of Salmonella typhimurium that potently activate dendritic cells, prime B and T cell responses, and stimulate protective immunity in vivo,” Journal of Immunology, vol. 179, no. 11, pp. 7692–7701, 2007. View at Google Scholar · View at Scopus
  33. G. F. Ames, “Lipids of Salmonella typhimurium and Escherichia coli: structure and metabolism,” Journal of Bacteriology, vol. 95, no. 3, pp. 833–843, 1968. View at Google Scholar · View at Scopus
  34. S. O. Kwon, Y. S. Gho, J. C. Lee, and S. I. Kim, “Proteome analysis of outer membrane vesicles from a clinical Acinetobacter baumannii isolate,” FEMS Microbiology Letters, vol. 297, no. 2, pp. 150–156, 2009. View at Publisher · View at Google Scholar · View at Scopus
  35. V. Venketaraman, A. K. Lin, A. Le, S. C. Kachlany, N. D. Connell, and J. B. Kaplan, “Both leukotoxin and poly-N-acetylglucosamine surface polysaccharide protect Aggregatibacter actinomycetemcomitans cells from macrophage killing,” Microbial Pathogenesis, vol. 45, no. 3, pp. 173–180, 2008. View at Publisher · View at Google Scholar · View at Scopus
  36. M. Wilm, A. Shevchenko, T. Houthaeve et al., “Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry,” Nature, vol. 379, no. 6564, pp. 466–469, 1996. View at Google Scholar · View at Scopus
  37. J. Sambrook, E. F. Fritsch, and T. Maniatis, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA, 2nd edition, 2001.
  38. J. N. Williams, P. J. Skipp, H. E. Humphries, M. Christodoulides, C. D. O'Connor, and J. E. Heckels, “Proteomic analysis of outer membranes and vesicles from wild-type serogroup B Neisseria meningitidis and a lipopolysaccharide-deficient mutant,” Infection and Immunity, vol. 75, no. 3, pp. 1364–1372, 2007. View at Publisher · View at Google Scholar · View at Scopus
  39. D. J. C. Pappin, P. Hojrup, and A. J. Bleasby, “Rapid identification of proteins by peptide-mass fingerprinting,” Current Biology, vol. 3, no. 6, pp. 327–332, 1993. View at Google Scholar · View at Scopus
  40. H. Gotoh, N. Kasaraneni, N. Devineni, S. F. Dallo, and T. Weitao, “SOS involvement in stress-inducible biofilm formation,” Biofouling, vol. 26, no. 5, pp. 603–611, 2010. View at Google Scholar
  41. O. Huisman, R. D'Ari, and S. Gottesman, “Cell-division control in Escherichia coli: specific induction of the SOS function SfiA protein is sufficient to block septation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 81, no. 14, pp. 4490–4494, 1984. View at Google Scholar · View at Scopus
  42. C. Jones and I. B. Holland, “Role of the SulB (FtsZ) protein in division inhibition during the SOS response in Escherichia coli: FtsZ stabilizes the inhibitor SulA in maxicells,” Proceedings of the National Academy of Sciences of the United States of America, vol. 82, no. 18, pp. 6045–6049, 1985. View at Google Scholar · View at Scopus
  43. J. F. Lutkenhaus, “Coupling of DNA replication and cell division: sulB is an allele of ftsZ,” Journal of Bacteriology, vol. 154, no. 3, pp. 1339–1346, 1983. View at Google Scholar · View at Scopus
  44. Y. Tashiro, R. Sakai, M. Toyofuku et al., “Outer membrane machinery and alginate synthesis regulators control membrane vesicle production in Pseudomonas aeruginosa,” Journal of Bacteriology, vol. 191, no. 24, pp. 7509–7519, 2009. View at Publisher · View at Google Scholar · View at Scopus
  45. T. N. Ellis and M. J. Kuehn, “Virulence and immunomodulatory roles of bacterial outer membrane vesicles,” Microbiology and Molecular Biology Reviews, vol. 74, no. 1, pp. 81–94, 2010. View at Publisher · View at Google Scholar · View at Scopus
  46. X. Peng, C. Xu, H. Ren, X. Lin, L. Wu, and S. Wang, “Proteomic analysis of the sarcosine-insoluble outer membrane fraction of Pseudomonas aeruginosa responding to ampicilin, kanamycin, and tetracycline resistance,” Journal of Proteome Research, vol. 4, no. 6, pp. 2257–2265, 2005. View at Publisher · View at Google Scholar · View at Scopus
  47. C. Xu, X. Lin, H. Ren, Y. Zhang, S. Wang, and X. Peng, “Analysis of outer membrane proteome of Escherichia coli related to resistance to ampicillin and tetracycline,” Proteomics, vol. 6, no. 2, pp. 462–473, 2006. View at Publisher · View at Google Scholar · View at Scopus
  48. J. L. Kadurugamuwa and T. J. Beveridge, “Virulence factors are released from Pseudomonas aeruginosa in association with membrane vesicles during normal growth and exposure to gentamicin: a novel mechanism of enzyme secretion,” Journal of Bacteriology, vol. 177, no. 14, pp. 3998–4008, 1995. View at Google Scholar · View at Scopus
  49. M. Nevot, V. Deroncelé, P. Messner, J. Guinea, and E. Mercadé, “Characterization of outer membrane vesicles released by the psychrotolerant bacterium Pseudoalteromonas antarctica NF3,” Environmental Microbiology, vol. 8, no. 9, pp. 1523–1533, 2006. View at Publisher · View at Google Scholar · View at Scopus
  50. S. J. Bauman and M. J. Kuehn, “Purification of outer membrane vesicles from Pseudomonas aeruginosa and their activation of an IL-8 response,” Microbes and Infection, vol. 8, no. 9-10, pp. 2400–2408, 2006. View at Publisher · View at Google Scholar · View at Scopus
  51. D. S. Choi, D. K. Kim, S. J. Choi et al., “Proteomic analysis of outer membrane vesicles derived from Pseudomonas aeruginosa,” Proteomics, vol. 11, no. 16, pp. 3424–3429, 2011. View at Publisher · View at Google Scholar
  52. G. Ferrari, I. Garaguso, J. Adu-Bobie et al., “Outer membrane vesicles from group B Neisseria meningitidis Δgna33 mutant: proteomic and immunological comparison with detergent-derived outer membrane vesicles,” Proteomics, vol. 6, no. 6, pp. 1856–1866, 2006. View at Publisher · View at Google Scholar · View at Scopus
  53. L. Wang and J. Lutkenhaus, “FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response,” Molecular Microbiology, vol. 29, no. 3, pp. 731–740, 1998. View at Publisher · View at Google Scholar · View at Scopus
  54. J. A. Imlay and S. Linn, “Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide,” Journal of Bacteriology, vol. 169, no. 7, pp. 2967–2976, 1987. View at Google Scholar · View at Scopus
  55. J. Overhage, M. Bains, M. D. Brazas, and R. E. W. Hancock, “Swarming of Pseudomonas aeruginosa is a complex adaptation leading to increased production of virulence factors and antibiotic resistance,” Journal of Bacteriology, vol. 190, no. 8, pp. 2671–2679, 2008. View at Publisher · View at Google Scholar · View at Scopus
  56. K. Poole, K. Krebes, C. McNally, and S. Neshat, “Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon,” Journal of Bacteriology, vol. 175, no. 22, pp. 7363–7372, 1993. View at Google Scholar · View at Scopus
  57. B. A. Cowell, S. S. Twining, J. A. Hobden, M. S. F. Kwong, and S. M. J. Fleiszig, “Mutation of lasA and lasB reduces Pseudomonas aeruginosa invasion of epithelial cells,” Microbiology, vol. 149, no. 8, pp. 2291–2299, 2003. View at Google Scholar · View at Scopus
  58. H. B. Tang, E. Dimango, R. Bryan et al., “Contribution of specific Pseudomonas aeruginosa virulence factors to pathogenesis of pneumonia in a neonatal mouse model of infection,” Infection and Immunity, vol. 64, no. 1, pp. 37–43, 1996. View at Google Scholar · View at Scopus
  59. S. S. Twining, S. E. Kirschner, L. A. Mahnke, and D. W. Frank, “Effect of Pseudomonas aeruginosa elastase, alkaline protease, and exotoxin A on corneal proteinases and proteins,” Investigative Ophthalmology and Visual Science, vol. 34, no. 9, pp. 2699–2712, 1993. View at Google Scholar · View at Scopus
  60. O. Zaborina, N. Dhiman, M. L. Chen, J. Kostal, I. A. Holder, and A. M. Chakrabarty, “Secreted products of a nonmucoid Pseudomonas aeruginosa strain induce two modes of macrophage killing: external-ATP-dependent, P2Z-receptor-mediated necrosis and ATP-independent, caspase-mediated apoptosis,” Microbiology, vol. 146, no. 10, pp. 2521–2530, 2000. View at Google Scholar · View at Scopus
  61. J. B. McPhee, S. Tamber, M. Bains et al., “The major outer membrane protein OprG of Pseudomonas aeruginosa contributes to cytotoxicity and forms an anaerobically regulated, cation-selective channel,” FEMS Microbiology Letters, vol. 296, no. 2, pp. 241–247, 2009. View at Publisher · View at Google Scholar · View at Scopus
  62. G. Buist, A. Steen, J. Kok, and O. P. Kuipers, “LysM, a widely distributed protein motif for binding to (peptido)glycans,” Molecular Microbiology, vol. 68, no. 4, pp. 838–847, 2008. View at Publisher · View at Google Scholar · View at Scopus
  63. E. Y. Lee, D. S. Choi, K. P. Kim, and Y. S. Gho, “Proteomics in Gram-negative bacterial outer membrane vesicles,” Mass Spectrometry Reviews, vol. 27, no. 6, pp. 535–555, 2008. View at Publisher · View at Google Scholar · View at Scopus
  64. J. J. Davie and A. A. Campagnari, “Comparative proteomic analysis of the haemophilus ducreyi porin-deficient mutant 35000HP::P2AB,” Journal of Bacteriology, vol. 191, no. 7, pp. 2144–2152, 2009. View at Publisher · View at Google Scholar · View at Scopus
  65. A. Frisk, C. A. Ison, and T. Lagergård, “GroEL heat shock protein of Haemophilus ducreyi: association with cell surface and capacity to bind to eukaryotic cells,” Infection and Immunity, vol. 66, no. 3, pp. 1252–1257, 1998. View at Google Scholar · View at Scopus
  66. G. Kumar, P. Sharma, G. Rathore, D. Bisht, and U. Sengupta, “Proteomic analysis of outer membrane proteins of Edwardsiella tarda,” Journal of Applied Microbiology, vol. 108, no. 6, pp. 2214–2221, 2010. View at Publisher · View at Google Scholar · View at Scopus
  67. S. F. Dallo, B. Zhang, J. Denno et al., “Association of Acinetobacter baumannii EF-Tu with cell surface, outer membrane vesicles and fibronectin,” . In press.
  68. T. Hesterkamp and B. Bukau, “The Escherichia coli trigger factor,” FEBS Letters, vol. 389, no. 1, pp. 32–34, 1996. View at Publisher · View at Google Scholar
  69. W. R. Lyon, C. M. Gibson, and M. G. Caparon, “A role for Trigger factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes,” EMBO Journal, vol. 17, no. 21, pp. 6263–6275, 1998. View at Publisher · View at Google Scholar · View at Scopus
  70. S. Vorderwülbecke, G. Kramer, F. Merz et al., “Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK,” FEBS Letters, vol. 559, no. 1–3, pp. 181–187, 2004. View at Publisher · View at Google Scholar · View at Scopus
  71. O. Kandror, M. Sherman, and A. Goldberg, “Rapid degradation of an abnormal protein in Escherichia coli proceeds through repeated cycles of association with GroEL,” Journal of Biological Chemistry, vol. 274, no. 53, pp. 37743–37749, 1999. View at Publisher · View at Google Scholar · View at Scopus
  72. O. Kandror, M. Sherman, R. Moerschell, and A. L. Goldberg, “Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides,” Journal of Biological Chemistry, vol. 272, no. 3, pp. 1730–1734, 1997. View at Publisher · View at Google Scholar · View at Scopus
  73. O. Kandror, M. Sherman, M. Rhode, and A. L. Goldberg, “Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins,” EMBO Journal, vol. 14, no. 23, pp. 6021–6027, 1995. View at Google Scholar · View at Scopus
  74. G. L. Kolling and K. R. Matthews, “Export of virulence genes and Shiga toxin by membrane vesicles of Escherichia coli O157:H7,” Applied and Environmental Microbiology, vol. 65, no. 5, pp. 1843–1848, 1999. View at Google Scholar · View at Scopus
  75. M. Renelli, V. Matias, R. Y. Lo, and T. J. Beveridge, “DNA-containing membrane vesicles of Pseudomonas aeruginosa PAO1 and their genetic transformation potential,” Microbiology, vol. 150, no. 7, pp. 2161–2169, 2004. View at Google Scholar · View at Scopus
  76. Z. Li, A. J. Clarke, and T. J. Beveridge, “A major autolysin of Pseudomonas aeruginosa: subcellular distribution, potential role in cell growth and division, and secretion in surface membrane vesicles,” Journal of Bacteriology, vol. 178, no. 9, pp. 2479–2488, 1996. View at Google Scholar · View at Scopus
  77. A. J. McBroom, A. P. Johnson, S. Vemulapalli, and M. J. Kuehn, “Outer membrane vesicle production by Escherichia coli is independent of membrane instability,” Journal of Bacteriology, vol. 188, no. 15, pp. 5385–5392, 2006. View at Publisher · View at Google Scholar · View at Scopus
  78. D. Mug-Opstelten and B. Witholt, “Preferential release of new outer membrane fragments by exponentially growing Escherichia coli,” Biochimica et Biophysica Acta, vol. 508, no. 2, pp. 287–295, 1978. View at Google Scholar · View at Scopus
  79. L. Zhou, R. Srisatjaluk, D. E. Justus, and R. J. Doyle, “On the origin of membrane vesicles in Gram-negative bacteria,” FEMS Microbiology Letters, vol. 163, no. 2, pp. 223–228, 1998. View at Publisher · View at Google Scholar · View at Scopus
  80. T. M. Hill, B. Sharma, M. Valjavec-Gratian, and J. Smith, “sfi-Independent filamentation in Escherichia coli is lexA dependent and requires DNA damage for induction,” Journal of Bacteriology, vol. 179, no. 6, pp. 1931–1939, 1997. View at Google Scholar · View at Scopus
  81. D. Trusca, S. Scott, C. Thompson, and D. Bramhill, “Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein,” Journal of Bacteriology, vol. 180, no. 15, pp. 3946–3953, 1998. View at Google Scholar · View at Scopus
  82. S. C. Cordell, E. J. H. Robinson, and J. Löwe, “Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 13, pp. 7889–7894, 2003. View at Publisher · View at Google Scholar · View at Scopus
  83. T. K. Lu and J. J. Collins, “Engineered bacteriophage targeting gene networks as adjuvants for antibiotic therapy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 12, pp. 4629–4634, 2009. View at Publisher · View at Google Scholar · View at Scopus