- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
Interdisciplinary Perspectives on Infectious Diseases
Volume 2012 (2012), Article ID 843509, 10 pages
Pyoverdine, the Major Siderophore in Pseudomonas aeruginosa, Evades NGAL Recognition
1School of Chemistry & Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA
2Division of Pulmonology, Allergy/Immunology, Cystic Fibrosis, and Sleep, Department of Pediatrics and Emory+Children’s Center for Cystic Fibrosis Research, Emory University School of Medicine and Children’s Healthcare of Atlanta, Atlanta, GA 30322, USA
Received 27 May 2012; Accepted 26 July 2012
Academic Editor: Adalberto R. Santos
Copyright © 2012 Mary E. Peek 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.
- P. Visca, F. Imperi, and I. L. Lamont, “Pyoverdine siderophores: from biogenesis to biosignificance,” Trends in Microbiology, vol. 15, no. 1, pp. 22–30, 2007.
- C. Cigana, L. Curcuru, M. R. Leone et al., “Pseudomonas aeruginosa exploits lipid a and muropeptides modification as a strategy to lower innate immunity during cystic fibrosis lung infection,” PLoS ONE, vol. 4, no. 12, Article ID e8439, 2009.
- K. D. Smith, “Iron metabolism at the host pathogen interface: lipocalin 2 and the pathogen-associated iroA gene cluster,” International Journal of Biochemistry and Cell Biology, vol. 39, no. 10, pp. 1776–1780, 2007.
- I. L. Lamont, A. F. Konings, and D. W. Reid, “Iron acquisition by Pseudomonas aeruginosa in the lungs of patients with cystic fibrosis,” BioMetals, vol. 22, no. 1, pp. 53–60, 2009.
- H. Saiga, J. Nishimura, H. Kuwata et al., “Lipocalin 2-dependent inhibition of mycobacterial growth in alveolar epithelium,” Journal of Immunology, vol. 181, no. 12, pp. 8521–8527, 2008.
- T. H. Flo, K. D. Smith, S. Sato et al., “Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron,” Nature, vol. 432, no. 7019, pp. 917–921, 2004.
- Y. R. Chan, J. S. Liu, D. A. Pociask et al., “Lipocalin 2 is required for pulmonary host defense against Klebsiella infection,” Journal of Immunology, vol. 182, no. 8, pp. 4947–4956, 2009.
- T. Berger, A. Togawa, G. S. Duncan et al., “Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 6, pp. 1834–1839, 2006.
- K. M. Schmidt-Ott, K. Mori, Y. L. Jau et al., “Dual action of neutrophil gelatinase-associated lipocalin,” Journal of the American Society of Nephrology, vol. 18, no. 2, pp. 407–413, 2007.
- I. Eichler, M. Nilsson, R. Rath, I. Enander, P. Venge, and D. Y. Koller, “Human neutrophil lipocalin, a highly specific marker for acute exacerbation in cystic fibrosis,” European Respiratory Journal, vol. 14, no. 5, pp. 1145–1149, 1999.
- S. I. Müller, M. Valdebenito, and K. Hantke, “Salmochelin, the long-overlooked catecholate siderophore of Salmonella,” BioMetals, vol. 22, no. 4, pp. 691–695, 2009.
- M. A. Fischbach, H. Lin, D. R. Liu, and C. T. Walsh, “How pathogenic bacteria evade mammalian sabotage in the battle for iron,” Nature Chemical Biology, vol. 2, no. 3, pp. 132–138, 2006.
- M. A. Fischbach, H. Lin, L. Zhou et al., “The pathogen-associated iroA gene cluster mediates bacterial evasion of lipocalin 2,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 44, pp. 16502–16507, 2006.
- H. Lin, M. A. Fischbach, D. R. Liu, and C. T. Walsh, “In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes,” Journal of the American Chemical Society, vol. 127, no. 31, pp. 11075–11084, 2005.
- R. J. Abergel, M. K. Wilson, J. E. L. Arceneaux et al., “Anthrax pathogen evades the mammalian immune system through stealth siderophore production,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 49, pp. 18499–18503, 2006.
- M. A. Bachman, J. E. Oyler, S. H. Burns et al., “Klebsiella pneumoniae yersiniabactin promotes respiratory tract infection through evasion of lipocalin 2,” Infection and Immunity, vol. 79, no. 8, pp. 3309–3316, 2011.
- N. Li, C. Zhang, B. Li et al., “Unique iron coordination in iron-chelating molecule vibriobactin helps Vibrio cholerae evade mammalian siderocalin-mediated immune response,” The Journal of Biological Chemistry, vol. 287, no. 12, pp. 8912–8919, 2012.
- D. H. Goetz, M. A. Holmes, N. Borregaard, M. E. Bluhm, K. N. Raymond, and R. K. Strong, “The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition,” Molecular Cell, vol. 10, no. 5, pp. 1033–1043, 2002.
- D. H. Goetz, S. T. Willie, R. S. Armen, T. Bratt, N. Borregaard, and R. K. Strong, “Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin,” Biochemistry, vol. 39, no. 8, pp. 1935–1941, 2000.
- H. M. Berman, J. Westbrook, Z. Feng et al., “The protein data bank,” Nucleic Acids Research, vol. 28, no. 1, pp. 235–242, 2000.
- K. Mori, H. T. Lee, D. Rapoport et al., “Endocytic delivery of lipocalin-siderophore-iron complex rescues the kidney from ischemia-reperfusion injury,” The Journal of Clinical Investigation, vol. 115, no. 3, pp. 610–621, 2005.
- L. Cai, J. Rubin, W. Han, P. Venge, and S. Xu, “The origin of multiple molecular forms in urine of HNL/NGAL,” Clinical Journal of the American Society of Nephrology, vol. 5, no. 12, pp. 2229–2235, 2010.
- L. Hu, W. Hittelman, T. Lu et al., “NGAL decreases E-cadherin-mediated cellcell adhesion and increases cell motility and invasion through Rac1 in colon carcinoma cells,” Laboratory Investigation, vol. 89, no. 5, pp. 531–548, 2009.
- O. Trott and A. J. Olson, “Software news and update AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading,” Journal of Computational Chemistry, vol. 31, no. 2, pp. 455–461, 2010.
- Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco, with support from the National Institutes of Health (National Center for Research Resources grant 2P41RR001081, National Institute of General Medical Sciences grant 9P41GM103311).
- E. F. Pettersen, T. D. Goddard, C. C. Huang et al., “UCSF Chimera—a visualization system for exploratory research and analysis,” Journal of Computational Chemistry, vol. 25, no. 13, pp. 1605–1612, 2004.
- M. F. Sanner, “Python: a programming language for software integration and development,” Journal of Molecular Graphics and Modelling, vol. 17, no. 1, pp. 57–61, 1999.
- M. A. Holmes, W. Paulsene, X. Jide, C. Ratledge, and R. K. Strong, “Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration,” Structure, vol. 13, no. 1, pp. 29–41, 2005.
- R. N. Jones, “Microbial etiologies of Hospital-acquired bacterial pneumonia and ventilator-associated bacterial pneumonia,” Clinical Infectious Diseases, vol. 51, supplement 1, pp. S81–S87, 2010.
- J. B. Goldberg, “Why is Pseudomonas aeruginosa a pathogen?” F1000 Biology Reports, vol. 2, no. 1, article 29, 2010.
- A. B. H. Khalifa, D. Moissenet, H. V. Thien, and M. Khedher, “Virulence factors in Pseudomonas aeruginosa: mechanisms and modes of regulation,” Annales de Biologie Clinique, vol. 69, no. 4, pp. 393–403, 2011.
- K. Poole and G. A. McKay, “Iron acquisition and its control in Pseudomonas aeruginosa: many roads lead to Rome,” Frontiers in Bioscience, vol. 8, pp. d661–d686, 2003.
- M. A. Fischbach, H. Lin, D. R. Liu, and C. T. Walsh, “In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 3, pp. 571–576, 2005.
- S. Xu and P. Venge, “Lipocalins as biochemical markers of disease,” Biochimica et Biophysica Acta, vol. 1482, no. 1-2, pp. 298–307, 2000.
- D. R. Flower, “The lipocalin protein family: a role in cell regulation,” FEBS Letters, vol. 354, no. 1, pp. 7–11, 1994.
- T. M. Hoette, M. C. Clifton, A. M. Zawadzka, M. A. Holmes, R. K. Strong, and K. N. Raymond, “Immune interference in Mycobacterium tuberculosis intracellular iron acquisition through siderocalin recognition of carboxymycobactins,” ACS Chemical Biology, vol. 6, no. 12, pp. 1327–1331, 2011.
- R. J. Abergel, M. C. Clifton, J. C. Pizarro et al., “The siderocalin/enterobactin interaction: a link between mammalian immunity and bacterial iron transport,” Journal of the American Chemical Society, vol. 130, no. 34, pp. 11524–11534, 2008.
- D. A. Dartt, “Tear lipocalin: structure and function,” Ocular Surface, vol. 9, no. 3, pp. 126–138, 2011.
- M. Fluckinger, H. Haas, P. Merschak, B. J. Glasgow, and B. Redl, “Human tear lipocalin exhibits antimicrobial activity by scavenging microbial siderophores,” Antimicrobial Agents and Chemotherapy, vol. 48, no. 9, pp. 3367–3372, 2004.
- C. Correnti, M. C. Clifton, R. J. Abergel et al., “Galline Ex-FABP is an antibacterial siderocalin and a lysophosphatidic acid sensor functioning through dual ligand specificities,” Structure, vol. 19, no. 12, pp. 1796–1806, 2011.
- E. Banin, M. L. Vasil, and E. P. Greenberg, “Iron and Pseudomonas aeruginosa biofilm formation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 31, pp. 11076–11081, 2005.
- Y. Wang, J. C. Wilks, T. Danhorn, I. Ramos, L. Croal, and D. K. Newman, “Phenazine-1-carboxylic acid promotes bacterial biofilm development via ferrous iron acquisition,” Journal of Bacteriology, vol. 193, no. 14, pp. 3606–3617, 2011.