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BioMed Research International
Volume 2013 (2013), Article ID 192589, 10 pages
Characterization and Complete Sequence of Lactonase Enzyme from Bacillus weihenstephanensis Isolate P65 with Potential Activity against Acyl Homoserine Lactone Signal Molecules
Department of Microbiology and Immunology, Faculty of Pharmacy, Ain Shams University, Organization of African Unity Street,
P.O. Box 11566, Abbassia, Cairo, Egypt
Received 17 April 2013; Revised 18 June 2013; Accepted 18 June 2013
Academic Editor: Anastasia Kotanidou
Copyright © 2013 Masarra Mohammed Sakr 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.
- K. H. Nealson and J. W. Hastings, “Bacterial bioluminescence: its control and ecological significance,” Microbiological Reviews, vol. 43, no. 4, pp. 496–518, 1979.
- C. Fuqua, M. R. Parsek, and E. P. Greenberg, “Regulation of gene expression by cell-to-cell communication: acyl-homoserine lactone quorum sensing,” Annual Review of Genetics, vol. 35, pp. 439–468, 2001.
- M. B. Miller and B. L. Bassler, “Quorum sensing in bacteria,” Annual Review of Microbiology, vol. 55, pp. 165–199, 2001.
- W. C. Fuqua, S. C. Winans, and E. P. Greenberg, “Quorum sensing in bacteria: the LuxR-LuxI family of cell density-responsive transcriptional regulators,” Journal of Bacteriology, vol. 176, no. 2, pp. 269–275, 1994.
- T. R. De Kievit and B. H. Iglewski, “Bacterial quorum sensing in pathogenic relationships,” Infection and Immunity, vol. 68, no. 9, pp. 4839–4849, 2000.
- W. R. J. D. Galloway, J. T. Hodgkinson, S. D. Bowden, M. Welch, and D. R. Spring, “Quorum sensing in gram-negative bacteria: small-molecule modulation of AHL and AI-2 quorum sensing pathways,” Chemical Reviews, vol. 111, no. 1, pp. 28–67, 2011.
- J. M. Henke and B. L. Bassler, “Bacterial social engagements,” Trends in Cell Biology, vol. 14, no. 11, pp. 648–656, 2004.
- M. Juhas, L. Eberl, and B. Tümmler, “Quorum sensing: the power of cooperation in the world of Pseudomonas,” Environmental Microbiology, vol. 7, no. 4, pp. 459–471, 2005.
- S. P. Diggle, S. A. West, A. Gardner, and A. S. Griffin, “Communication in bacteria,” in Sociobiology of Communication: An Interdisciplinary Perspective, P. d'Ettorre and D. P. Hughes, Eds., pp. 11–31, Oxford University Press, 2008.
- M. Schuster and E. P. Greenberg, “A network of networks: quorum-sensing gene regulation in Pseudomonas aeruginosa,” International Journal of Medical Microbiology, vol. 296, no. 2-3, pp. 73–81, 2006.
- A. U. Viretta and M. Fussenegger, “Modeling the quorum sensing regulatory network of human-pathogenic Pseudomonas aeruginosa,” Biotechnology Progress, vol. 20, no. 3, pp. 670–678, 2004.
- C. van Delden and B. H. Iglewski, “Cell-to-cell signaling and Pseudomonas aeruginosa infections,” Emerging Infectious Diseases, vol. 4, no. 4, pp. 551–560, 1998.
- K. Poole, “Efflux-mediated multiresistance in Gram-negative bacteria,” Clinical Microbiology and Infection, vol. 10, no. 1, pp. 12–26, 2004.
- M. Hentzer and M. Givskov, “Pharmacological inhibition of quorum sensing for the treatment of chronic bacterial infections,” Journal of Clinical Investigation, vol. 112, no. 9, pp. 1300–1307, 2003.
- T. B. Rasmussen and M. Givskov, “Quorum-sensing inhibitors as anti-pathogenic drugs,” International Journal of Medical Microbiology, vol. 296, no. 2-3, pp. 149–161, 2006.
- I. A. Khmel and A. Z. Metlitskaya, “Quorum sensing regulation of gene expression: a promising target for drugs against bacterial pathogenicity,” Molecular Biology, vol. 40, no. 2, pp. 169–182, 2006.
- Y.-H. Dong, J.-L. Xu, X.-Z. Li, and L.-H. Zhang, “AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 7, pp. 3526–3531, 2000.
- Y.-H. Dong, A. R. Gusti, Q. Zhang, J.-L. Xu, and L.-H. Zhang, “Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species,” Applied and Environmental Microbiology, vol. 68, no. 4, pp. 1754–1759, 2002.
- S. J. Lee, S.-Y. Park, J.-J. Lee, D.-Y. Yum, B.-T. Koo, and J.-K. Lee, “Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis,” Applied and Environmental Microbiology, vol. 68, no. 8, pp. 3919–3924, 2002.
- M. H. Kim, W.-C. Choi, H. O. Kang et al., “The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 49, pp. 17606–17611, 2005.
- R. Czajkowski and S. Jafra, “Quenching of acyl-homoserine lactone-dependent quorum sensing by enzymatic disruption of signal molecules,” Acta Biochimica Polonica, vol. 56, no. 1, pp. 1–16, 2009.
- P. W. Thomas, E. M. Stone, A. L. Costello, D. L. Tierney, and W. Fast, “The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein,” Biochemistry, vol. 44, no. 20, pp. 7559–7569, 2005.
- K. H. McClean, M. K. Winson, L. Fish et al., “Quorum sensing and chromobacterium violaceum: exploitation of violacein production and inhibition for the detection of N-acylhomoserine lactones,” Microbiology, vol. 143, no. 12, pp. 3703–3711, 1997.
- L. Ravn, A. B. Christensen, S. Molin, M. Givskov, and L. Gram, “Methods for detecting acylated homoserine lactones produced by Gram-negative bacteria and their application in studies of AHL-production kinetics,” Journal of Microbiological Methods, vol. 44, no. 3, pp. 239–251, 2001.
- M. Boyer, R. Bally, S. Perrotto, C. Chaintreuil, and F. Wisniewski-Dyé, “A quorum-quenching approach to identify quorum-sensing-regulated functions in Azospirillum lipoferum,” Research in Microbiology, vol. 159, no. 9-10, pp. 699–708, 2008.
- O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, “Protein measurement with the folin phenol reagent,” The Journal of Biological Chemistry, vol. 193, no. 1, pp. 265–275, 1951.
- Y. Cao, S. He, Z. Zhou et al., “Orally administered thermostable N-acyl homoserine lactonase from Bacillus sp. strain AI96 attenuates Aeromonas hydrophila infection in zebrafish,” Applied and Environmental Microbiology, vol. 78, no. 6, pp. 1899–1908, 2012.
- A. Pospiech and B. Neumann, “A versatile quick-prep of genomic DNA from gram-positive bacteria,” Trends in Genetics, vol. 11, no. 6, pp. 217–218, 1995.
- J. Sambrook and D. W. Russell, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA, 3rd edition, 2001.
- R. Staden, “The staden sequence analysis package,” Applied Biochemistry and Biotechnology, vol. 5, no. 3, pp. 233–241, 1996.
- J. Ishikawa and K. Hotta, “FramePlot: a new implementation of the Frame analysis for predicting protein-coding regions in bacterial DNA with a high G+C content,” FEMS Microbiology Letters, vol. 174, no. 2, pp. 251–253, 1999.
- K. Arnold, L. Bordoli, J. Kopp, and T. Schwede, “The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling,” Bioinformatics, vol. 22, no. 2, pp. 195–201, 2006.
- N. Guex and M. C. Peitsch, “SWISS-MODEL and the Swiss-pdb viewer: an environment for comparative protein modeling,” Electrophoresis, vol. 18, no. 15, pp. 2714–2723, 1997.
- T. Schwede, J. Kopp, N. Guex, and M. C. Peitsch, “SWISS-MODEL: an automated protein homology-modeling server,” Nucleic Acids Research, vol. 31, no. 13, pp. 3381–3385, 2003.
- P. Benkert, M. Biasini, and T. Schwede, “Toward the estimation of the absolute quality of individual protein structure models,” Bioinformatics, vol. 27, no. 3, pp. 343–350, 2011.
- R. Chen, Z. Zhou, Y. Cao, Y. Bai, and B. Yao, “High yield expression of an AHL-lactonase from Bacillus sp. B546 in Pichia pastoris and its application to reduce Aeromonas hydrophila mortality in aquaculture,” Microbial Cell Factories, vol. 9, article 39, pp. 1–10, 2010.
- L.-H. Wang, L.-X. Weng, Y.-H. Dong, and L.-H. Zhang, “Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase),” Journal of Biological Chemistry, vol. 279, no. 14, pp. 13645–13651, 2004.
- J. Hiblot, G. Gotthard, E. Chabriere, and M. Elias, “Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus,” Plos One, vol. 7, no. 10, article e47028, 2012.
- J. Momb, P. W. Thomas, R. M. Breece, D. L. Tierney, and W. Fast, “The quorum-quenching metallo-γ-lactonase from Bacillus thuringiensis exhibits a leaving group thio effect,” Biochemistry, vol. 45, no. 44, pp. 13385–13393, 2006.
- M. Elias, J. Dupuy, L. Merone et al., “Structural basis for natural lactonase and promiscuous phosphotriesterase activities,” Journal of Molecular Biology, vol. 379, no. 5, pp. 1017–1028, 2008.