Lysine decarboxylase activity as a factor of fluoroquinolone resistance in Escherichia coli

Microbiology

Volumn 78, Issue 5, 2009, Pages 575-579

  Akhova, A V ^a   Tkachenko, A G ^a  

^a INSTITUTE OF ECOLOGY AND GENETICS OF MICROORGANISMS   (Russian Federation)

Author keywords

Antibiotic resistance; Cadaverine; Fluoroquinolones; LdcC; Lysine decarboxylase; Polyamines; rpoS

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 70350389387     PISSN: 00262617     EISSN: None     Source Type: Journal    
DOI: 10.1134/S0026261709050075     Document Type: Article

References (22)

1. Normark, B.H. and Normark, S., Evolution and Spread of Antibiotic Resistance, J. Intern. Med., 2002, vol. 252, no. 2, pp. 91-106.
2. Escribano, I., Rodríguez, J.C., Pertegás, V., Cebrian, L., and Royo, G., Relation between Induction of the mar Operon and Cyclohexane Tolerance and Reduction in Fluoroquinolone Susceptibility in Salmonella spp., J. Infect. Chemother, 2006, vol. 12, no. 4, pp. 177-180.
3. Depardieu, F., Podglajen, I., Leclercq, R., Collatz, E., and Courvalin, P., Modes and Modulations of Antibiotic Resistance Gene Expression, Clin. Microbiol. Rev., 2007, vol. 20, no. 1, pp. 79-114.
4. Dupont, M., James, C.E., Chevalier, J., and Pagés, J.M., An Early Response to Environmental Stress Involves Regulation of OmpX and OmpF, Two Enterobacterial Outer Membrane Pore-Forming Proteins, Antimicrob. Agents Chemother., 2007, vol. 51, no. 9, pp. 3190-3198.
5. Samartzidou, H. and Delcour, A.H., Excretion of Endogenous Cadaverine Leads to a Decrease in Porin-Mediated Outer Membrane Permeability, J. Bacteriol., 1999, vol. 181, no. 3, pp. 791-798.
6. Meng, S.Y. and Bennett, G.N., Regulation of the Escherichia coli cad Operon: Location of a Site Required for Acid Induction, J. Bacteriol., 1992, vol. 174, no. 8, pp. 2670-2678.
7. Yamamoto, Y., Miwa, Y., Miyoshi, K., Furuyama, J., and Ohmori, H., The Escherichia coli ldcC Gene Encodes Another Lysine Decarboxylase, Probably a Constitutive Enzyme, Genes. Genet. Syst, 1997, vol. 72, no. 3, pp. 167-172.
8. Tkachenko, A.G., Pozhidaeva, O.N., and Shumkov, M.S., Role of Polyamines in Formation of Multiple Antibiotic Resistance of Escherichia coli under Stress Conditions, Biokhimiya, 2006, vol. 71, no. 9, pp. 1287-1296 [Biochemistry (Moscow) (Engl. Transl.), vol. 71, no. 9, pp. 1042-1050].
9. Chen, G., Patten, C.L., and Schellhorn, H.E., Controlled Expression of an RpoS Antisense RNA Can Inhibit RpoS Function in Escherichia coli, Antimicrob. Agents Chemother., 2003, vol. 47, no. 11, pp. 3485-3493.
10. Lange, R. and Hengge-Aronis, R., The Cellular Concentration of the Sigma S Subunit of RNA Polymerase in Escherichia coli Is Controlled at the Levels of Transcription, Translation, and Protein Stability, Genes Dev., 1994, vol. 8, no. 13, pp. 1600-1612.
11. Ding, H. and Demple, B., Thiol-Mediated Disassembly and Reassembly of [2Fe-2S] Clusters in the Redox-Regulated Transcription Factor SoxR, Biochemistry, 1998, vol. 37, no. 49, pp. 17280-17286.
12. Miller, J.H., Experiments in Molecular Genetics, New York: Cold Spring Harbor, 1992.
13. Lemonnier, M. and Lane, D., Expression of the Second Lysine Decarboxylase Gene of Escherichia coli, Microbiology (UK), 1998, vol. 144, pp. 751-760.
14. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J., Protein Measurement with the Folin Phenol Reagent, J. Biol. Chem., 1951, vol. 193, no. 1, pp. 265-275.
15. Chudinov, A.A., Chudinova, L.A., and Korobov, V.P., Method for Determination of Low-Molecular Oligoamines in Biological Materials, Vopr. Med. Khim., 1984, vol. 30, no. 4, pp. 127-132.
16. Metodicheskie ukazaniya po opredeleniyu chuvstvitel'nosti mikroorganizmov k antibikterial'nym preparatam: Metodicheskie ukazaniya (Instructions for Determination of Microbial Sensitivity to Antibacterial Preparations), Moscow: Federal'nyi tsentr Gossanepidnadzora Minzdrava Rossii, 2004.
17. Kikuchi, Y., Kurahashi, O., Nagano, T., and Kamio, Y., RpoS-Dependent Expression of the Second Lysine Decarboxylase Gene in Escherichia coli, Boisci. Biotechnol. Biochem., 1998, vol. 62, no. 6, pp. 1267-1270.
18. Koski, P. and Vaara, M., Polyamines as Constituents of the Outer Membranes of Escherichia coli and Salmonella typhimurium, J. Bacteriol., 1991, vol. 173, no. 12, pp. 3695-3699.
19. Iyer, R. and Delcour, A.H., Complex Inhibition of OmpF and OmpC Bacterial Porins by Polyamines, J. Biol. Chem., 1997, vol. 272, pp. 18595-18601.
20. Tkachenko, A.G. and Chudinov, A.A., Changes in the Polyamine Pool in the Course of Transition from Anaerobic to Aerobic Conditions and Localization of the Relevant Synthetic Enzymes in Escherichia coli Cells, Mikrobiologiya, 1989, vol. 58, no. 6, pp. 885-891.
21. Neves, P., Berkane, E., Gameiro, P., Winterhalter, M., and deCastro, B., Interaction between Quinolones Antibiotics and Bacterial Outer Membrane Porin OmpF, Biophys. Chem., 2005, vol. 113, no. 2, pp. 123-128.
22. Chevalier, J., Mallea, M., and Pages, J.M., Comparative Aspects of the Diffusion of Norfloxacin, Cefepime and Spermine through the F Porin Channel of Enterobacter cloacae, Biochem. J., 2000, vol. 348, pp. 223-227.