This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dela Vega, A. L.
Right arrow Articles by Delcour, A. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dela Vega, A. L.
Right arrow Articles by Delcour, A. H.

 Previous Article  |  Next Article 

J. Bacteriol., Jul 1996, 3715-3721, Vol 178, No. 13
Copyright © 1996, American Society for Microbiology

Polyamines decrease Escherichia coli outer membrane permeability

AL Dela Vega and AH Delcour
Department of Biology, University of Houston, Texas 77204, USA.

The permeability of the outer membranes of gram-negative bacteria to hydrophilic compounds is mostly due to the presence of porin channels. We tested the effects of four polyamines (putrescine, cadaverine, spermidine, and spermine) on two processes known to depend on intact porin function: fluxes of beta-lactam antibiotics in live cells and chemotaxis. In both cases, inhibition was observed. Measurements of the rate of permeation of cephaloridine and of chemotaxis in swarm plates and capillary assays were used to determine the concentration dependence of this modulation. The effective concentration ranges depended on the nature of the polyamine and varied from submillimolar for spermine to tens of millimolar for cadaverine. Both OmpC and OmpF porins were inhibited, although the effects on OmpC appeared to be milder. These results are in agreement with our observations that polyamines inhibit porin-mediated ion fluxes in electrophysiological experiments, and they suggest that a low-affinity polyamine binding site might exist in these porins. These results reveal the potential use of porins as targets for blocking agents and suggest that polyamines may act as endogenous modulators of outer membrane permeability.


This article has been cited by other articles:

  • Terui, Y., Higashi, K., Tabei, Y., Tomitori, H., Yamamoto, K., Ishihama, A., Igarashi, K., Kashiwagi, K. (2009). Enhancement of the Synthesis of RpoE and StpA by Polyamines at the Level of Translation in Escherichia coli under Heat Shock Conditions. J. Bacteriol. 191: 5348-5357 [Abstract] [Full Text]  
  • Pagel, M., Simonet, V., Li, J., Lallemand, M., Lauman, B., Delcour, A. H. (2007). Phenotypic Characterization of Pore Mutants of the Vibrio cholerae Porin OmpU. J. Bacteriol. 189: 8593-8600 [Abstract] [Full Text]  
  • Kwon, D.-H., Lu, C.-D. (2007). Polyamine Effects on Antibiotic Susceptibility in Bacteria. Antimicrob. Agents Chemother. 51: 2070-2077 [Abstract] [Full Text]  
  • Pan, Y.-H., Liao, C.-C., Kuo, C.-C., Duan, K.-J., Liang, P.-H., Yuan, H. S., Hu, S.-T., Chak, K.-F. (2006). The Critical Roles of Polyamines in Regulating ColE7 Production and Restricting ColE7 Uptake of the Colicin-producing Escherichia coli. J. Biol. Chem. 281: 13083-13091 [Abstract] [Full Text]  
  • Kwon, D. H., Lu, C.-D. (2006). Polyamines Induce Resistance to Cationic Peptide, Aminoglycoside, and Quinolone Antibiotics in Pseudomonas aeruginosa PAO1.. Antimicrob. Agents Chemother. 50: 1615-1622 [Abstract] [Full Text]  
  • Kwon, D. H., Lu, C.-D. (2006). Polyamines Increase Antibiotic Susceptibility in Pseudomonas aeruginosa.. Antimicrob. Agents Chemother. 50: 1623-1627 [Abstract] [Full Text]  
  • Nikaido, H. (2003). Molecular Basis of Bacterial Outer Membrane Permeability Revisited. Microbiol. Mol. Biol. Rev. 67: 593-656 [Abstract] [Full Text]  
  • Samartzidou, H., Mehrazin, M., Xu, Z., Benedik, M. J., Delcour, A. H. (2003). Cadaverine Inhibition of Porin Plays a Role in Cell Survival at Acidic pH. J. Bacteriol. 185: 13-19 [Abstract] [Full Text]  
  • Wibbenmeyer, J. A., Provenzano, D., Landry, C. F., Klose, K. E., Delcour, A. H. (2002). Vibrio cholerae OmpU and OmpT Porins Are Differentially Affected by Bile. Infect. Immun. 70: 121-126 [Abstract] [Full Text]  
  • Leitão, A. L., Enguita, F. J., Luis De La Fuente, J., Liras, P., Martin, J. F. (1999). Inducing Effect of Diamines on Transcription of the Cephamycin C Genes from the lat and pcbAB Promoters in Nocardia lactamdurans. J. Bacteriol. 181: 2379-2384 [Abstract] [Full Text]  
  • Samartzidou, H., Delcour, A. H. (1999). Excretion of Endogenous Cadaverine Leads to a Decrease in Porin-Mediated Outer Membrane Permeability. J. Bacteriol. 181: 791-798 [Abstract] [Full Text]  
  • Pohlmeyer, K., Soll, J., Grimm, R., Hill, K., Wagner, R. (1998). A High-Conductance Solute Channel in the Chloroplastic Outer Envelope from Pea. Plant Cell 10: 1207-1216 [Abstract] [Full Text]  
  • Pohlmeyer, K., Soll, J., Steinkamp, T., Hinnah, S., Wagner, R. (1997). Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane. Proc. Natl. Acad. Sci. USA 94: 9504-9509 [Abstract] [Full Text]  
  • Iyer, R., Delcour, A. H. (1997). Complex Inhibition of OmpF and OmpC Bacterial Porins by Polyamines. J. Biol. Chem. 272: 18595-18601 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»