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Gene Review

D786_p195  -  porin

Pseudomonas resinovorans

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Disease relevance of ORF184

  • Pseudomonas aeruginosa porin OprF: properties of the channel [1].
  • Earlier studies have shown that the major porin species in Pseudomonas aeruginosa outer membrane is protein F (OprF), which produces channels wider than those produced by Escherichia coli porins [2].
  • The susceptibility of beta-lactamase-producing strains and known porin mutants of the Enterobacteriaceae suggests that CGP 31608 is resistant to many important beta-lactamases (including the mutationally derepressed chromosomal enzymes) and is not excluded from the bacterial cell in strains expressing these known porin mutations [3].
  • By using purified preparations of Salmonella typhimurium and Pseudomonas aeruginosa porins, in the presence of polymyxin B, it was possible to induce concentration-dependent loss of calcium from cultured murine calvaria at porin concentrations in the range of 1 to 10 nM [4].
  • In contrast, porin-induced bone resorption could be inhibited by relatively high concentrations of the natural inhibitor of interleukin-1 (IL-1 receptor antagonist) [4].

High impact information on ORF184


Chemical compound and disease context of ORF184


Biological context of ORF184


Anatomical context of ORF184

  • Similar channel sizes were observed for porin protein F purified by the same method from P. aeruginosa outer membranes [20].

Associations of ORF184 with chemical compounds

  • These results suggested that in Mueller-Hinton medium the uptake of BMY 45047 through the non-D2 pathway is more rapid than that of meropenem through the D2 porin [16].
  • No aminoglycoside-modifying enzymes were observed, and outer membrane compositional analyses of the resistant variants revealed porin protein and lipopolysaccharide profiles similar to those of the aminoglycoside-susceptible parental strain (PA-96) [21].
  • Salicylate had no apparent effect, however, on expression of a 40-kDa porin protein in P. mirabilis [15].
  • This suggests that OprH is not a porin but, instead, may cause increased uptake of quinolones and chloramphenicol via a non-porin pathway [22].
  • Conversely, binding of [14C]imipenem in a porin D2-positive strain was reduced by sparfloxacin but not by the nonamphoteric quinolone nalidixic acid [23].

Analytical, diagnostic and therapeutic context of ORF184


  1. Pseudomonas aeruginosa porin OprF: properties of the channel. Nestorovich, E.M., Sugawara, E., Nikaido, H., Bezrukov, S.M. J. Biol. Chem. (2006) [Pubmed]
  2. Identification and characterization of porins in Pseudomonas aeruginosa. Nikaido, H., Nikaido, K., Harayama, S. J. Biol. Chem. (1991) [Pubmed]
  3. In vitro activity of CGP 31608, a new penem. Wise, R., Andrews, J.M., Piddock, L.J. Antimicrob. Agents Chemother. (1987) [Pubmed]
  4. Bacterial porins stimulate bone resorption. Meghji, S., Henderson, B., Nair, S.P., Tufano, M.A. Infect. Immun. (1997) [Pubmed]
  5. CzcR-CzcS, a two-component system involved in heavy metal and carbapenem resistance in Pseudomonas aeruginosa. Perron, K., Caille, O., Rossier, C., Van Delden, C., Dumas, J.L., Köhler, T. J. Biol. Chem. (2004) [Pubmed]
  6. The role of specific lysine residues in the passage of anions through the Pseudomonas aeruginosa porin OprP. Sukhan, A., Hancock, R.E. J. Biol. Chem. (1996) [Pubmed]
  7. Cloning and nucleotide sequence of anaerobically induced porin protein E1 (OprE) of Pseudomonas aeruginosa PAO1. Yamano, Y., Nishikawa, T., Komatsu, Y. Mol. Microbiol. (1993) [Pubmed]
  8. Sequence and relatedness in other bacteria of the Pseudomonas aeruginosa oprP gene coding for the phosphate-specific porin P. Siehnel, R., Martin, N.L., Hancock, R.E. Mol. Microbiol. (1990) [Pubmed]
  9. C-terminal region of Pseudomonas aeruginosa outer membrane porin OprD modulates susceptibility to meropenem. Epp, S.F., Köhler, T., Plésiat, P., Michéa-Hamzehpour, M., Frey, J., Pechère, J.C. Antimicrob. Agents Chemother. (2001) [Pubmed]
  10. Interplay of impermeability and chromosomal beta-lactamase activity in imipenem-resistant Pseudomonas aeruginosa. Livermore, D.M. Antimicrob. Agents Chemother. (1992) [Pubmed]
  11. Distribution of porin and lipopolysaccharide antigens on a Pseudomonas aeruginosa permeability mutant. Godfrey, A.J., Shahrabadi, M.S., Bryan, L.E. Antimicrob. Agents Chemother. (1986) [Pubmed]
  12. Negative regulation of the Pseudomonas aeruginosa outer membrane porin OprD selective for imipenem and basic amino acids. Ochs, M.M., McCusker, M.P., Bains, M., Hancock, R.E. Antimicrob. Agents Chemother. (1999) [Pubmed]
  13. Outer membrane permeability and beta-lactamase stability of dipolar ionic cephalosporins containing methoxyimino substituents. Nikaido, H., Liu, W., Rosenberg, E.Y. Antimicrob. Agents Chemother. (1990) [Pubmed]
  14. Outer membrane protein F preparation of Pseudomonas aeruginosa as a vaccine against chronic pulmonary infection with heterologous immunotype strains in a rat model. Gilleland, H.E., Gilleland, L.B., Matthews-Greer, J.M. Infect. Immun. (1988) [Pubmed]
  15. Effect of salicylate on expression of flagella by Escherichia coli and Proteus, Providencia, and Pseudomonas spp. Kunin, C.M., Hua, T.H., Bakaletz, L.O. Infect. Immun. (1995) [Pubmed]
  16. Structure-activity relationships of carbapenems that determine their dependence on porin protein D2 for activity against Pseudomonas aeruginosa. Fung-Tomc, J.C., Huczko, E., Banville, J., Ménard, M., Kolek, B., Gradelski, E., Kessler, R.E., Bonner, D.P. Antimicrob. Agents Chemother. (1995) [Pubmed]
  17. Colonial dissociation and susceptibility to phagocytosis of Pseudomonas aeruginosa grown in a chamber implant model in mice. Kelly, N.M., Battershill, J.L., Kuo, S., Arbuthnott, J.P., Hancock, R.E. Infect. Immun. (1987) [Pubmed]
  18. Mechanism of enhanced antipseudomonal activity of BO-2727, a new injectable 1-beta-methyl carbapenem. Hazumi, N., Fuse, A., Matsuda, K., Hashizume, T., Sanada, M. Antimicrob. Agents Chemother. (1995) [Pubmed]
  19. Insertion mutagenesis of the Pseudomonas aeruginosa phosphate-specific porin OprP. Sukhan, A., Hancock, R.E. J. Bacteriol. (1995) [Pubmed]
  20. Expression in Escherichia coli and function of Pseudomonas aeruginosa outer membrane porin protein F. Woodruff, W.A., Parr, T.R., Hancock, R.E., Hanne, L.F., Nicas, T.I., Iglewski, B.H. J. Bacteriol. (1986) [Pubmed]
  21. Mechanisms of aminoglycoside resistance in variants of Pseudomonas aeruginosa isolated during treatment of experimental endocarditis in rabbits. Parr, T.R., Bayer, A.S. J. Infect. Dis. (1988) [Pubmed]
  22. Fluoroquinolone supersusceptibility mediated by outer membrane protein OprH overexpression in Pseudomonas aeruginosa: evidence for involvement of a nonporin pathway. Young, M., Hancock, R.E. Antimicrob. Agents Chemother. (1992) [Pubmed]
  23. Role of protein D2 and lipopolysaccharide in diffusion of quinolones through the outer membrane of Pseudomonas aeruginosa. Michéa-Hamzehpour, M., Furet, Y.X., Pechère, J.C. Antimicrob. Agents Chemother. (1991) [Pubmed]
  24. Membrane topology and site-specific mutagenesis of Pseudomonas aeruginosa porin OprD. Huang, H., Jeanteur, D., Pattus, F., Hancock, R.E. Mol. Microbiol. (1995) [Pubmed]
  25. Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF. Rawling, E.G., Martin, N.L., Hancock, R.E. Infect. Immun. (1995) [Pubmed]
  26. Biophysical characterization of OprB, a glucose-inducible porin of Pseudomonas aeruginosa. Wylie, J.L., Bernegger-Egli, C., O'Neil, J.D., Worobec, E.A. J. Bioenerg. Biomembr. (1993) [Pubmed]
  27. Lipopolysaccharide-free Escherichia coli OmpF and Pseudomonas aeruginosa protein P porins are functionally active in lipid bilayer membranes. Parr, T.R., Poole, K., Crockford, G.W., Hancock, R.E. J. Bacteriol. (1986) [Pubmed]
  28. Role of porins in the antibiotic susceptibility of Pseudomonas aeruginosa: construction of mutants with deletions in the multiple porin genes. Yoneyama, H., Yamano, Y., Nakae, T. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
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