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Gene Review

ECs3104  -  outer membrane porin protein C

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs3104

  • OmpC and PhoE porins of Escherichia coli were examined by the patch-clamp technique following reconstitution in liposomes, and were observed primarily in the open (conducting) state [1].
  • The hybrid gene products were normally expressed and they were characterized with respect to functions and properties in which the native OmpC and PhoE proteins differ, such as pore characteristics, the receptor activity for phages and the binding of specific antibodies [2].
  • Because RseP is shown to be no longer essential in a strain lacking OmpA and OmpC, we conclude that RseP, which is required for normal sigma(E) activation, prevents toxicity due to the presence of two specific outer membrane proteins that are down-regulated by RseX [3].
  • The Salmonella typhi ompS1 gene codes for an outer membrane protein of the OmpC/OmpF porin family [4].
  • Ileal lesions of 36.4% of patients with Crohn's disease (CD), an inflammatory bowel disease in humans, are colonized by pathogenic adherent-invasive Escherichia coli (AIEC), and high levels of antibodies directed against E. coli OmpC are present in 37-55% of CD patients [5].

High impact information on ECs3104

  • In addition, several PhoE mutants with amino acid substitutions and insertions in either the L3 or L4 loop of the monomer exhibited pressure sensitivity comparable with the wild-type OmpC porin [1].
  • Analysis of amino acid sequences reported for the major outer membrane proteins of Escherichia coli, including the porins (OmpF, OmpC, and PhoE), the phage lambda receptor (LamB), and another protein (OmpA), revealed several regions of local homology that is statistically significant [6].
  • RseX activity was shown to confer an Hfq-dependent coordinate OmpA and OmpC down-regulation [3].
  • Three linker mutants give rise to an OmpF(+) OmpC(-) phenotype, but the defects are not due to a shared molecular mechanism [7].
  • EnvZ, a histidine kinase/phosphatase in Escherichia coli, responds to the osmolarity changes in the medium by regulating the phosphorylation state of the transcription factor OmpR, which controls the expression levels of outer membrane porin proteins OmpF and OmpC [8].

Chemical compound and disease context of ECs3104

  • The histidine kinase/phosphatase EnvZ helps Escherichia coli adapt to osmotic shock by controlling the phosphorylation state of the transcription factor OmpR, which regulates the levels of the outer membrane porin proteins OmpF and OmpC [9].
  • The phage resistance seen in these mutants could be a result of both the presence of defective LPS and reduced OmpC levels [10].
  • OmpC, a major outer-membrane protein, is highly expressed when Salmonella typhi is grown in nutrient broth (NB) of either low (NB + 0% sucrose) or high (NB + 20% sucrose) osmolarity [11].
  • The antigenic determinants of Salmonella typhimurium OmpC were investigated by the analysis of cyanogen bromide (CNBr)-generated porin peptides with antiporin monoclonal antibodies (MAbs) [12].
  • Studies on Salmonella typhi and Salmonella typhimurium outer membrane proteins have shown that the relative position of OmpC porin in sodium dodecyl sulfate.polyacrylamide gel electrophoresis undergoes an important shift when the concentration of ammonium persulfate in the running gel is increased from 6 to 12 mM [13].

Biological context of ECs3104


Anatomical context of ECs3104

  • We therefore investigated the expression of OmpC and its role in the interaction of CD-associated adherent-invasive E. coli strain LF82 with intestinal epithelial cells [5].
  • Single OmpC porin channels have been reconstituted in planar bilayer membranes [19].
  • Evidence from this study supports a role for the OmpC protein in initial recognition by macrophages and distinguishes regions of this protein that potentially participate in host-cell recognition of bacteria by phagocytic cells [20].
  • The effects of a hydrophobic peptide segment inserted into the amino-terminal region of the mature domain of OmpC, an outer membrane protein, on its translocation across the cytoplasmic membrane was studied [21].
  • In contrast, the supernatants from the immunization with outer membrane preparation lacking S. typhi Ty2 OmpC induced a significantly reduced bactericidal capacity of U937 cells [22].

Associations of ECs3104 with chemical compounds

  • OmpF and OmpC, although highly homologous, have distinct sensitivities to modulation, especially by spermine [16].
  • By measuring the permeability of porin channels in intact cells suspended in solutions of widely different ionic strengths, it was shown that changing Donnan potential from 5 mV to approximately 100 mV had no effect on the permeability of either OmpF or OmpC porin channel toward a zwitterionic compound, cephaloridine [23].
  • The gene appears to encode a secretory precursor of OmpC protein consisting of a total of 367 amino acid residues with a signal peptide of 21 amino acid residues at its NH2-terminal end [24].
  • At low substrate concentration (0.7 microM), permeation of glycine betaine was entirely dependent on the OmpF and OmpC porins [25].
  • The possibility that heterologous nitrate reductases could be formed in vivo is discussed with reference to the existence of porin heterotrimers of the outer membrane proteins OmpC, OmpF and PhoE [26].

Analytical, diagnostic and therapeutic context of ECs3104

  • Western blot analyses of cell extracts with anti-TolA antibodies indicated that TolA forms high molecular weight complexes specifically with trimeric OmpF, OmpC, PhoE and LamB, but not with OmpA [27].
  • The three-dimensional structure of OmpC has been determined to 2.0 A resolution by X-ray crystallography [28].
  • Electron microscopy of unstained, frozen-hydrated OmpC reveals the trimeric pore structure with equal clarity [29].
  • Immunoprecipitation of labeled proteins showed no evidence of accumulation of uncleaved precursor forms of OmpA or maltose-binding protein following induction of OmpC overexpression [30].
  • Two oligonucleotides encoding the N-terminal portion of the 38-kDa OMP and C-terminal portion of OmpC were used to amplify the 38-kDa gene by PCR [31].


  1. Porins of Escherichia coli: unidirectional gating by pressure. Le Dain, A.C., Häse, C.C., Tommassen, J., Martinac, B. EMBO J. (1996) [Pubmed]
  2. Localization of functional domains in E. coli K-12 outer membrane porins. Tommassen, J., van der Ley, P., van Zeijl, M., Agterberg, M. EMBO J. (1985) [Pubmed]
  3. Down-regulation of Porins by a Small RNA Bypasses the Essentiality of the Regulated Intramembrane Proteolysis Protease RseP in Escherichia coli. Douchin, V., Bohn, C., Bouloc, P. J. Biol. Chem. (2006) [Pubmed]
  4. Negative and positive regulation of the non-osmoregulated ompS1 porin gene in Salmonella typhi: a novel regulatory mechanism that involves OmpR. Oropeza, R., Sampieri, C.L., Puente, J.L., Calva, E. Mol. Microbiol. (1999) [Pubmed]
  5. OmpC and the sigma(E) regulatory pathway are involved in adhesion and invasion of the Crohn's disease-associated Escherichia coli strain LF82. Rolhion, N., Carvalho, F.A., Darfeuille-Michaud, A. Mol. Microbiol. (2007) [Pubmed]
  6. Amino acid sequence homology among the major outer membrane proteins of Escherichia coli. Nikaido, H., Wu, H.C. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  7. The linker region plays an important role in the interdomain communication of the response regulator OmpR. Mattison, K., Oropeza, R., Kenney, L.J. J. Biol. Chem. (2002) [Pubmed]
  8. EnvZ-OmpR interaction and osmoregulation in Escherichia coli. Cai, S.J., Inouye, M. J. Biol. Chem. (2002) [Pubmed]
  9. The critical role of the conserved Thr247 residue in the functioning of the osmosensor EnvZ, a histidine Kinase/Phosphatase, in Escherichia coli. Dutta, R., Yoshida, T., Inouye, M. J. Biol. Chem. (2000) [Pubmed]
  10. A genetic approach for analysing surface-exposed regions of the OmpC protein of Escherichia coli K-12. Vakharia, H., Misra, R. Mol. Microbiol. (1996) [Pubmed]
  11. Expression of Salmonella typhi and Escherichia coli OmpC is influenced differently by medium osmolarity; dependence on Escherichia coli OmpR. Puente, J.L., Verdugo-Rodríguez, A., Calva, E. Mol. Microbiol. (1991) [Pubmed]
  12. Antigenic determinants of the OmpC porin from Salmonella typhimurium. Singh, S.P., Singh, S.R., Williams, Y.U., Jones, L., Abdullah, T. Infect. Immun. (1995) [Pubmed]
  13. Alteration in the electrophoretic mobility of OmpC due to variations in the ammonium persulfate concentration in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Lobos, S.R., Mora, G.C. Electrophoresis (1991) [Pubmed]
  14. Localization and membrane topology of EnvZ, a protein involved in osmoregulation of OmpF and OmpC in Escherichia coli. Forst, S., Comeau, D., Norioka, S., Inouye, M. J. Biol. Chem. (1987) [Pubmed]
  15. Properties of Escherichia coli mutants lacking membrane-derived oligosaccharides. Fiedler, W., Rotering, H. J. Biol. Chem. (1988) [Pubmed]
  16. Complex inhibition of OmpF and OmpC bacterial porins by polyamines. Iyer, R., Delcour, A.H. J. Biol. Chem. (1997) [Pubmed]
  17. Cloning and identification of a two-component signal-transducing regulatory system from Bacteroides fragilis. Rasmussen, B.A., Kovacs, E. Mol. Microbiol. (1993) [Pubmed]
  18. Hc1-mediated effects on DNA structure: a potential regulator of chlamydial development. Barry, C.E., Brickman, T.J., Hackstadt, T. Mol. Microbiol. (1993) [Pubmed]
  19. Altered voltage sensitivity of mutant OmpC porin channels. Bishop, N.D., Lea, E.J., Mobasheri, H., Spiro, S. FEBS Lett. (1996) [Pubmed]
  20. The porin OmpC of Salmonella typhimurium mediates adherence to macrophages. Negm, R.S., Pistole, T.G. Can. J. Microbiol. (1999) [Pubmed]
  21. Insertion of a signal peptide-derived hydrophobic segment into the mature domain of OmpC, an outer membrane protein, does not interfere with the export of the following polypeptide chain across the cytoplasmic membrane of E. coli. Shinkai, A., Yamada, H., Mizuno, T., Mizushima, S. J. Biochem. (1989) [Pubmed]
  22. Salmonella typhi Ty2 OmpC porin induces bactericidal activity on U937 monocytes. Blanco, L.P., Toro, C.S., Romero, J.M., Santiviago, C.A., Mora, G.C. Microbiol. Immunol. (1997) [Pubmed]
  23. Porin channels in intact cells of Escherichia coli are not affected by Donnan potentials across the outer membrane. Sen, K., Hellman, J., Nikaido, H. J. Biol. Chem. (1988) [Pubmed]
  24. A comparative study on the genes for three porins of the Escherichia coli outer membrane. DNA sequence of the osmoregulated ompC gene. Mizuno, T., Chou, M.Y., Inouye, M. J. Biol. Chem. (1983) [Pubmed]
  25. Cloned structural genes for the osmotically regulated binding-protein-dependent glycine betaine transport system (ProU) of Escherichia coli K-12. Faatz, E., Middendorf, A., Bremer, E. Mol. Microbiol. (1988) [Pubmed]
  26. Formation of active heterologous nitrate reductases between nitrate reductases A and Z of Escherichia coli. Blasco, F., Nunzi, F., Pommier, J., Brasseur, R., Chippaux, M., Giordano, G. Mol. Microbiol. (1992) [Pubmed]
  27. TolA central domain interacts with Escherichia coli porins. Derouiche, R., Gavioli, M., Bénédetti, H., Prilipov, A., Lazdunski, C., Lloubès, R. EMBO J. (1996) [Pubmed]
  28. Crystal Structure of Osmoporin OmpC from E. coli at 2.0 A. Baslé, A., Rummel, G., Storici, P., Rosenbusch, J.P., Schirmer, T. J. Mol. Biol. (2006) [Pubmed]
  29. Projected structure of the pore-forming OmpC protein from Escherichia coli outer membrane. Chang, C.F., Mizushima, S., Glaeser, R.M. Biophys. J. (1985) [Pubmed]
  30. Translational control of exported proteins that results from OmpC porin overexpression. Click, E.M., McDonald, G.A., Schnaitman, C.A. J. Bacteriol. (1988) [Pubmed]
  31. A major outer membrane protein of Rahnella aquatilis functions as a porin and root adhesin. Achouak, W., Pages, J.M., De Mot, R., Molle, G., Heulin, T. J. Bacteriol. (1998) [Pubmed]
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