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2014 | 61 | 2 | 369-373
Article title

High-grade mutant OmpF induces decreased bacterial survival rate

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OmpF plays very important roles in the influx of antibiotics and bacterial survival in the presence of antibiotics. However, high-grade mutant OmpF and its function in decreasing bacterial survival rate have not been reported to date. In the present study, we cloned a high-grade mutant OmpF (mOmpF) and sequence analysis suggested that over 45 percent of the DNA sequence was significantly mutated, leading to dramatic changes in over 55 percent of the amino acid sequence. mOmpF protein was successfully expressed. When grown in the presence of antibiotic, the bacterial survival rate decreased and the antibiotic inhibition zone became larger with the increase of the mOmpF. It was concluded that concentration of high-grade mutant mOmpF dramatically influenced the bacterial survival rate. The study presented here may provide insights into better understanding of the relationships between structure and function of OmpF.
Physical description
  • Bekhit A, Fukamachi T, Saito H, Kobayashi H (2011) The role of OmpC and OmpF in acidic resistance in Escherichia coli. Biol Pharm Bull 34: 330-334.
  • Bredin J, Simonet V, Iyer R, Delcour AH, Pages JM (2003) Colicins, spermine and cephalosporins: a competitive interaction with the OmpF eyelet. Biochem J 376: 245-252.
  • Chevalier J, Pages JM, Mallea M (1999) In vivo modification of porin activity conferring antibiotic resistance to Enterobacter aerogenes. Biochem Biophys Res Commun 266: 248-251.
  • Cohen SP, McMurry LM, Hooper DC, Wolfson JS, Levy SB (1989) Cross-resistance to fluoroquinolones in multiple-antibiotic-resistant (Mar) Escherichia coli selected by tetracycline or chloramphenicol: decreased drug accumulation associated with membrane changes in addition to OmpF reduction. Antimicrob Agents Chemother 33: 1318-1325.
  • Cowan SW, Garavito RM, Jansonius JN, Jenkins JA, Karlsson R, Konig N, Pai EF, Pauptit RA, Rizkallah PJ, Rosenbusch JP, Rummel G, Schirmer T (1995) The structure of OmpF porin in a tetragonal crystal form. Structure 3: 1041-1050.
  • Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit RA, Jansonius JN, Rosenbusch JP (1992) Crystal structures explain functional properties of two E. coli porins. Nature 358: 727-733.
  • Davin-Regli A, Bolla JM, James CE, Lavigne JP, Chevalier J, Garnotel E, Molitor A, Pagès JM (2008) Membrane permeability and regulation of drug 'influx and efflux' in enterobacterial pathogens. Curr Drug Targets 9: 750-759.
  • Dupont M, James CE, Chevalier J, Pages JM (2007) An early response to environmental stress involves regulation of OmpX and OmpF, two enterobacterial outer membrane pore-forming proteins. Antimicrob Agents Chemother 51: 3190-3198.
  • Fernandes F, Neves P, Gameiro P, Loura LM, Prieto M (2007) Ciprofloxacin interactions with bacterial protein OmpF: modelling of FRET from a multi-tryptophan protein trimer. Biochim Biophys Acta 1768: 2822-2830.
  • Ho MY, Chiou ML, Chang RC, Chen YH, Cheng CC (2010) Outer membrane protein OmpF involved in the transportation of polypyridyl ruthenium complexes into Escherichia coli. J Inorg Biochem 104: 614-617.
  • Jaffe A, Chabbert YA, Semonin O (1982) Role of porin proteins OmpF and OmpC in the permeation of beta-lactams. Antimicrob Agents Chemother 22: 942-948.
  • James CE, Mahendran KR, Molitor A, Bolla JM, Bessonov AN, Winterhalter M, Pagès JM (2009) How beta-lactam antibiotics enter bacteria: a dialogue with the porins. PLoS One 4: e5453.
  • Kefala G, Ahn C, Krupa M, Esquivies L, Maslennikov I, Kwiatkowski W, Choe S. (2010) Structures of the OmpF porin crystallized in the presence of foscholine-12. Protein Sci 19: 1117-1125.
  • Kishii R, Takei M (2009) Relationship between the expression of ompF and quinolone resistance in Eshcherichia coli. J Infect Chemother 15: 361-366.
  • Koebnik R, Locher KP, Van Gelder P (2000) Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol Microbiol 37: 239-253.
  • Lou KL, Saint N, Prilipov A, Rummel G, Benson SA, Rosenbusch JP, Schirmer T (1996) Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis. J Biol Chem 271: 20669-20675.
  • Masi M, Pages JM (2013) Structure, function and regulation of outer membrane proteins involved in drug transport in Enterobactericeae: the OmpF/C-TolC Case. Open Microbiol J 7: 22-33.
  • Nikaido H (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67: 593-656.
  • Pages JM, James CE, Winterhalter M (2008) The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria. Nat Rev Microbiol 6: 893-903.
  • Saint N, Lou KL, Widmer C, Luckey M, Schirmer T, Rosenbusch JP (1996) Structural and functional characterization of OmpF porin mutants selected for larger pore size. II. Functional characterization. J Biol Chem 271: 20676-20680.
  • Schulz GE (2002) The structure of bacterial outer membrane proteins. Biochim Biophys Acta 1565: 308-317.
  • Simonet V, Mallea M, Pages JM (2000) Substitutions in the eyelet region disrupt cefepime diffusion through the Escherichia coli OmpF channel. Antimicrob Agents Chemother 44: 311-315.
  • Yigit H, Anderson GJ, Biddle JW, Steward CD, Rasheed JK, Valera LL, McGowan JE Jr, Tenover FC (2002) Carbapenem resistance in a clinical isolate of Enterobacter aerogenes is associated with decreased expression of OmpF and OmpC porin analogs. Antimicrob Agents Chemother 46: 3817-3822.
  • Zhao Z, Nie X, Li Z, Zhang Z, Ding J, Xie W (2013) Amino terminus mutant OmpA from an isolated antibiotic resistant Escherichia coli still possess resistance to environmental stresses Advances in Biological Chemistry 3: 108-113.
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