Substitutions in the eyelet region disrupt cefepime diffusion through the Escherichia coli OmpF channel

Antimicrobial Agents and Chemotherapy

Volumn 44, Issue 2, 2000, Pages 311-315

  Simonet, Valérie ^a   Malléa, Monique ^a   Pagès, Jean Marie ^a,b  

^a AIX MARSEILLE UNIVERSITY   (France)

^b INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAM ANTIBIOTIC; CEFEPIME; CEPHALOSPORIN DERIVATIVE; COLICIN; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN F; PORIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANTIBIOTIC SENSITIVITY; ARTICLE; CHANNEL GATING; CONTROLLED STUDY; DRUG DIFFUSION; ESCHERICHIA COLI; EXPERIMENTAL MODEL; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; REACTION ANALYSIS; SURFACE CHARGE; TRANSPORT KINETICS;

ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; CEPHALOSPORINS; COLICINS; ESCHERICHIA COLI; MICROBIAL SENSITIVITY TESTS; MODELS, MOLECULAR; MUTAGENESIS; PORINS; PROTEIN FOLDING;

EID: 0033978873     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.44.2.311-315.2000     Document Type: Article

References (37)

1. Bellido, F., J. C. Pechère, and R. E. W. Hancock. 1991. Reevaluation of the factors involved in the efficacy of new β-lactams against Enterobacter aerogenes. Antimicrob. Agents Chemother. 35:73-78.
2. Benson, S. A., J. L. L. Occi, and B. A. Sampson. 1988. Mutations that alter the pore function of the OmpF porin of Escherichia coli K-12. J. Mol. Biol. 203:961-970.
3. Bernstein, F., T. F. Koetzle, G. Williams, E. F. Meyer, M. D. Brice, J. R. Rodgers, O. Kennard, T. Shimanouchi, and M. Tasumi. 1977. The protein data hank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112:535-542.
4. Bouveret, E., A. Rigal, C. Lazdunski, and H. Benedetti. 1998. Distinct regions of the colicin A translocation domain are involved in the interaction with ToI A and Tol B proteins upon import into Escherichia coli. Mol. Microbiol. 27:143-157.
5. Charrel, R. N., J.-M. Pages, P. De Micco, and M. Malléa. 1996. Prevalence of outer membrane porin alteration in β-lactam-antibiotic-resistant Enterobacter aerogenes. Antimicrob. Agents Chemother. 40:2854-2858.
6. Cowan, S. W., T. Schirmer, G. Rummel, M. Steiert, R. Ghosh, R. A. Pauptit, J. A. Jansonius, and J. P. Rosenbusch. 1992. Crystal structures explain functional properties of two E. coli porins. Nature 358:727-733.
7. Fourel, D., A. Bernadac, and J.-M. Pagès. 1994. Involvement of exposed polypeptide loops in trimeric and membrane insertion of Escherichia coli OmpF porin. Eur. J. Biochem. 222:625-630.
8. Fourel, D., S. Mizushima, A. Bernadac, and J.-M. Pagès. 1993. Specific regions of Escherichia coli OmpF protein involved in antigenic and colicin receptor sites and in stable trimerization. J. Bacteriol. 175:2754-2757.
9. Gill, M. J., S. Simjee, K. Al-Hattawi, B. D. Robertson, C. S. F. Easmon, and C. A. Ison. 1998. Gonococcal resistance to β-lactams and tetracycline involves mutation in loop 3 of the porin encoded at the penB locus. Antimicrob. Agents Chemother. 42:2799-2803.
10. Hancock, R. E. W. 1997. The bacterial outer membrane as a drug barrier. Trends Microbiol. 5:37-42.
11. Jeanteur, D., T. Schirmer, D. Fourel, V. Simonet, G. Rummel, J. P. Rosenbusch, and J.-M. Pagès. 1994. Structural and functional alterations of a colicin resistant mutant of OmpF from E. coli. Proc. Natl. Acad. Sci. USA 91:10675-10679.
12. Karshikoff, A., S. W. Cowan, V. Spassov, R. Ladenslein, and T. Schirmer. 1994. Electrostatic properties of two porin channels from E. coli. J. Mol. Biol. 240:372-384.
13. Lee, E. H., M. H. Nicolas, M. D. Kitzis, G. Pialoux, E. Collatz, and L. Gutmann. 1991. Association of two resistance mechanisms in a clinical isolate of Enterobacter cloacae with high-level resistance to imipenem. Antimicrob. Agents Chemother. 35:1093-1098.
14. Lou, K. L., N. Saint, A. Prilipov, G. Rummel, S. A. Benson, J. P. Rosenbusch, and T. Schirmer. 1996. Structural and functional characterization of OmpF porin mutants selected for larger pore size. Crystallographic analysis. J. Biol. Chem. 271:20669-20675.
15. Lupi, N., A. Bourgois, A. Bernadac, S. Laboucarié, and J.-M. Pagès. 1989. Immunological analysis of porin polymorphism in Escherichia coli B and K-12. Mol. Immunol. 26:1027-1036.
16. Malléa, M., J. Chevalier, C. Bornet, A. Eyraud, A. Davin-Regli, C. Bollet, and J.-M. Pagès. 1998. Porin alteration and active efflux: two in vivo drug resistance strategies used by Enterobacter aerogenes. Microbiology 144:3003-3009.
17. Malléa, M., V. Simonet, L. Eun-Hee, E. Collatz, R. Gervier, L. Gutmann, and J.-M. Pagès. 1995. Biological and immunological comparisons of Enterobacter cloacae and Escherichia coli porins. FEMS Microbiol. Lett. 129:273-280.
18. Nikaido, H. 1994. Porins and specific diffusion channels in bacterial outer membranes. J. Biol. Chem. 269:3905-3908.
19. Nikaido. H. 1994. Prevention of drug access to bacterial targets: permeability barriers and active efflux. Science 264:382-388.
20. Nikaido, H. 1996. Outer membrane, p. 29-47. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, D.C.
21. Nikaido, H., W. Liu, and E. Y. Rosenberg. 1990 Outer membrane permeability and β-lactamase stability of dipolar ionic cephalosporins containing methoxyimino substituents. Antimicrob. Agents Chemother. 34:337-342.
22. Nikaido, H., and S. Normark. 1987. Sensitivity of Escherichia coli to various β-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic β-lactamases: a quantitative predictive treatment. Mol. Microbiol. 1:29-36.
23. Ohmori, H. 1994. A new method for strand discrimination in sequence-directed mutagenesis. Nucleic Acids Res. 22:884-885.
24. Pearlman, D. A., D. A. Case, J. W. Caldwell, W. S. Ross, T. E. Cheatham, D. M. Ferguson, G. L. Seibel, U. Chandra Singh, P. K. Keiner, and P. A. Kollman. 1995. AMBER 4.1. University of California, San Franscisco.
25. Phale, P. S., A. Philippsen, T. Kiefhaber, R. Koebnik, V. P. Phale, T. Schirmer, and J. P. Rosenbusch. 1998. Stability of trimeric OmpF porin: the contribution of the latching loop L2. Biochemistry 37:15663-15670.
26. Phale, P. S., T. Schirmer, A. Prilipov, A. Hardmeyer, and J. P. Rosenbusch. 1997. Voltage gating of E. coli porin channels: role of the constriction loop. Proc. Natl. Acad. Sci. USA 94:6741-6745.
27. Prilipov, A., P. S. Phale, P. Van Gelder, J. P. Rosenbusch, and R. Koebnik. 1998. Coupling site-directed mutagenesis with high-level expression: large scale production of mutant porins from E. coli. FEMS Microbiol. Lett. 163:65-72.
28. Pugsley, A. P. 1987. Nucleotide sequencing of the structural gene for colicin N reveals homology between the catalytic, C-terminal domains of colicins A and N. Mol. Microbiol. 1:317-325.
29. Saint, N., K. L. Lou, C. Widmer, M. Luckey, T. Schirmer, and J. P. Rosenbusch. 1996. Structural and functional characterization of OmpF porin mutants selected for larger pore size. Functional characterization. J. Biol. Chem. 271:20676-20680.
30. Sali, A., and T. Blundell. 1995. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
31. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
32. Suenaga, A., Y. Komeiji, M. Uebayasi, T. Meguro, M. Saito, and I. Yamato. 1998, Computational observation of an ion permeation through a channel protein. Biosci. Rep. 18:39-48.
33. Tieleman, D. P., and H. J. C. Berendsen. 1998. A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine hilayer. Biophys. J. 74:2786-2801.
34. van Gelder, P., N. Saint, P. Phale, E. F. Eppens, A. Prilipov, R. van Boxtel, J. F. Rosenbusch, and J. Tommassen. 1997. Voltage sensing in the PhoE and OmpF outer membrane porins of Escherichia coli: role of charged residues. J. Mol. Biol. 269:468-472.
35. Vetter, I. R., M. W. Parker, A. D. Tucker, J. H. Lakey, F. Pattus, and D. Tsernoglou. 1998. Crystal structure of a colicin N fragment suggests a model for toxicity. Structure 6:863-874.
36. Watanabe, M., J. P. Rosenbusch, T. Schirmer, and M. Karplus. 1997. Computer simulations of the OmpF porin from the outer membrane of Escherichia coli. Biophys. J. 72:2094-2102.
37. Yoshimura, F., and H. Nikaido. 1985. Diffusion of β-lactam antibiotics through the porin channels of E. coli K-12. Antimicrob. Agents Chemother. 27:84-92.