Reevaluation of the Factors Involved in the Efficacy of New Beta-lactams Against Enterobacter Cloacae

Overview

Journal Antimicrob Agents Chemother

Publisher American Society for Microbiology

Specialty Pharmacology

Date 1991 Jan 1

PMID 2014984

Citations 16

Authors

F Bellido

J C Pechere

R E Hancock

Affiliations

Soon will be listed here.

Abstract

The roles of outer membrane permeability, beta-lactamase stability, and inhibition of penicillin-binding proteins in the activity of new beta-lactams against Enterobacter cloacae were reappraised by using several methodological improvements. Outer membrane permeability in intact cells was determined by using a high-pressure liquid chromatography (HPLC)-based technique that avoided certain possible artifacts of the traditional methods. Vmax values were calculated from the numbers of enzyme molecules produced per cell and from catalytic constant (Kcat) values, which were obtained with purified beta-lactamase. Minimal periplasmic antibiotic concentrations needed to inhibit bacterial cell wall synthesis were estimated from the Zimmermann-Rosselet equation. All the beta-lactams tested formed relatively stable complexes with purified beta-lactamase. The antibiotics that exhibited low affinity for beta-lactamase apparently needed higher periplasmic concentrations to inhibit cell wall synthesis, suggesting a possible correlation between the affinity of beta-lactamase and the affinity of penicillin-binding proteins for the new beta-lactams. By using these estimates of outer membrane permeability, beta-lactamase hydrolysis, and cell wall-inhibiting concentrations, MIC could be theoretically predicted to within 1 dilution for five beta-lactams in three isogenic E. cloacae strains with differences in antibiotic susceptibility due to different porin or beta-lactamase contents.

Citing Articles

Antibacterial-resistant Pseudomonas aeruginosa: clinical impact and complex regulation of chromosomally encoded resistance mechanisms.

Lister P, Wolter D, Hanson N Clin Microbiol Rev. 2009; 22(4):582-610.

PMID: 19822890 PMC: 2772362. DOI: 10.1128/CMR.00040-09.

Method for estimation of low outer membrane permeability to beta-lactam antibiotics.

Lakaye B, Dubus A, Joris B, Frere J Antimicrob Agents Chemother. 2002; 46(9):2901-7.

PMID: 12183245 PMC: 127435. DOI: 10.1128/AAC.46.9.2901-2907.2002.

Mutational replacement of Leu-293 in the class C Enterobacter cloacae P99 beta-lactamase confers increased MIC of cefepime.

Vakulenko S, Golemi D, Geryk B, Suvorov M, Knox J, Mobashery S Antimicrob Agents Chemother. 2002; 46(6):1966-70.

PMID: 12019116 PMC: 127218. DOI: 10.1128/AAC.46.6.1966-1970.2002.

The development of beta-lactam antibiotics in response to the evolution of beta-lactamases.

Essack S Pharm Res. 2001; 18(10):1391-9.

PMID: 11697463 DOI: 10.1023/a:1012272403776.

Efficacies of imipenem, meropenem, cefepime, and ceftazidime in rats with experimental pneumonia due to a carbapenem-hydrolyzing beta-lactamase-producing strain of Enterobacter cloacae.

Mimoz O, Leotard S, Jacolot A, Padoin C, Louchahi K, Petitjean O Antimicrob Agents Chemother. 2000; 44(4):885-90.

PMID: 10722486 PMC: 89787. DOI: 10.1128/AAC.44.4.885-890.2000.

References

Smit J, Kamio Y, Nikaido H . Outer membrane of Salmonella typhimurium: chemical analysis and freeze-fracture studies with lipopolysaccharide mutants. J Bacteriol. 1975; 124(2):942-58. PMC: 235985. DOI: 10.1128/jb.124.2.942-958.1975. View

Then R, Angehrn P . Ways to overcome cephalosporinase-mediated beta-lactam resistance in Enterobacter cloacae. Chemioterapia. 1985; 4(1):83-9. View

Zimmermann W, Rosselet A . Function of the outer membrane of Escherichia coli as a permeability barrier to beta-lactam antibiotics. Antimicrob Agents Chemother. 1977; 12(3):368-72. PMC: 429920. DOI: 10.1128/AAC.12.3.368. View

Vu H, Nikaido H . Role of beta-lactam hydrolysis in the mechanism of resistance of a beta-lactamase-constitutive Enterobacter cloacae strain to expanded-spectrum beta-lactams. Antimicrob Agents Chemother. 1985; 27(3):393-8. PMC: 176283. DOI: 10.1128/AAC.27.3.393. View

Frere J, Joris B . Penicillin-sensitive enzymes in peptidoglycan biosynthesis. Crit Rev Microbiol. 1985; 11(4):299-396. DOI: 10.3109/10408418409105906. View

Werner V, Sanders C, Sanders Jr W, Goering R . Role of beta-lactamases and outer membrane proteins in multiple beta-lactam resistance of Enterobacter cloacae. Antimicrob Agents Chemother. 1985; 27(4):455-9. PMC: 180074. DOI: 10.1128/AAC.27.4.455. View

Bush K, Tanaka S, Bonner D, Sykes R . Resistance caused by decreased penetration of beta-lactam antibiotics into Enterobacter cloacae. Antimicrob Agents Chemother. 1985; 27(4):555-60. PMC: 180094. DOI: 10.1128/AAC.27.4.555. View

Livermore D . Do beta-lactamases 'trap' cephalosporins?. J Antimicrob Chemother. 1985; 15(5):511-4. DOI: 10.1093/jac/15.5.511. View

Phelps D, Carlton D, Farrell C, Kessler R . Affinity of cephalosporins for beta-lactamases as a factor in antibacterial efficacy. Antimicrob Agents Chemother. 1986; 29(5):845-8. PMC: 284164. DOI: 10.1128/AAC.29.5.845. View

10.

Kobayashi S, Arai S, Hayashi S, Fujimoto K . Beta-lactamase stability of cefpirome (HR 810), a new cephalosporin with a broad antimicrobial spectrum. Antimicrob Agents Chemother. 1986; 30(5):713-8. PMC: 176519. DOI: 10.1128/AAC.30.5.713. View

11.

Then R . Ability of newer beta-lactam antibiotics to induce beta-lactamase production in Enterobacter cloacae. Eur J Clin Microbiol. 1987; 6(4):451-5. DOI: 10.1007/BF02013109. View

12.

Marchou B, Bellido F, Charnas R, Lucain C, Pechere J . Contribution of beta-lactamase hydrolysis and outer membrane permeability to ceftriaxone resistance in Enterobacter cloacae. Antimicrob Agents Chemother. 1987; 31(10):1589-95. PMC: 174996. DOI: 10.1128/AAC.31.10.1589. View

13.

Hiraoka M, Masuyoshi S, Mitsuhashi S, Tomatsu K, Inoue M . Cephalosporinase interactions and antimicrobial activity of BMY-28142, ceftazidime and cefotaxime. J Antibiot (Tokyo). 1988; 41(1):86-93. DOI: 10.7164/antibiotics.41.86. View

14.

Nikaido H, Normark S . Sensitivity of Escherichia coli to various beta-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic beta-lactamases: a quantitative predictive treatment. Mol Microbiol. 1987; 1(1):29-36. DOI: 10.1111/j.1365-2958.1987.tb00523.x. View

15.

Then R, Charnas R, Kocher H, Manneberg M, Rothlisberger U, Stocker J . Biochemical characterization of type A and type B beta-lactamase from Enterobacter cloacae. Rev Infect Dis. 1988; 10(4):714-20. DOI: 10.1093/clinids/10.4.714. View

16.

Charnas R, Then R . Mechanism of inhibition of chromosomal beta-lactamases by third-generation cephalosporins. Rev Infect Dis. 1988; 10(4):752-60. DOI: 10.1093/clinids/10.4.752. View

17.

Bellido F, VLADOIANU I, Auckenthaler R, Suter S, Wacker P, Then R . Permeability and penicillin-binding protein alterations in Salmonella muenchen: stepwise resistance acquired during beta-lactam therapy. Antimicrob Agents Chemother. 1989; 33(7):1113-5. PMC: 176073. DOI: 10.1128/AAC.33.7.1113. View

18.

Bellido F, Veuthey C, Blaser J, Bauernfeind A, Pechere J . Novel resistance to imipenem associated with an altered PBP-4 in a Pseudomonas aeruginosa clinical isolate. J Antimicrob Chemother. 1990; 25(1):57-68. DOI: 10.1093/jac/25.1.57. View

19.

Nikaido H, Liu W, Rosenberg E . Outer membrane permeability and beta-lactamase stability of dipolar ionic cephalosporins containing methoxyimino substituents. Antimicrob Agents Chemother. 1990; 34(2):337-42. PMC: 171583. DOI: 10.1128/AAC.34.2.337. View

20.

WALEY S . An explicit model for bacterial resistance: application to beta-lactam antibiotics. Microbiol Sci. 1987; 4(5):143-6. View