Contribution of beta-lactamase hydrolysis and outer membrane permeability to ceftriaxone resistance in Enterobacter cloacae

Marchou, B.; Bellido, F.; Charnas, Robert L.; Lucain, C; Péchère, Jean-Claude

doi:10.1128/aac.31.10.1589

Cited by 49 publications

(44 citation statements)

References 28 publications

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“…An exceptional ability of imipenem to remain growthinhibitory at low concentration has been reported frequently for P-lactamase-overproducing and penetration-restricted Enterobacter cloacae highly resistant to other extended-spectrum p-lactams (Bush et al, 1985 ;Werner et al, 1985;Then & Angehrn, 1986;Marchou et al, 1987). For P. aeruginosa it has been proposed that imipenem uses specific penetration channels which are impermeable for other p-lactams (Buscher et al, 1987;Nikaido, 1989).…”

Section: Binding Of P-lactams To Pbps In Growing Cells Of S Marcescmentioning

confidence: 99%

“…This has been found to be related to the limitation of antibiotic penetration by the outer membrane barrier and the degradation of the p-lactams by overproduced, chromosomally encoded p-lactamase in the bacterial periplasm (Vu & Nikaido, 1985;Bush et al, 1985;Marchou et al, 1987;Nikaido & Normark, 1987;Hechler et al, 1989;Nikaido, 1989) combined functions of both resistance factors are thought to block the access of the antibiotics to their targets, the essential penicillin-binding proteins (PBPs), on the bacterial cytoplasmic membrane.…”

Section: Introductionmentioning

confidence: 99%

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State of penicillin-binding proteins and requirements for their bactericidal interaction with β-lactam antibiotics in Serratia marcescens highly resistant to extended-spectrum β-lactams

Gunkel

Hechler²,

Martin

1991

Microbiology

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The quantities of penicillin-binding proteins (PBPs), and sensitivity to extended-spectrum p-lactams, were measured in isogenic strains of Serrutia marcescens with high (HR) and low (LR) resistance to extended-spectrum Elactam antibiotics and with constitutively overproduced chromosomal P-lactamase in the periplasm. The binding of structurally different p-lactams to PBPs in growing resistant bacteria was determined quantitatively. In S. murcescens HR, the amounts of PBPs 3 and 6 were, respectively, 1.5 and 2 times those in strain LR and in sensitive reference strains. Sensitivities of the essential PBPs in S. murcescens LR and HR to the tested p-lactams were identical. Only a single target, PBP 3, was highly sensitive to cefotaxime, ceftazidime and aztreonam. In contrast, three PBPs (2,lA and 3) were highly sensitive to imipenem. In growing S. murcescens HR and LR, all antibiotics, even at fractions of their minimal growth inhibitory concentrations (MICs), bound extensively to those PBPs which were highly sensitive to them. Thus, overproduced P-lactamase did not prevent PBP-P-lactam interaction. Only at or above their (high) MICs did cefotaxime, ceftazidime and aztreonam bind to multiple targets. Growth inhibition of the otherwise highly resistant S. murcescens HR at the lower MIC of imipenem was correlated with the binding of this antibiotic to multiple, highly sensitive targets in the bacteria. Killing of the bacteria by inactivation of multiple targets was suggested. This assumption was supported by the synergistic killing of HR bacteria by combinations of the PBP-2-specific mecillinam with PBP-3-specific p-lactams.

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Section: Binding Of P-lactams To Pbps In Growing Cells Of S Marcescmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

State of penicillin-binding proteins and requirements for their bactericidal interaction with β-lactam antibiotics in Serratia marcescens highly resistant to extended-spectrum β-lactams

Gunkel

Hechler²,

Martin

1991

Microbiology

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“…Existen microorganismos patógenos, como E. cloacae, con la capacidad de producir por vía cromosómica o constitutiva betalactamasas de clase C (cefalosporinasas) y, por esta razón, han desarrollado resistencia frente a los fármacos betalactámicos (12,13).…”

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Actividad inhibitoria de dihidroxifenilpropenona sobre β-lactamasa de Enterobacter cloacae: estudio preliminar en el desarrollo de fármacos para enfrentar la resistencia bacteriana

2013

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“…The inoculum contained c. 10 4 cfu per spot. The second method used antibiotic gradient containing plates, as described previously (Marchou et al, 1987a). The inoculum was c. 10* per dish.…”

Section: Growth-inhibitory Activitymentioning

confidence: 99%

Development of resistance during ceftazidime and cefepime therapy in a murine peritonitis model

Péchère¹,

Vladoianu²

1992

J Antimicrob Chemother

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Resistance emerging after ceftazidime or cefepime therapy was investigated in a peritonitis model. Mice were given a peritoneal challenge (10* cfu plus talcum) and treated by either antibiotic (50 mg/kg/dose, which produced similar antibiotic concentrations in peritoneal fluid in both cases). After one or three doses, resistance never developed in Serratia marcescens or Citrobacter freiouiii infections. After Enterobacter cloacae and Pseudomonas aeruginosa challenge, ceftazidime selected more resistance (21/36 cases) than did cefepime (1/36 cases). In mice challenged with resistant strains selected by ceftazidime therapy, cefepime (six doses) successfully treated 7/18 E. cloacae infections but 0/18 P. aeruginosa infections; ceftazidime was never effective. Neither cefepime nor ceftazidime cured mice infected with the resistant strain selected by cefepime. MICs were poor predictors of further emergence of resistance in mice inoculated with strains classified as susceptible, but antibiotic-containing agar gradients plated with a high inoculum (10* cfu) allowed better prediction. In selected clinical situations, cefepime may be preferable because it may be associated with less frequent emergence of resistance.

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Contribution of beta-lactamase hydrolysis and outer membrane permeability to ceftriaxone resistance in Enterobacter cloacae

Cited by 49 publications

References 28 publications

State of penicillin-binding proteins and requirements for their bactericidal interaction with β-lactam antibiotics in Serratia marcescens highly resistant to extended-spectrum β-lactams

State of penicillin-binding proteins and requirements for their bactericidal interaction with β-lactam antibiotics in Serratia marcescens highly resistant to extended-spectrum β-lactams

Actividad inhibitoria de dihidroxifenilpropenona sobre β-lactamasa de Enterobacter cloacae: estudio preliminar en el desarrollo de fármacos para enfrentar la resistencia bacteriana

Development of resistance during ceftazidime and cefepime therapy in a murine peritonitis model

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