Synergistic resistance mechanisms in Pseudomonas aeruginosa

Stratton, Charles W.; Tausk, Francisca

doi:10.1093/jac/19.4.413

Cited by 18 publications

(3 citation statements)

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“…Sanders and Sanders (8), who examined the ability of cephalosporins to select derepressed mutants producing /~-lactamases among Enterobacteriaceae and Pseudomonas aeruginosa, reported that the in vitro activity of cefepime was least affected. The observed discrepancy in susceptibility to ceftazidime and cefepime In the present study may be explained by the fact that resistance o f Pseudomonas aeruginosa to beta-lactams may depend on a varying extent of different factors, ineluding beta-lactamase level, antibiotic penetration and altered penicillin binding proteins (9). In our study, the rather high preva/ence of resistance (26%) to cefepime, an antibiotic that has never been used for patient therapy in our hospital, is disturbing and difficult to explain, Since cefepime shows rerriarkable stability towards and low affinity for the commonly occurring betaqactamases (4,10), and the rate of selection of resistant mutants by cefepime is extremely low (7, I1), a common permeability barrier can be speculated.…”

Section: Methodscontrasting

confidence: 58%

Comparative in vitro activity of cefepime (BMY 28142) against multiresistant nosocomial isolates ofPseudomonas aeruginosa

Voutsinas

Mavroudis

Avlamis

et al. 1989

Eur. J. Clin. Microbiol. Infect. Dis.

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The in vitro activity of a new parenteral cephalosporin cefepime (BMY 28142) was compared with that of ceftazidime, cefotaxime, piperacillin, imipenem, gentamicin, amikacin and ciprofloxacin against 173 recent multiresistant Pseudomonas aeruginosa isolates of nosocomial origin using an agar dilution technique with an inoculum of 10(4) CFU per spot. The activity of cefepime was comparable to that of ceftazidime, superior to that of cefotaxime, piperacillin, gentamicin and amikacin, but inferior to that of imipenem and ciprofloxacin. Cross-resistance of Pseudomonas aeruginosa to ceftazidime and cefepime occurred in nearly 50% of the cefepime resistant strains and 61.5% of the ceftazidime resistant strains respectively.

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Section: Methodscontrasting

confidence: 58%

Comparative in vitro activity of cefepime (BMY 28142) against multiresistant nosocomial isolates ofPseudomonas aeruginosa

Voutsinas

Mavroudis

Avlamis

et al. 1989

Eur. J. Clin. Microbiol. Infect. Dis.

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“…Nevertheless, bacterial resistance to P-lactam drugs may arise during treatment as a consequence of derepression or activation of chromosomal ,-lactamase (6,10,12), modifications of outer membrane proteins (OMPs) (10,12), or altered penicillin-binding proteins (PBPs) (9,10). In some cases, combinations of these mechanisms may provoke a synergistic effect, leading to an increased level of resistance (20).…”

mentioning

confidence: 99%

Beta-lactam-fosfomycin antagonism involving modification of penicillin-binding protein 3 in Pseudomonas aeruginosa

Reguera

Baquero

Berenguer

et al. 1990

Antimicrob Agents Chemother

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Antagonism between fosfomycin and antipseudomonal penicillins, cefotaxime, and ceftriaxone was observed in Pseudomonas aeruginosa RYC212. Fosfomycin, a non-i-lactam antibiotic that acts on bacterial cell wall synthesis, decreased the expression of penicillin-binding protein 3 and induced j8-lactamase. The antagonistic effect was reduced in the presence of high concentrations of the ,l-lactamase inhibitor tazobactam or in fosfomycin-resistant mutants. We suggest that products resulting from fosfomycin cell wail damage could interact with a system that regulates penicillin-binding protein and I8-lactamase production.

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“…The in creased P-lactam resistance of P. aeruginosa isolates did not result from the altered pro duction of p-lactamases, since 23% of resis tant strains did not possess the enzyme. It should be emphasized, therefore, that P-lactamase alone could not account for the high lev el of resistance found in these strains [17], Hence the interaction between the penetra tion rate and the rate of removal by hydrolysis plays an important role in the activity of (3-lactams against P. aeruginosa strains [18]. Simpson et al [19] reported that some bacte ria such as Enterobacter spp.…”

Section: Discussionmentioning

confidence: 99%

Effect of Beta-Lactamase Expression on Susceptibility of Local Isolates of Enterobacter cloacae, Serratia marcescens and Pseudomonas aeruginosasBeta-Lactam Antibiotics

Ramadan

Tawfik²,

Shibl³

1995

Chemotherapy

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During surveillance studies, a total of 66 strains of gram-negative bacilli (28 Enterobacter cloacae, 20 Serratia marcescens and 18 Pseudomonas aeruginosa) with a reduced susceptibility to third-generation cephalosporins, aztreonam and amikacin were isolated from documented infections. All isolates were highly susceptible to imipenem and sparfloxacin. β-Lactamase activity was demonstrated in all isolates of E. cloacae and S. marcescens, and in 77% of P. aeruginosa isolates. Inducible β-lactamase activity was detected in 80, 65 and 40% of E. cloacae, S. marcescens and P. aeruginosa isolates, respectively, when cefoxitin was used as an inducer. More inducible β-lactamase producers were observed when imipenem was used as an inducer. Isolates of E. cloacae, and to a lesser extent S. marcescens, expressed a wide spectrum of β-lactamase activities. There was a good correlation between baseline β-lactamase activity and the respective MIC of ceftazidime, cefotaxime and ceftriaxone, and to a lesser extent aztreonam in E. cloacae and S. marcescens isolates. Only one isolate of E. cloacae demonstrated an extended β-lactamase activity. The data suggest that the resistance of E. cloacae and S. marcescens isolates to β-lactam antibiotics is largely dependent upon hyperproduction of β-lactamase.

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Synergistic resistance mechanisms in Pseudomonas aeruginosa

Cited by 18 publications

References 0 publications

Comparative in vitro activity of cefepime (BMY 28142) against multiresistant nosocomial isolates ofPseudomonas aeruginosa

Comparative in vitro activity of cefepime (BMY 28142) against multiresistant nosocomial isolates ofPseudomonas aeruginosa

Beta-lactam-fosfomycin antagonism involving modification of penicillin-binding protein 3 in Pseudomonas aeruginosa

Effect of Beta-Lactamase Expression on Susceptibility of Local Isolates of <i>Enterobacter cloacae, Serratia marcescens </i>and <i>Pseudomonas aeruginosas</i>Beta-Lactam Antibiotics

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