ceftazidime and Burns

ceftazidime has been researched along with Burns* in 2 studies

Other Studies

2 other study(ies) available for ceftazidime and Burns

Article	Year
Acquisition of a transposon encoding extended-spectrum beta-lactamase SHV-12 by Pseudomonas aeruginosa isolates during the clinical course of a burn patient. Antimicrobial agents and chemotherapy, 2010, Volume: 54, Issue:9 Three of seven clonally related Pseudomonas aeruginosa strains isolated from a burn patient produced the extended-spectrum beta-lactamase (ESBL) SHV-12. Its gene was flanked by two IS26 elements with a large transposon (>24 kb). The transposon also contained at least five IS26 elements and a gene encoding the amikacin resistance determinant aminoglycoside 6'-N-acetyltransferase type Ib [aac(6')-Ib]. It was inserted into the gene PA5317 in the P. aeruginosa chromosome. Topics: Adult; beta-Lactamases; Burns; DNA Transposable Elements; Female; Humans; Microbial Sensitivity Tests; Polymerase Chain Reaction; Pseudomonas aeruginosa	2010
In vitro and in vivo activities of a new cephalosporin, FR264205, against Pseudomonas aeruginosa. Antimicrobial agents and chemotherapy, 2007, Volume: 51, Issue:3 FR264205 is a novel parenteral 3'-aminopyrazolium cephalosporin. This study evaluated the in vitro and in vivo activities of FR264205 against Pseudomonas aeruginosa. The MIC of FR264205 at which 90% of 193 clinical isolates of P. aeruginosa were inhibited was 1 microg/ml, 8- to 16-fold lower than those of ceftazidime (CAZ), imipenem (IPM), and ciprofloxacin (CIP). FR264205 also exhibited this level of activity against CAZ-, IPM-, and CIP-resistant P. aeruginosa. The reduction in the susceptibility of FR264205 by AmpC beta-lactamase was lower than that of CAZ, indicating a relatively high stability of FR264205 against AmpC beta-lactamase, the main resistance mechanism for cephalosporins. Neither expression of efflux pumps nor deficiency of OprD decreased the activity of FR264205. No spontaneous resistance mutants were selected in the presence of FR264205, and the reduction in susceptibility to FR264205 was lower than that to CAZ, IPM, and CIP after serial passage, suggesting that FR264205 has a low propensity for selecting resistance. In murine pulmonary, urinary tract, and burn wound models of infection caused by P. aeruginosa, the efficacy of FR264205 was superior or comparable to those of CAZ and IPM. These results indicate that FR264205 should have good potential as an antibacterial agent for P. aeruginosa. Topics: Animals; beta-Lactamases; Burns; Cephalosporins; Drug Resistance, Multiple, Bacterial; Lung Diseases; Mice; Mice, Inbred ICR; Microbial Sensitivity Tests; Mutation; Pseudomonas aeruginosa; Pseudomonas Infections; Urinary Tract Infections; Wound Infection	2007

Article

Year

Acquisition of a transposon encoding extended-spectrum beta-lactamase SHV-12 by Pseudomonas aeruginosa isolates during the clinical course of a burn patient.

Antimicrobial agents and chemotherapy, 2010, Volume: 54, Issue:9

Three of seven clonally related Pseudomonas aeruginosa strains isolated from a burn patient produced the extended-spectrum beta-lactamase (ESBL) SHV-12. Its gene was flanked by two IS26 elements with a large transposon (>24 kb). The transposon also contained at least five IS26 elements and a gene encoding the amikacin resistance determinant aminoglycoside 6'-N-acetyltransferase type Ib [aac(6')-Ib]. It was inserted into the gene PA5317 in the P. aeruginosa chromosome.

Topics: Adult; beta-Lactamases; Burns; DNA Transposable Elements; Female; Humans; Microbial Sensitivity Tests; Polymerase Chain Reaction; Pseudomonas aeruginosa

2010

In vitro and in vivo activities of a new cephalosporin, FR264205, against Pseudomonas aeruginosa.

Antimicrobial agents and chemotherapy, 2007, Volume: 51, Issue:3

FR264205 is a novel parenteral 3'-aminopyrazolium cephalosporin. This study evaluated the in vitro and in vivo activities of FR264205 against Pseudomonas aeruginosa. The MIC of FR264205 at which 90% of 193 clinical isolates of P. aeruginosa were inhibited was 1 microg/ml, 8- to 16-fold lower than those of ceftazidime (CAZ), imipenem (IPM), and ciprofloxacin (CIP). FR264205 also exhibited this level of activity against CAZ-, IPM-, and CIP-resistant P. aeruginosa. The reduction in the susceptibility of FR264205 by AmpC beta-lactamase was lower than that of CAZ, indicating a relatively high stability of FR264205 against AmpC beta-lactamase, the main resistance mechanism for cephalosporins. Neither expression of efflux pumps nor deficiency of OprD decreased the activity of FR264205. No spontaneous resistance mutants were selected in the presence of FR264205, and the reduction in susceptibility to FR264205 was lower than that to CAZ, IPM, and CIP after serial passage, suggesting that FR264205 has a low propensity for selecting resistance. In murine pulmonary, urinary tract, and burn wound models of infection caused by P. aeruginosa, the efficacy of FR264205 was superior or comparable to those of CAZ and IPM. These results indicate that FR264205 should have good potential as an antibacterial agent for P. aeruginosa.

Topics: Animals; beta-Lactamases; Burns; Cephalosporins; Drug Resistance, Multiple, Bacterial; Lung Diseases; Mice; Mice, Inbred ICR; Microbial Sensitivity Tests; Mutation; Pseudomonas aeruginosa; Pseudomonas Infections; Urinary Tract Infections; Wound Infection

2007