Efficacy and safety of novel β-lactam/β-lactamase inhibitor combinations for the treatment of complicated urinary tract infections or acute pyelonephritis: A systematic review and meta-analysis [PDF]
Journal of Global Antimicrobial ResistanceObjectives: The increasing resistance of gram-negative bacteria in complicated urinary tract infections (cUTI) and acute pyelonephritis (APN) poses major treatment challenges.
Sirui Tang +3 more
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Frontiers in Cellular and Infection Microbiology, 2022 ObjectivesThe addition of novel β-lactamase inhibitors to carbapenems restores the activity against multidrug-resistant Gram-negative bacteria. The aim of this study was to summarize the evidence on the efficacy and safety of novel carbapenem–β-lactamase
Wei Yu +4 more
doaj +1 more source
Outer membrane permeability of β-lactamase inhibitors inPseudomonas aeruginosa [PDF]
FEMS Microbiology Letters, 1995 Evaluation of four beta-lactamase inhibitors in terms of their outer membrane permeability in Pseudomonas aeruginosa revealed that sulbactam and tazobactam diffused most efficiently and equally well. That of BRL42715 appeared to be a factor of ten lower than that of the above two, but it showed the strongest beta-lactamase inhibitory activity.
S, Satake, T, Nakae
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Iranian Journal of Microbiology, 2022 Background and Objectives: Escherichia coli (E. coli) is an important member of Enterobacteriaceae family involved in severe infections. The increased rate of resistance towards different classes of antibiotics limits their treatment options. The aim of
Ashraf Ahmed Kadry +2 more
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Comparative Evaluation of the in-vitro Activity of Six β-lactam/β-lactamase Inhibitor Combinations against Gram Negative Bacilli [PDF]
Journal of Clinical and Diagnostic Research, 2013 Background: The extensive use of the β-lactam antibiotics in hospitals and in the community has created major resistance problems which has led to increased morbidity, mortality and healthcare costs.
Smita Sood
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Penetration of β-lactamase inhibitors into the periplasm of Gram-negative bacteria [PDF]
FEMS Microbiology Letters, 1999 The effectiveness of a beta-lactamase inhibitor/beta-lactam combination against Gram-negative pathogens depends on many interplaying factors, one of which is the penetration of the inhibitor across the outer membrane. In this work we have measured the relative penetrations of clavulanic acid, sulbactam, tazobactam and BRL 42715 into two strains of ...
Farmer TH, Degnan BA, Payne DJ
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Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance inEscherichia coliexpressing IMP-1 [PDF]
FEMS Microbiology Letters, 2005 IMP-1 metallo-beta-lactamase is a zinc metalloenzyme that confers antibiotic resistance to bacteria through the hydrolysis of beta-lactam antibiotics. Pathogens that express the enzyme show reduced susceptibility to carbapenems, such as meropenem and imipenem.
Joseph G, Moloughney +2 more
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Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to β-lactamase inhibitors [PDF]
FEMS Microbiology Letters, 1994 The clinical isolate Escherichia coli PEY was highly resistant to amoxycillin, ticarcillin and piperacillin associated to beta-lactamase inhibitors such as clavulanic acid, sulbactam, tazobactam and brobactam but susceptible to cephalosporins, aztreonam and imipenem.
T, Brun +6 more
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Substitution of Met-69 by Ala or Gly in TEM-1 β-lactamase confer an increased susceptibility to clavulanic acid and other inhibitors [PDF]
FEMS Microbiology Letters, 2002 In some inhibitor-resistant TEM-derived beta-lactamases, Met-69 is substituted by Leu, Ile or Val. Residue 69 is located in a region of strong structural constraints, at the beginning of H2 alpha-helix, and in the vicinity of B3 and B4 beta-strands.
Stéphanie, Madec +6 more
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Substitution of Arg-244 by Cys or Ser in SHV-1 and SHV-5 β-lactamases confers resistance to mechanism-based inhibitors and reduces catalytic efficiency of the enzymes [PDF]
FEMS Microbiology Letters, 1998 The conserved residue Arg-244 was substituted by the smaller uncharged amino acids Cys and Ser in SHV-1 and SHV-5 beta-lactamases by a PCR-based site-specific mutagenesis procedure. The mutant beta-lactamases displayed decreased susceptibility to clavulanate and, to a lesser extent, to tazobactam and sulbactam.
Giakkoupi, P +3 more
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