Role of beta-lactam hydrolysis in the mechanism of resistance of a beta-lactamase-constitutive Enterobacter cloacae strain to expanded-spectrum beta-lactams

  title={Role of beta-lactam hydrolysis in the mechanism of resistance of a beta-lactamase-constitutive Enterobacter cloacae strain to expanded-spectrum beta-lactams},
  author={H K Vu and Hiroshi Nikaido},
  journal={Antimicrobial Agents and Chemotherapy},
  pages={393 - 398}
  • H. Vu, H. Nikaido
  • Published 1 March 1985
  • Chemistry, Medicine
  • Antimicrobial Agents and Chemotherapy
Enterobacter cloacae strains producing chromosomally mediated beta-lactamase constitutively show high degrees of resistance to most of the third-generation beta-lactams. It has been proposed that this resistance is due to the nonhydrolytic binding or trapping of beta-lactams by the enzyme. We found that the outer membrane of E. cloacae strain 55M indeed had permeability to cefazolin about 14-fold lower than that of Escherichia coli, and that the number of beta-lactamase molecules produced by… 
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Chromosomal beta-lactamase expression and antibiotic resistance in Enterobacter cloacae.
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Relative importances of outer membrane permeability and group 1 beta-lactamase as determinants of meropenem and imipenem activities against Enterobacter cloacae
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Type I β-Lactamases of Gram-Negative Bacteria: Interactions with β-Lactam Antibiotics
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Emergence of Resistance to β-Lactam Agents in Enterobacteriaceae Species with Group I β-Lactamases in Spain
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Permeability to cefsulodin of the outer membrane of Pseudomonas aeruginosa and discrimination between beta-lactamase-mediated trapping and hydrolysis as mechanisms of resistance.
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Resistance to cefamandole: derepression of beta-lactamases by cefoxitin and mutation in Enterobacter cloacae.
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Emergence of Resistance to Cefamandole: Possible Role of Cefoxitin-Inducible Beta-Lactamases
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Function of the Outer Membrane of Escherichia coli as a Permeability Barrier to Beta-Lactam Antibiotics
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Kinetics and significance of the activity of the Sabath and Abrahams' beta-lactamase of Pseudomonas aeruginosa against cefotaxime and cefsulodin.
  • D. Livermore
  • Biology, Medicine
    The Journal of antimicrobial chemotherapy
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Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibacterial activity.
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