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avibactam

  • Open Access
    Structural Investigations of the Inhibition of <span class="named-content genus-species" id="named-content-1">Escherichia coli</span> AmpC β-Lactamase by Diazabicyclooctanes
    Mechanisms of Resistance
    Structural Investigations of the Inhibition of Escherichia coli AmpC β-Lactamase by Diazabicyclooctanes

    β-Lactam antibiotics are presently the most important treatments for infections by pathogenic Escherichia coli, but their use is increasingly compromised by β-lactamases, including the chromosomally encoded class C AmpC serine-β-lactamases (SBLs). The diazabicyclooctane (DBO) avibactam is a potent AmpC inhibitor; the clinical success of avibactam combined with...

    Pauline A. Lang, Thomas M. Leissing, Malcolm G. P. Page, Christopher J. Schofield, Jürgen Brem
  • Activity of Aztreonam in Combination with Avibactam, Clavulanate, Relebactam, and Vaborbactam against Multidrug-Resistant <span class="named-content genus-species" id="named-content-1">Stenotrophomonas maltophilia</span>
    Experimental Therapeutics
    Activity of Aztreonam in Combination with Avibactam, Clavulanate, Relebactam, and Vaborbactam against Multidrug-Resistant Stenotrophomonas maltophilia

    The intrinsic L1 metallo- and L2 serine-β-lactamases in Stenotrophomonas maltophilia make it naturally multidrug resistant and difficult to treat. There is a need to identify novel treatment strategies for this pathogen, especially against isolates resistant to first-line agents. Aztreonam in combination with avibactam has demonstrated potential, although data on...

    M. Biagi, D. Lamm, K. Meyer, A. Vialichka, M. Jurkovic, S. Patel, R. E. Mendes, Z. P. Bulman, E. Wenzler
  • Adding Insult to Injury: Mechanistic Basis for How AmpC Mutations Allow <span class="named-content genus-species" id="named-content-1">Pseudomonas aeruginosa</span> To Accelerate Cephalosporin Hydrolysis and Evade Avibactam
    Editor's Pick Mechanisms of Resistance
    Adding Insult to Injury: Mechanistic Basis for How AmpC Mutations Allow Pseudomonas aeruginosa To Accelerate Cephalosporin Hydrolysis and Evade Avibactam

    Pseudomonas aeruginosa is a leading cause of nosocomial infections worldwide and notorious for its broad-spectrum resistance to antibiotics. A key mechanism that provides extensive resistance to β-lactam antibiotics is the inducible expression of AmpC β-lactamase. Recently, a number of clinical isolates expressing mutated forms of AmpC have been found to be clinically...

    Cole L. Slater, Judith Winogrodzki, Pablo A. Fraile-Ribot, Antonio Oliver, Mazdak Khajehpour, Brian L. Mark
  • Structural Basis of Reduced Susceptibility to Ceftazidime-Avibactam and Cefiderocol in <em>Enterobacter cloacae</em> Due to AmpC R2 Loop Deletion
    Mechanisms of Resistance
    Structural Basis of Reduced Susceptibility to Ceftazidime-Avibactam and Cefiderocol in Enterobacter cloacae Due to AmpC R2 Loop Deletion

    Ceftazidime-avibactam and cefiderocol are two of the latest generation β-lactam agents that possess expanded activity against highly drug-resistant bacteria, including carbapenem-resistant Enterobacterales. Here, we show that structural changes in AmpC β-lactamases can confer reduced susceptibility to both agents. A multidrug-resistant Enterobacter cloacae...

    Akito Kawai, Christi L. McElheny, Alina Iovleva, Ellen G. Kline, Nicolas Sluis-Cremer, Ryan K. Shields, Yohei Doi
  • Ceftazidime-Avibactam Resistance Mediated by the N<sup>346</sup>Y Substitution in Various AmpC β-Lactamases
    Mechanisms of Resistance
    Ceftazidime-Avibactam Resistance Mediated by the N346Y Substitution in Various AmpC β-Lactamases

    Chromosomal and plasmid-borne AmpC cephalosporinases are a major resistance mechanism to β-lactams in Enterobacteriaceae and Pseudomonas aeruginosa. The new β-lactamase inhibitor avibactam effectively inhibits class C enzymes and can fully restore ceftazidime susceptibility. The conserved amino acid residue Asn346 of AmpC cephalosporinases directly...

    Fabrice Compain, Agathe Debray, Pauline Adjadj, Delphine Dorchêne, Michel Arthur
  • Ceftazidime-Avibactam Resistance Associated with Increased <em>bla</em><sub>KPC-3</sub> Gene Copy Number Mediated by pKpQIL Plasmid Derivatives in Sequence Type 258 <em>Klebsiella pneumoniae</em>
    Mechanisms of Resistance
    Ceftazidime-Avibactam Resistance Associated with Increased blaKPC-3 Gene Copy Number Mediated by pKpQIL Plasmid Derivatives in Sequence Type 258 Klebsiella pneumoniae

    This study reports on the characterization of two ceftazidime-avibactam (CZA)-resistant KPC-producing Klebsiella pneumoniae strains (KP-14159 and KP-8788) sequentially isolated from infections occurred in a patient never treated with CZA. Whole-genome sequencing characterization using a combined short- and long-read sequencing approach showed that both isolates...

    Marco Coppi, Vincenzo Di Pilato, Francesco Monaco, Tommaso Giani, Pier Giulio Conaldi, Gian Maria Rossolini
  • β-Lactamase of <span class="named-content genus-species" id="named-content-1">Mycobacterium tuberculosis</span> Shows Dynamics in the Active Site That Increase upon Inhibitor Binding
    Mechanisms of Resistance
    β-Lactamase of Mycobacterium tuberculosis Shows Dynamics in the Active Site That Increase upon Inhibitor Binding

    The Mycobacterium tuberculosis β-lactamase BlaC is a broad-spectrum β-lactamase that can convert a range of β-lactam antibiotics. Enzymes with low specificity are expected to exhibit active-site flexibility. To probe the motions in BlaC, we studied the dynamic behavior in solution using nuclear magnetic resonance (NMR) spectroscopy. 15N relaxation...

    Wouter Elings, Anamika Gaur, Anneloes J. Blok, Monika Timmer, Hugo van Ingen, Marcellus Ubbink
  • Inhibition Activity of Avibactam against <span class="named-content genus-species" id="named-content-1">Nocardia farcinica</span> β-Lactamase FAR<sub>IFM10152</sub>
    Editor's Pick Mechanisms of Resistance
    Inhibition Activity of Avibactam against Nocardia farcinica β-Lactamase FARIFM10152

    Nocardia farcinica, one of the most frequent pathogenic species responsible for nocardiosis, is characterized by frequent brain involvement and resistance to β-lactams mediated by a class A β-lactamase. Kinetic parameters for hydrolysis of various β-lactams by FARIFM10152 from strain IFM 10152 were determined by spectrophotometry revealing a high catalytic...

    David Lebeaux, Clément Ourghanlian, Delphine Dorchène, Daria Soroka, Zainab Edoo, Fabrice Compain, Michel Arthur
  • Open Access
    Molecular Basis of Class A β-Lactamase Inhibition by Relebactam
    Mechanisms of Resistance
    Molecular Basis of Class A β-Lactamase Inhibition by Relebactam

    β-Lactamase production is the major β-lactam resistance mechanism in Gram-negative bacteria. β-Lactamase inhibitors (BLIs) efficacious against serine β-lactamase (SBL) producers, especially strains carrying the widely disseminated class A enzymes, are required. Relebactam, a diazabicyclooctane (DBO) BLI, is in phase 3 clinical trials in combination with imipenem for the treatment of infections by multidrug-resistant...

    Catherine L. Tooke, Philip Hinchliffe, Pauline A. Lang, Adrian J. Mulholland, Jürgen Brem, Christopher J. Schofield, James Spencer
  • Patient-to-Patient Transmission of <span class="named-content genus-species" id="named-content-1">Klebsiella pneumoniae</span> Carbapenemase Variants with Reduced Ceftazidime-Avibactam Susceptibility
    Mechanisms of Resistance
    Patient-to-Patient Transmission of Klebsiella pneumoniae Carbapenemase Variants with Reduced Ceftazidime-Avibactam Susceptibility

    We report patient-to-patient transmission of Enterobacter hormaechei isolates with reduced susceptibility to ceftazidime-avibactam due to production of KPC-40, a variant of KPC-3 with a two-amino-acid insertion in the Ω-loop region (L167_E168dup). The index patient had received a prolonged course of ceftazidime-avibactam therapy, whereas the second patient had not...

    L. Silvia Munoz-Price, Allison E. Reeme, Blake W. Buchan, Roberta T. Mettus, Mustapha M. Mustapha, Daria Van Tyne, Ryan K. Shields, Yohei Doi

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