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clavulanate

  • 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
  • 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
  • Mechanisms of Resistance
    Inhibition by Avibactam and Clavulanate of the β-Lactamases KPC-2 and CTX-M-15 Harboring the Substitution N132G in the Conserved SDN Motif
    Clément Ourghanlian, Daria Soroka, Michel Arthur
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