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beta-lactamase inhibitors

  • Open Access
    Potency of Vaborbactam Is Less Affected than That of Avibactam in Strains Producing KPC-2 Mutations That Confer Resistance to Ceftazidime-Avibactam
    Editor's Pick Mechanisms of Resistance
    Potency of Vaborbactam Is Less Affected than That of Avibactam in Strains Producing KPC-2 Mutations That Confer Resistance to Ceftazidime-Avibactam

    Resistance to ceftazidime-avibactam due to mutations in KPC genes has been reported both in vitro and in clinical settings. The most frequently reported mutation leads to the amino acid substitution D179Y in the Ω loop of the enzyme. Bacterial cells that carry mutant KPC acquire a higher level of ceftazidime resistance, become more sensitive to other cephalosporins, and almost completely lose resistance to carbapenems. In this...

    Ruslan Tsivkovski, Olga Lomovskaya
  • Open Access
    Biochemical Activity of Vaborbactam
    Editor's Pick Mechanisms of Action: Physiological Effects
    Biochemical Activity of Vaborbactam

    The most common mechanism of resistance to β-lactams antibiotics in Gram-negative bacteria is production of β-lactamase enzymes capable of cleaving the β-lactam ring. Inhibition of β-lactamase activity with small-molecule drugs is a proven strategy to restore the potency of many β-lactam antibiotics.

    Ruslan Tsivkovski, Olga Lomovskaya
  • Optimal Piperacillin-Tazobactam Dosing Strategies against Extended-Spectrum-β-Lactamase-Producing <em>Enterobacteriaceae</em>
    Experimental Therapeutics
    Optimal Piperacillin-Tazobactam Dosing Strategies against Extended-Spectrum-β-Lactamase-Producing Enterobacteriaceae

    Piperacillin-tazobactam has been proposed as an alternative to carbapenems for the treatment of infections caused by extended-spectrum-β-lactamase (ESBL)-producing Enterobacteriaceae. However, limited understanding of optimal dosing strategies for this combination may curtail its utility.

    Henrietta Abodakpi, Kai-Tai Chang, Song Gao, Ana María Sánchez-Díaz, Rafael Cantón, Vincent H. Tam
  • Pharmacology
    First Penicillin-Binding Protein Occupancy Patterns of β-Lactams and β-Lactamase Inhibitors in Klebsiella pneumoniae
    Dhruvitkumar S. Sutaria, Bartolome Moya, Kari B. Green, Tae Hwan Kim, Xun Tao, Yuanyuan Jiao, Arnold Louie, George L. Drusano, Jürgen B. Bulitta
  • Mechanisms of Resistance
    Kinetics of Sulbactam Hydrolysis by β-Lactamases, and Kinetics of β-Lactamase Inhibition by Sulbactam
    Adam B. Shapiro
  • Experimental Therapeutics
    Modified Penicillin Molecule with Carbapenem-Like Stereochemistry Specifically Inhibits Class C β-Lactamases
    Xuehua Pan, Yunjiao He, Tianfeng Chen, Kin-Fai Chan, Yanxiang Zhao
  • Pharmacology
    Pharmacokinetics-Pharmacodynamics of Tazobactam in Combination with Cefepime in an In Vitro Infection Model
    Brian D. VanScoy, David Tenero, Simon Turner, David M. Livermore, Jennifer McCauley, Haley Conde, Sujata M. Bhavnani, Christopher M. Rubino, Paul G. Ambrose
  • Experimental Therapeutics
    Pharmacokinetics-Pharmacodynamics of CB-618 in Combination with Cefepime, Ceftazidime, Ceftolozane, or Meropenem: the Pharmacological Basis for a Stand-Alone β-Lactamase Inhibitor
    Paul G. Ambrose, Brian D. VanScoy, Michael Trang, Jennifer McCauley-Miller, Haley Conde, Sujata M. Bhavnani, Dylan C. Alexander, Lawrence V. Friedrich
  • Mechanisms of Resistance
    Emergence of Ceftolozane-Tazobactam-Resistant Pseudomonas aeruginosa during Treatment Is Mediated by a Single AmpC Structural Mutation
    Shawn H. MacVane, Ruchi Pandey, Lisa L. Steed, Barry N. Kreiswirth, Liang Chen
  • Open Access
    Mechanisms of Resistance
    Vaborbactam: Spectrum of Beta-Lactamase Inhibition and Impact of Resistance Mechanisms on Activity in Enterobacteriaceae
    Olga Lomovskaya, Dongxu Sun, Debora Rubio-Aparicio, Kirk Nelson, Ruslan Tsivkovski, David C. Griffith, Michael N. Dudley

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