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relebactam

  • 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
  • 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
  • <em>In Vitro</em> Activity of the New β-Lactamase Inhibitors Relebactam and Vaborbactam in Combination with β-Lactams against <span class="named-content genus-species" id="named-content-1">Mycobacterium abscessus</span> Complex Clinical Isolates
    Susceptibility
    In Vitro Activity of the New β-Lactamase Inhibitors Relebactam and Vaborbactam in Combination with β-Lactams against Mycobacterium abscessus Complex Clinical Isolates

    Pulmonary disease due to infection with Mycobacterium abscessus complex (MABC) is notoriously difficult to treat, in large part due to the intrinsic resistance of MABC strains to most antibiotics, including β-lactams. MABC organisms express a broad-spectrum β-lactamase that is resistant to traditional β-lactam-based β-lactamase inhibitors but inhibited by a newer non-...

    Amit Kaushik, Nicole C. Ammerman, Jin Lee, Olumide Martins, Barry N. Kreiswirth, Gyanu Lamichhane, Nicole M. Parrish, Eric L. Nuermberger
  • Open Access
    Pharmacology
    Pharmacokinetics, Safety, and Tolerability of Single and Multiple Doses of Relebactam, a β-Lactamase Inhibitor, in Combination with Imipenem and Cilastatin in Healthy Participants

    Relebactam is a novel class A and C β-lactamase inhibitor that is being developed in combination with imipenem-cilastatin for the treatment of serious infections with Gram-negative bacteria. Here we report on two phase 1 randomized, double-blind, placebo-controlled pharmacokinetics, safety, and tolerability studies of relebactam administered with or without imipenem-cilastatin to healthy participants: (i) a single-dose (25 to 1,150 mg)...

    Elizabeth G. Rhee, Matthew L. Rizk, Nicole Calder, Marcela Nefliu, Steven J. Warrington, Michael S. Schwartz, Eric Mangin, Keith Boundy, Pratik Bhagunde, Francheska Colon-Gonzalez, Patricia Jumes, Yang Liu, Joan R. Butterton
  • Experimental Therapeutics
    In Vivo Efficacy of Relebactam (MK-7655) in Combination with Imipenem-Cilastatin in Murine Infection Models

    The World Health Organization has identified antimicrobial resistance as a global public health threat since the prevalence and spread of antibiotic resistance among bacterial pathogens worldwide are staggering. Carbapenems, such as imipenem and meropenem, have been used to treat multidrug-resistant bacteria; however, since the development of resistance to carbapenems, β-lactam antibiotics in combination with β-lactamase inhibitors (BLI...

    Mary Ann Powles, Andrew Galgoci, Andrew Misura, Lawrence Colwell, Karen H. Dingley, Wei Tang, Jin Wu, Timothy Blizzard, Mary Motyl, Katherine Young
  • Susceptibility
    In Vitro Activity of Imipenem-Relebactam against Clinical Isolates of Gram-Negative Bacilli Isolated in Hospital Laboratories in the United States as Part of the SMART 2016 Program
    James A. Karlowsky, Sibylle H. Lob, Krystyna M. Kazmierczak, Katherine Young, Mary R. Motyl, Daniel F. Sahm
  • Mechanisms of Resistance
    Relebactam Is a Potent Inhibitor of the KPC-2 β-Lactamase and Restores Imipenem Susceptibility in KPC-Producing Enterobacteriaceae
    Krisztina M. Papp-Wallace, Melissa D. Barnes, Jim Alsop, Magdalena A. Taracila, Christopher R. Bethel, Scott A. Becka, David van Duin, Barry N. Kreiswirth, Keith S. Kaye, Robert A. Bonomo
  • Mechanisms of Resistance
    Inactivation of the Pseudomonas-Derived Cephalosporinase-3 (PDC-3) by Relebactam
    Melissa D. Barnes, Christopher R. Bethel, Jim Alsop, Scott A. Becka, Joseph D. Rutter, Krisztina M. Papp-Wallace, Robert A. Bonomo
  • Experimental Therapeutics
    Exploring the Pharmacokinetic/Pharmacodynamic Relationship of Relebactam (MK-7655) in Combination with Imipenem in a Hollow-Fiber Infection Model
    Jin Wu, Fred Racine, Michael K. Wismer, Katherine Young, Donna M. Carr, Jing C. Xiao, Ravi Katwaru, Qian Si, Paul Harradine, Mary Motyl, Pratik R. Bhagunde, Matthew L. Rizk

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