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β-lactamase

  • Open Access
    The Class A Carbapenemases BKC-1 and GPC-1 Both Originate from the Bacterial Genus <em>Shinella</em>
    Mechanisms of Resistance
    The Class A Carbapenemases BKC-1 and GPC-1 Both Originate from the Bacterial Genus Shinella

    Comparative genomics identified the environmental bacterial genus Shinella as the most likely origin of the class A carbapenemases BKC-1 and GPC-1. Available sequences and PCR analyses of additional Shinella species revealed homologous β-lactamases showing up to 85.4% and 93.3% amino acid identity to both enzymes, respectively. The genes conferred resistance to β-lactams once expressed in...

    Nicolas Kieffer, Stefan Ebmeyer, D. G. Joakim Larsson
  • Resistance to Ceftazidime/Avibactam plus Meropenem/Vaborbactam When Both Are Used Together Is Achieved in Four Steps in Metallo-β-Lactamase-Negative <span class="named-content genus-species" id="named-content-1">Klebsiella pneumoniae</span>
    Mechanisms of Resistance
    Resistance to Ceftazidime/Avibactam plus Meropenem/Vaborbactam When Both Are Used Together Is Achieved in Four Steps in Metallo-β-Lactamase-Negative Klebsiella pneumoniae

    Serine β-lactamases are dominant causes of β-lactam resistance in Klebsiella pneumoniae isolates. Recently, this has driven clinical deployment of the β-lactam–β-lactamase inhibitor pairs ceftazidime/avibactam and meropenem/vaborbactam. We show that four steps, i.e., ompK36 and ramR mutation plus carriage of OXA-232 and KPC-3-D178Y variant β-...

    Punyawee Dulyayangkul, Edward J. A. Douglas, Filip Lastovka, Matthew B. Avison
  • 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
  • Proteomic Changes of <span class="named-content genus-species" id="named-content-1">Klebsiella pneumoniae</span> in Response to Colistin Treatment and <em>crrB</em> Mutation-Mediated Colistin Resistance
    Mechanisms of Resistance
    Proteomic Changes of Klebsiella pneumoniae in Response to Colistin Treatment and crrB Mutation-Mediated Colistin Resistance

    Polymyxins are increasingly used as the critical last-resort therapeutic options for multidrug-resistant Gram-negative bacteria. Unfortunately, polymyxin resistance has increased gradually over the past few years. Although studies on polymyxin mechanisms are expanding, systemwide analyses of the underlying mechanism for polymyxin resistance and stress response are still lacking. To understand how...

    Lang Sun, Pernille Kronholm Rasmussen, Yinlei Bai, Xiulan Chen, Tanxi Cai, Jifeng Wang, Xiaojing Guo, Zhensheng Xie, Xiang Ding, Lili Niu, Nali Zhu, Xuefu You, Finn Kirpekar, Fuquan Yang
  • Role of Arginine 214 in the Substrate Specificity of OXA-48
    Mechanisms of Resistance
    Role of Arginine 214 in the Substrate Specificity of OXA-48

    Increasing numbers of variants of the carbapenem-hydrolyzing class D β-lactamase OXA-48 are identified in Enterobacterales worldwide. Among them, OXA-181 and OXA-232 are of particular interest, as they differ from each other by a single amino acid substitution at position 214 (R in OXA-181 and S in OXA-232) that results in reduced carbapenem-hydrolyzing activity for OXA-232. To investigate the role of amino acid position 214 (...

    Saoussen Oueslati, Pascal Retailleau, Ludovic Marchini, Camille Berthault, Laurent Dortet, Rémy A. Bonnin, Bogdan I. Iorga, Thierry Naas
  • 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
  • Regulation and Anaerobic Function of the <em>Clostridioides difficile</em> β-Lactamase
    Mechanisms of Resistance
    Regulation and Anaerobic Function of the Clostridioides difficile β-Lactamase

    Clostridioides difficile causes severe antibiotic-associated diarrhea and colitis. C. difficile is an anaerobic, Gram-positive sporeformer that is highly resistant to β-lactams, the most commonly prescribed antibiotics. The resistance of...

    Brindar K. Sandhu, Adrianne N. Edwards, Sarah E. Anderson, Emily C. Woods, Shonna M. McBride
  • Acquisition of Class C β-Lactamase PAC-1 by Sequence Type 644 Strains of <span class="named-content genus-species" id="named-content-1">Pseudomonas aeruginosa</span>
    Mechanisms of Resistance
    Acquisition of Class C β-Lactamase PAC-1 by Sequence Type 644 Strains of Pseudomonas aeruginosa

    Four sequence type 664 (ST664) (serotype O:5) strains of Pseudomonas aeruginosa that were highly resistant to antibiotics, including ceftolozane-tazobactam and ceftazidime-avibactam, but were susceptible to colistin were found to harbor the gene encoding the rare class C β-lactamase PAC-1 on a chromosomally located Tn1721-like transposon. The bla...

    Maxime Bour, Damien Fournier, Thomas Jové, Armelle Pouzol, Guillaume Miltgen, Frédéric Janvier, Katy Jeannot, Patrick Plésiat
  • Structural Insights into the Inhibition of the Extended-Spectrum β-Lactamase PER-2 by Avibactam
    Mechanisms of Resistance
    Structural Insights into the Inhibition of the Extended-Spectrum β-Lactamase PER-2 by Avibactam

    The diazabicyclooctane (DBO) avibactam (AVI) reversibly inactivates most serine-β-lactamases.

    Melina Ruggiero, Krisztina M. Papp-Wallace, Florencia Brunetti, Melissa D. Barnes, Robert A. Bonomo, Gabriel Gutkind, Sebastián Klinke, Pablo Power
  • Genomic Analysis Identifies Novel <span class="named-content genus-species" id="named-content-1">Pseudomonas aeruginosa</span> Resistance Genes under Selection during Inhaled Aztreonam Therapy <em>In Vivo</em>
    Mechanisms of Resistance
    Genomic Analysis Identifies Novel Pseudomonas aeruginosa Resistance Genes under Selection during Inhaled Aztreonam Therapy In Vivo

    Inhaled aztreonam is increasingly used for chronic Pseudomonas aeruginosa suppression in patients with cystic fibrosis (CF), but the potential for that organism to evolve aztreonam resistance remains incompletely explored. Here, we performed genomic analysis of clonally related pre- and posttreatment CF clinical isolate pairs to identify genes that are under positive...

    Kathryn McLean, Duankun Lee, Elizabeth A. Holmes, Kelsi Penewit, Adam Waalkes, Mingxin Ren, Samuel A. Lee, Joseph Gasper, Colin Manoil, Stephen J. Salipante

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