Reduced susceptibility to aztreonam-avibactam conferred by acquired AmpC-type β-lactamases in PBP3-modified Escherichia coli
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I-Site ULNE
Région Hauts-de-France
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Springer Science and Business Media LLC
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https://link.springer.com/content/pdf/10.1007/s10096-024-04769-z.pdf
Reference20 articles.
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2. Brogden RN, Heel RC (1986) Aztreonam. Drugs 31:96–130. https://doi.org/10.2165/00003495-198631020-00002
3. Philippon A, Arlet G, Jacoby GA (2002) Plasmid-determined AmpC-type β-lactamases. Antimicrob Agents Chemother 46:1–11. https://doi.org/10.1128/AAC.46.1.1-11.2002
4. Livermore DM, Mushtaq S, Vickers A, Woodford N (2023) Activity of aztreonam/avibactam against metallo-β-lactamase-producing Enterobacterales from the UK: impact of penicillin-binding protein-3 inserts and CMY-42 β-lactamase in Escherichia coli. Int J Antimicrob Agents 61:106776. https://doi.org/10.1016/j.ijantimicag.2023.106776
5. Sadek M, Juhas M, Poirel L, Nordmann P (2020) Genetic features leading to reduced susceptibility to aztreonam-avibactam among metallo-β-lactamase-producing Escherichia coli isolates. Antimicrob Agents Chemother 64:e01659-e1720. https://doi.org/10.1128/AAC.01659-20
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1. Multicenter evaluation of activity of aztreonam in combination with avibactam, relebactam, and vaborbactam against metallo-β-lactamase-producing carbapenem-resistant gram-negative bacilli;Antimicrobial Agents and Chemotherapy;2024-08-19
2. Impact of extended-spectrum chromosomal AmpC (ESAC) of Escherichia coli on susceptibility to cefiderocol;Microbiology Spectrum;2024-07-02
3. Effect of modification of penicillin-binding protein 3 on susceptibility to ceftazidime-avibactam, imipenem-relebactam, meropenem-vaborbactam, aztreonam-avibactam, cefepime-taniborbactam, and cefiderocol of Escherichia coli strains producing broad-spectrum β-lactamases;Antimicrobial Agents and Chemotherapy;2024-04-03
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