Ceftazidime-Avibactam Resistance Mediated by the N 346 Y Substitution in Various AmpC β-Lactamases-Reference-Cited by-同舟云学术

Ceftazidime-Avibactam Resistance Mediated by the N 346 Y Substitution in Various AmpC β-Lactamases

Published:2020-05-21 Issue:6 Volume:64 Page:
ISSN:0066-4804
Container-title:Antimicrobial Agents and Chemotherapy
language:en
Short-container-title:Antimicrob Agents Chemother

Author:

Compain Fabrice¹²,Debray Agathe¹,Adjadj Pauline¹,Dorchêne Delphine¹,Arthur Michel¹

Affiliation:

1. INSERM, Sorbonne Université, Université de Paris, Centre de Recherche des Cordeliers, Paris, France

2. Assistance Publique-Hôpitaux de Paris, Centre Université de Paris, Service de microbiologie, Hôpital Européen Georges Pompidou, Paris, France

Abstract

Chromosomal and plasmid-borne AmpC cephalosporinases are a major resistance mechanism to β-lactams in Enterobacteriaceae and Pseudomonas aeruginosa . The new β-lactamase inhibitor avibactam effectively inhibits class C enzymes and can fully restore ceftazidime susceptibility. The conserved amino acid residue Asn 346 of AmpC cephalosporinases directly interacts with the avibactam sulfonate. Disruption of this interaction caused by the N 346 Y amino acid substitution in Citrobacter freundii AmpC was previously shown to confer resistance to the ceftazidime-avibactam combination (CAZ-AVI).

Funder

Assistance Publique Hôpitaux de Paris

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Link

https://journals.asm.org/doi/pdf/10.1128/AAC.02311-19

Reference18 articles.

1. Past and Present Perspectives on β-Lactamases

2. Contribution of extended-spectrum AmpC (ESAC) β-lactamases to carbapenem resistance in Escherichia coli

3. Extended-Spectrum Cephalosporinases in Pseudomonas aeruginosa