The interaction of the azetidine thiazole side chain with the active site loop (ASL) 3 drives the evolution of IMP metallo-β-lactamase against tebipenem.

IMP carbapenemase metallo-β-lactamase tebipenem

Journal

Antimicrobial agents and chemotherapy
ISSN: 1098-6596
Titre abrégé: Antimicrob Agents Chemother
Pays: United States
ID NLM: 0315061

Informations de publication

Date de publication:
18 Jul 2024
Historique:
medline: 18 7 2024
pubmed: 18 7 2024
entrez: 18 7 2024
Statut: aheadofprint

Résumé

Imipenemase (IMP) metallo-β-lactamases (MBLs) hydrolyze almost all available β-lactams including carbapenems and are not inhibited by any commercially available β-lactamase inhibitor. Tebipenem (TP) pivoxil is the first orally available carbapenem and possesses a unique bicyclic azetidine thiazole moiety located at the R2 position. TP has potent

Identifiants

pubmed: 39023262
doi: 10.1128/aac.00687-24
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e0068724

Auteurs

Daisuke Ono (D)

Division of Infectious Diseases, Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Research Service, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, Ohio, USA.

Anna Cmolik (A)

Research Service, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, Ohio, USA.

Christopher R Bethel (CR)

Research Service, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, Ohio, USA.

Yoshikazu Ishii (Y)

The Center for Planetary Health and Innovation Science (PHIS), The IDEC Institute, Hiroshima University, Hiroshima, Japan.

Salvador I Drusin (SI)

Instituto de Química Rosario (IQUIR, CONICET-UNR), Rosario, Santa Fe, Argentina.
Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Santa Fe, Argentina.

Diego M Moreno (DM)

Instituto de Química Rosario (IQUIR, CONICET-UNR), Rosario, Santa Fe, Argentina.
Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Santa Fe, Argentina.

Alejandro J Vila (AJ)

Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Santa Fe, Argentina.
Laboratorio de Metaloproteínas, Instituto de Biología Molecular y Celular de Rosario (CONICET IBR -UNR), Rosario, Santa Fe, Argentina.
CWRU-Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology (Case VA CARES), Cleveland, Ohio, USA.

Robert A Bonomo (RA)

Division of Infectious Diseases, Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Research Service, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, Ohio, USA.
CWRU-Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology (Case VA CARES), Cleveland, Ohio, USA.
Departments of Pharmacology, Biochemistry, Proteomics and Bioinformatics, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Clinician Scientist Investigator, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, Ohio, USA.

Maria F Mojica (MF)

Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Research Service, Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, Ohio, USA.
CWRU-Cleveland VAMC Center for Antimicrobial Resistance and Epidemiology (Case VA CARES), Cleveland, Ohio, USA.
Grupo de Investigación en Resistencia Antimicrobiana y Epidemiología Hospitalaria, Universidad El Bosque, Bogotá, Colombia.

Classifications MeSH