ESAC beta-lactamases have increased catalytic efficiencies toward extended-spectrum cephalosporins and to a lesser extent toward imipenem as compared with the wild-type cephalosporinases. We show here that ESAC expression associated with the loss of both OmpC and OmpF porins conferred in Escherichia coli a high level of resistance to ertapenem and reduced the susceptibility to imipenem. On the contrary, ESAC expressed in the OmpC- or OmpF-deficient E. coli strains or narrow-spectrum cephalosporinase expressed in the OmpC-and OmpF-deficient strain do not confer reduced susceptibility to any of the carbapenems. The production of ESAC beta-lactamase in favorable E. coli background may represent an additional mechanism of resistance to ertapenem.
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http://dx.doi.org/10.1111/j.1574-6968.2008.01126.x | DOI Listing |
Infect Genet Evol
December 2024
Department of Clinical Microbiology, Christian Medical College, Vellore 632004, India. Electronic address:
Microbiol Spectr
July 2024
Medical and Molecular Microbiology, Faculty of Science and Medicine, University of Fribourg, Fribourg, Switzerland.
Unlabelled: The impact of chromosomally encoded wild-type or extended-spectrum (ESAC) AmpC β-lactamases of on susceptibility to ceftazidime, cefepime, and cefiderocol was evaluated in different genetic backgrounds, including wild-type, PBP3-modified, and porin-deficient strains. Recombinant strains possessing the different backgrounds and producing variable ESACs were evaluated. Although ESAC enzymes conferred resistance to ceftazidime and decreased susceptibility to cefepime as expected, we showed here that cefiderocol was also a substrate of ESAC enzymes.
View Article and Find Full Text PDFAntibiotics (Basel)
March 2023
Department of Life Sciences, Università di Modena e Reggio Emilia, Via Campi 103, 41125 Modena, Italy.
is a Gram-negative organism listed as an urgent threat pathogen by the World Health Organization (WHO). Carbapenem-resistant (CRAB), especially, present therapeutic challenges due to complex mechanisms of resistance to -lactams. One of the most important mechanisms is the production of -lactamase enzymes capable of hydrolyzing -lactam antibiotics.
View Article and Find Full Text PDFAntibiotics (Basel)
January 2023
Department of Pharmaceutical and Clinical Sciences, College of Pharmacy & Health Sciences, Campbell University, Buies Creek, NC 27506, USA.
The genus (family ) causes a wide spectrum of acute infections in immunocompromised hosts, from pneumonia and bacteremia to oral ulcers and dialysis-related peritonitis. While infections are reported infrequently in the literature, documented clinical cases of this emerging opportunistic human pathogen have occurred worldwide. has clinical significance and exhibits antimicrobial drug resistance.
View Article and Find Full Text PDFClin Microbiol Rev
September 2022
Université Paris-Saclay, CNRS, Institut de Chimie des Substances Naturelles, Gif-sur-Yvette, France.
Class C β-lactamases or cephalosporinases can be classified into two functional groups (1, 1e) with considerable molecular variability (≤20% sequence identity). These enzymes are mostly encoded by chromosomal and inducible genes and are widespread among bacteria, including Proteobacteria in particular. Molecular identification is based principally on three catalytic motifs (SXSK, YXN, KTG), but more than 70 conserved amino-acid residues (≥90%) have been identified, many close to these catalytic motifs.
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