Microbiology SpectrumCarbapenem-resistant Enterobacterales represent a major health threat and have few approved therapeutic options. Enterobacterales isolates were collected from hospitalized inpatients from 49 sites in six European countries (1 January–31 December 2020 ...
Anne Santerre Henriksen +7 more
doaj +3 more sources
Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to β-lactamase inhibitors [PDF]
FEMS Microbiology Letters, 1994 The clinical isolate Escherichia coli PEY was highly resistant to amoxycillin, ticarcillin and piperacillin associated to beta-lactamase inhibitors such as clavulanic acid, sulbactam, tazobactam and brobactam but susceptible to cephalosporins, aztreonam and imipenem.
T, Brun +6 more
openaire +2 more sources
Substitution of Met-69 by Ala or Gly in TEM-1 β-lactamase confer an increased susceptibility to clavulanic acid and other inhibitors [PDF]
FEMS Microbiology Letters, 2002 In some inhibitor-resistant TEM-derived beta-lactamases, Met-69 is substituted by Leu, Ile or Val. Residue 69 is located in a region of strong structural constraints, at the beginning of H2 alpha-helix, and in the vicinity of B3 and B4 beta-strands.
Stéphanie, Madec +6 more
openaire +2 more sources
Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance inEscherichia coliexpressing IMP-1 [PDF]
FEMS Microbiology Letters, 2005 IMP-1 metallo-beta-lactamase is a zinc metalloenzyme that confers antibiotic resistance to bacteria through the hydrolysis of beta-lactam antibiotics. Pathogens that express the enzyme show reduced susceptibility to carbapenems, such as meropenem and imipenem.
Joseph G, Moloughney +2 more
openaire +2 more sources
Substitution of Arg-244 by Cys or Ser in SHV-1 and SHV-5 β-lactamases confers resistance to mechanism-based inhibitors and reduces catalytic efficiency of the enzymes [PDF]
FEMS Microbiology Letters, 1998 The conserved residue Arg-244 was substituted by the smaller uncharged amino acids Cys and Ser in SHV-1 and SHV-5 beta-lactamases by a PCR-based site-specific mutagenesis procedure. The mutant beta-lactamases displayed decreased susceptibility to clavulanate and, to a lesser extent, to tazobactam and sulbactam.
Giakkoupi, P +3 more
openaire +3 more sources
Journal of Global Antimicrobial Resistance, 2020 Objectives: The aim of this study was to correlate the results of a modified susceptibility testing method with outcomes of ceftazidime/avibactam (CAZ/AVI) therapy. Methods: Two bloodstream K.
Andrei Zidaru +6 more
doaj +1 more source
PLoS ONE, 2021 β-lactam antibiotics are the most widely used antimicrobial agents since the discovery of benzylpenicillin in the 1920s. Unfortunately, these life-saving antibiotics are vulnerable to inactivation by continuously evolving β-lactamase enzymes that are ...
Nousheen Parvaiz +4 more
doaj +1 more source
The Mechanisms of Catalysis by Metallo β-Lactamases [PDF]
, 2008 Class B β-lactamases or metallo-β-lactamases (MBLs) require zinc ions to catalyse the hydrolysis of β-lactam antibiotics such as penicillins, cephalosporins, carbapenems, and cephamycins.
Michael I. Page +3 more
core +3 more sources
European Journal of Medicinal Chemistry Reports, 2023 The β-lactamase enzyme is a leading cause of drug resistance developed by bacteria. The combination of β-lactam (BL) antibiotics with an appropriate β-lactamase inhibitor (BLI) is a fundamental approach used to circumvent the problem of β-lactamase ...
Harshal S. Oman +8 more
doaj +1 more source
Fluoroquinolones versus β-Lactam/β-Lactamase Inhibitors in Outpatients with Chronic Obstructive Pulmonary Disease and Pneumonia: A Nationwide Population-Based Study. [PDF]
PLoS ONE, 2015 Studies on the association between antibiotic treatment and outcomes in outpatients with chronic obstructive pulmonary disease (COPD) and pneumonia are scarce.
Kuan-Yin Lin +4 more
doaj +1 more source