Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution [PDF]
The production of β-lactamase enzymes is one of the most distributed resistance mechanisms towards β-lactam antibiotics. Metallo-β-lactamases constitute a worrisome group of these kinds of enzymes, since they present a broad spectrum profile, being able
María-Rocío Meini +2 more
doaj +5 more sources
Rapid Typing of Extended-Spectrum β-Lactamase (ESBL)- and Metallo-β-Lactamase (MBL)-Producing Enterobacterales Using Fourier Transform Infrared (FT-IR) Spectroscopy. [PDF]
Clinical isolates of Klebsiella pneumoniae and Enterobacter cloacae complex were analyzed using FT‐IR spectroscopy and genotyping methods. High concordance was observed, demonstrating the potential of FT‐IR spectroscopy as a rapid screening tool.
Kawamoto Y +9 more
europepmc +2 more sources
The flavonoid galangin inhibits the L1 metallo-β-lactamase fromStenotrophomonas maltophilia [PDF]
The flavonoid galangin inhibits the partially purified metallo-beta-lactamase from Stenotrophomonas maltophilia. The effect was not reversed by the addition of ZnCl(2) suggesting that the inhibitory effect is not related to metal chelation. The flavonoid quercetin also has some inhibitory effect against the enzyme.
Brian J, Denny +2 more
openaire +2 more sources
Isolation and partial purification of a carbapenem-hydrolysing metallo-β-lactamase fromPseudomonas cepacia [PDF]
A metallo-beta-lactamase has been isolated from a clinical strain of Pseudomonas cepacia and partially purified using Cibacron blue F3GA coupled agarose. The resulting preparation showed a single band of beta-lactamase activity (pI 8.45) after analytical isoelectric focusing.
I A, Baxter, P A, Lambert
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Inhibition of IMP-1 metallo-β-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives [PDF]
IMP-1 metallo-beta-lactamase is a transferable carbapenem-hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and Klebsiella pneumoniae. Bacteria that express IMP-1 show significantly reduced sensitivity to carbapenems and other beta-lactam antibiotics.
G G, Hammond +11 more
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IntroductionCarbapenemase-producing Enterobacteriales (CPE) are a major health threat worldwide, and therefore the development of rapid detection methods is needed.
Xiaopeng Jing +8 more
doaj +1 more source
Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo β-lactamase [PDF]
The roles of lysine at position 161 and asparagine at position 167 in IMP-1 metallo beta-lactamase were studied by site-directed mutagenesis. These residues are highly conserved in metallo beta-lactamases and are thought to be present in the active-site cavity.
S, Haruta +3 more
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Draft Genome Sequences of Four NDM-1-Producing Klebsiella pneumoniae Strains from a Health Care Facility in Northern California. [PDF]
We report the draft genome sequences of Klebsiella pneumoniae strains from four patients at a northern California health care facility. All strains contained the New Delhi metallo-β-lactamase (NDM1) carbapenemase with extended antibiotic resistance ...
Chaturvedi, Vishnu +4 more
core +1 more source
Pseudomonas aeruginosa is a frequent nosocomial pathogen that causes severe disease in many clinical and community settings. The objective of this paper was to isolate Pseudomonas aeruginosa from clinical samples and to investigate the occurrence of ...
O.C. Adekunle +3 more
doaj +1 more source
Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance inEscherichia coliexpressing IMP-1 [PDF]
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

