Corpus ID: 39597009

Metallo-beta-lactamases: the quiet before the storm?

  title={Metallo-beta-lactamases: the quiet before the storm?},
  author={T. Walsh and M. Toleman and L. Poirel and P. Nordmann},
  journal={Clinical microbiology reviews},
  volume={18 2},
The ascendancy of metallo-beta-lactamases within the clinical sector, while not ubiquitous, has nonetheless been dramatic; some reports indicate that nearly 30% of imipenem-resistant Pseudomonas aeruginosa strains possess a metallo-beta-lactamase. Acquisition of a metallo-beta-lactamase gene will invariably mediate broad-spectrum beta-lactam resistance in P. aeruginosa, but the level of in vitro resistance in Acinetobacter spp. and Enterobacteriaceae is less dependable. Their clinical… Expand
Inhibition of metallo-β-lactamases by pyridine monothiocarboxylic acid analogs
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Rapidly emerging novel metallo beta lactamase--New Delhi metallo beta lactamase-1 (NDM-1)--is it a misnomer.
These are the antibiotics in reserve used presently for the multidrug (fluoroquinolones, aminoglycosides and cephalosporins) resistance bacteria, but of late these bacteria have also been found producing metalo β-lactamases 3 and have become resistant to even this group of antibiotics and are referred to as superbugs. Expand
Epidemiology and genetics of VIM-type metallo-β-lactamases in Gram-negative bacilli.
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Carbapenem resistance in Acinetobacter baumannii: mechanisms and epidemiology.
  • L. Poirel, P. Nordmann
  • Biology, Medicine
  • Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases
  • 2006
In addition to beta-lactamases, carbapenem resistance in A. baumannii may also result from porin or penicillin-binding protein modifications, and several porins, including the 33-kDa CarO protein, that constitute a pore channel for influx ofcarbapenems, might be involved in carbapanem resistance. Expand
Design and synthesis of metallo-β-lactamase inhibitors
A combination of structure-based drug design, chemical synthesis and biological evaluation has been used to rationally identify novel inhibitors of VIM-2, IMP-1, NDM-1 and SPM-1 which have also been co administered with a current β-lactam antibiotic and been found to re-sensitise the bacteria to the antibiotic. Expand
Prevalence of metallo-beta-lactamase genes blaVIM-1 and blaSPM-1 in Pseudomonas aeruginosa Clinical Isolates in Isfahan, Iran
It is found that none of MBL-producing isolates in this study carries blaVIM or blaSPM-1 genes; therefore, other genes in MBLs family should be investigated. Expand
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The aims of the current review are to define and categorize the different families of carbapenemases, and to overview the main lines of their spread across different bacterial groups. Expand
Contributions of IMP-10 Metallo-β-Lactamase, the Outer Membrane Barrier and the MexAB-OprM Efflux System to High-Level Carbapenem Resistance in Pseudomonas aeruginosa
The acquired IMP-10 MBL is a crucial factor in the high-level resistance to carbapenems in P. aeruginosa clinical isolates, while the outer membrane barrier and the MexAB-OprM efflux system play a basic and minor role, respectively. Expand
Therapeutic Options for Metallo-β-Lactamase-Producing Enterobacterales
There are several promising MBL inhibitors in the pipeline, which may further improve the treatment of MBL-producing Enterobacterales and currently has the most clinical data of any available antibiotic to support its use. Expand