Extended-spectrum cephalosporinases: structure, detection and epidemiology.
Extended-spectrum AmpC beta-lactamases of Enterobacteriaceae, which are chromosomally or plasmid-encoded, possess structural modifications in the vicinity of the active site compared with their progenitors. They display an increased catalytic efficiency against extended-spectrum beta-lactams, such as ceftazidime, cefotaxime, cefepime, cefpirome and, in some cases, also against imipenem. An overview of the molecular and biochemical characterization of this recently identified mechanism of resistance to beta-lactams is provided as well as its prevalence and possible clinical significance.
Nordmann
Patrice
P
Service de Bactériologie-Virologie, Hôpital de Bicêtre, Le Kremlin-Bicêtre, France. nordmann.patrice@bct.aphp.fr
Mammeri
Hedi
H
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002510:Cephalosporinase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004755:Enterobacteriaceae / Q000187:drug effects / Q000201:enzymology / Q000235:genetics; D004756:Enterobacteriaceae Infections / Q000175:diagnosis / Q000453:epidemiology; D008958:Models, Molecular; D015394:Molecular Structure; D011485:Protein Binding; D017433:Protein Structure, Secondary; D018440:beta-Lactam Resistance / Q000235:genetics; D001618:beta-Lactamases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D047090:beta-Lactams / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology
D001426:Bacterial Proteins; D047090:beta-Lactams; D002510:Cephalosporinase; C048795:AmpC beta-lactamases; D001618:beta-Lactamases