title: beta-Lactamases responsible for resistance to expanded-spectrum cephalosporins in Klebsiella pneumoniae, Escherichia coli, and Proteus mirabilis isolates recovered in South Africa.
abstract: Although resistance to the expanded-spectrum cephalosporins among members of the family Enterobacteriaceae lacking inducible beta-lactamases occurs virtually worldwide, little is known about this problem among isolates recovered in South Africa. Isolates of Klebsiella pneumoniae, Escherichia coli, and Proteus mirabilis resistant to expanded-spectrum cephalosporins recovered from patients in various parts of South Africa over a 3-month period were investigated for extended-spectrum beta-lactamase production. Antibiotic susceptibility was determined by standard disk diffusion and agar dilution procedures. Production of extended-spectrum beta-lactamases was evaluated by using the double-disk test, and the beta-lactamases were characterized by spectrophotometric hydrolysis assays and an isoelectric focusing overlay technique which simultaneously determined isoelectric points and general substrate or inhibitor characteristics. DNA amplification and sequencing were performed to confirm the identities of these enzymes. The P. mirabilis and E. coli isolates were found to produce TEM-26-type, SHV-2, and SHV-5 extended-spectrum beta-lactamases. An AmpC-related enzyme which had a pI of 8.0 and which conferred resistance to cefoxitin as well as the expanded-spectrum cephalosporins was found in a strain of K. pneumoniae. This is the first study which has identified organisms producing different extended-spectrum beta-lactamases from South Africa and the first report describing strains of P. mirabilis producing a TEM-26-type enzyme. The variety of extended-spectrum beta-lactamases found among members of the family Enterobacteriaceae isolated from major medical centers in South Africa is troubling and adds to the growing list of countries where these enzymes pose a serious problem for antimicrobial therapy.
authors.affiliation: Department of Medical Microbiology and Immunology, Creighton University School of Medicine, Omaha, Nebraska 68178, USA.
authors.forename: J D
authors.initials: JD
authors.lastname: Pitout
authors.forename: K S
authors.initials: KS
authors.lastname: Thomson
authors.forename: N D
authors.initials: ND
authors.lastname: Hanson
authors.forename: A F
authors.initials: AF
authors.lastname: Ehrhardt
authors.forename: E S
authors.initials: ES
authors.lastname: Moland
authors.forename: C C
authors.initials: CC
authors.lastname: Sanders
mesh_terms: D018550:Cephalosporin Resistance / Q000235:genetics*; D002511:Cephalosporins / Q000494:pharmacology*; D004269:DNA, Bacterial / Q000235:genetics*; D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D006801:Humans; D007711:Klebsiella pneumoniae / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D010641:Phenotype; D011513:Proteus mirabilis / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D013019:South Africa; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000235:genetics*
chemical_list: D002511:Cephalosporins; D004269:DNA, Bacterial; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases