Objectives: To characterize CTX-M-12 extended-spectrum β-lactamase (ESBL) produced by clinical Escherichia coli isolates and to investigate its genetic environment. Methods: Antimicrobial susceptibilities were determined by disc diffusion and agar dilution methods, and the double-disc synergy test was carried out. Detection of genes encoding class A β-lactamases was performed by PCR amplification, and the genetic environments of the bla CTX-M-12 genes were investigated by PCR and sequencing of the regions surrounding the genes. Kinetic parameters were determined from purified CTX-M-12. Results: Sequence data for the CTX-M-1 cluster from three clinical E. coli isolates indicated the presence of CTX-M-12. An IS Ecp1 insertion sequence was located 49 bp upstream of bla CTX-M-12 in all three E. coli isolates. CTX-M-12 had a more potent hydrolytic activity against cefotaxime than against ceftazidime and was encoded on a self-transferable ∼18 kbp plasmid. Conclusions: This work shows that CTX-M-12, which confers high-level resistance to cefotaxime but not to ceftazidime, has emerged in Korea. The blaCTX-M-12 gene was associated with an upstream IS Ecp1 insertion sequence.
Bibliographical noteFunding Information:
This work was supported by a research grant from the Korea Food and Drug Administration (06042HangNaeMae129).
All Science Journal Classification (ASJC) codes
- Microbiology (medical)
- Infectious Diseases
- Pharmacology (medical)