Decreased susceptibility to cefepime in a clinical strain of Escherichia coli related to plasmid- and integron-encoded OXA-30 beta-lactamase.

@article{Dubois2003DecreasedST,
  title={Decreased susceptibility to cefepime in a clinical strain of Escherichia coli related to plasmid- and integron-encoded OXA-30 beta-lactamase.},
  author={V{\'e}ronique Dubois and Corinne Arpin and Claudine Quentin and Jeannette Texier-Maugein and Laurent Poirel and Patrice L. Nordmann},
  journal={Antimicrobial agents and chemotherapy},
  year={2003},
  volume={47 7},
  pages={2380-1}
}
The most frequent extended-spectrum -lactamases (ESBLs) in members of the family Enterobacteriaceae are derived from the clavulanic acid-inhibited Ambler class A enzymes TEM-1/ TEM-2 and SHV-1, which may hydrolyze ceftazidime and cefepime (4, 5). The Ambler class B enzymes have the broadest hydrolysis profiles, including cefepime and ceftazidime (8), whereas several OXA-derived ESBLs (Ambler class D) usually hydrolyze more ceftazidime than cefepime (3). However, cefepime resistance combined… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 16 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 11 references

OXA-type -lactamases. Curr. Pharm. 8 8 Des. 5:865–879

  • T. Naas, P. Nordmann
  • 1999

Similar Papers

Loading similar papers…