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J Med Microbiol 58 (2009), 811-815; DOI: 10.1099/jmm.0.006007-0
© 2009 Society for General Microbiology
ISSN 0022-2615

Characterization of two plasmid-encoded cefotaximases found in clinical Escherichia coli isolates: CTX-M-65 and a novel enzyme, CTX-M-87

Jun Yin1,{dagger}, Jun Cheng1,{dagger}, Zhen Sun1, Ying Ye1, Yu-Feng Gao1, Jia-Bin Li1,2 and Xue-Jun Zhang2,3

1 Department of Infectious Diseases, First Affiliated Hospital of Anhui Medical University, Hefei, Anhui 230022, PR China

2 Clinical Medicine Post-Doctorate Position of Anhui Medical University, Hefei, Anhui 230032, PR China

3 Institute of Dermatology, Anhui Medical University, Hefei, Anhui 230032, PR China

Correspondence
Jia-Bin Li
lijiabin948{at}vip.sohu.com
Xue-Jun Zhang
ayzxj{at}vip.sina.com

Received August 19, 2008
Accepted March 3, 2009

Three clinical strains of Escherichia coli (p168, p517 and p667) were collected in 2006 from three hospitals in Anhui Province (China). PCR and DNA sequencing revealed that E. coli p168 carried a novel extended-spectrum β-lactamase (ESBL), which was designated CTX-M-87. The extended-spectrum β-lactamase which was carried by E. coli p517 and E. coli p667 was previously named CTX-M-65. The deduced amino acid sequence of CTX-M-87, with pI 9.1, differed from that of CTX-M-14 by the substitutions Ala77->Val and Pro167->Leu. Like CTX-M-14, CTX-M-87 had a more potent hydrolytic activity against cefotaxime than against ceftazidime and had high affinity for cefuroxime and cefotaxime. These data show that mutations at position 167 in CTX-M do not always affect catalytic activity and substrate preference.

Abbreviations: ESBL, extended-spectrum β-lactamase.

{dagger}These authors contributed equally to this work.

The GenBank/EMBL/DDBJ accession number for the CTX-M-87 gene sequence is EU545409.






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