CTX-M-190, a Novel β-Lactamase Resistant to Tazobactam and Sulbactam, Identified in an Escherichia coli Clinical Isolate
Author(s) -
Zhen Shen,
Baixing Ding,
Yingmin Bi,
Shi Wu,
Su Xu,
Xiaogang Xu,
Qinglan Guo,
Minggui Wang
Publication year - 2016
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.01848-16
Subject(s) - sulbactam , escherichia coli , tazobactam , cefotaxime , microbiology and biotechnology , biology , plasmid , antibiotics , dna , antibiotic resistance , gene , biochemistry , imipenem
A novel β-lactamase, CTX-M-190, derived from CTX-M-55 by a single substitution of Ser for Thr at position 133 (Ser133Thr), was identified in a natural Escherichia coli clinical isolate. CTX-M-190 exhibited potent hydrolytic activity against cefotaxime, with a k cat /K m ratio of 14.5 μM -1 s -1 , and was highly resistant to inhibition by the β-lactamase inhibitors tazobactam and sulbactam, whose 50% inhibitory concentrations were 77- and 55-fold higher, respectively, for CTX-M-190 than for CTX-M-55. bla CTX-M-190 was located within the genetic platform ISEcp1-bla CTX-M -orf477, which was harbored by a 70-kb IncI1 plasmid.
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