z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom