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. 2015 Nov;59(11):7090-3.
doi: 10.1128/AAC.01611-15. Epub 2015 Aug 17.

IMP-51, a novel IMP-type metallo-β-lactamase with increased doripenem- and meropenem-hydrolyzing activities, in a carbapenem-resistant Pseudomonas aeruginosa clinical isolate

Tatsuya Tada  1 , Pham Hong Nhung  2 , Tohru Miyoshi-Akiyama  3 , Kayo Shimada  1 , Doan Mai Phuong  4 , Nguyen Quoc Anh  4 , Norio Ohmagari  5 , Teruo Kirikae  6
Affiliations

IMP-51, a novel IMP-type metallo-β-lactamase with increased doripenem- and meropenem-hydrolyzing activities, in a carbapenem-resistant Pseudomonas aeruginosa clinical isolate

Tatsuya Tada et al. Antimicrob Agents Chemother. 2015 Nov.

Abstract

A meropenem-resistant Pseudomonas aeruginosa isolate was obtained from a patient in a medical setting in Hanoi, Vietnam. The isolate was found to have a novel IMP-type metallo-β-lactamase, IMP-51, which differed from IMP-7 by an amino acid substitution (Ser262Gly). Escherichia coli expressing blaIMP-51 showed greater resistance to cefoxitin, meropenem, and moxalactam than E. coli expressing blaIMP-7. The amino acid residue at position 262 was located near the active site, proximal to the H263 Zn(II) ligand.

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Figures

FIG 1
FIG 1
Dendrogram of 45 IMP-type MBLs for comparison with IMP-51. The dendrogram was calculated with the Clustal W2 program. Branch lengths correspond to the number of amino acid exchanges for IMP-type enzymes.
See this image and copyright information in PMC

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