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Mechanisms of Resistance

IMP-4, a Novel Metallo-β-Lactamase from Nosocomial Acinetobacter spp. Collected in Hong Kong between 1994 and 1998

Yiu-Wai Chu, Mariya Afzal-Shah, Elizabeth T. S. Houang, Marie-France I. Palepou, Donald J. Lyon, Neil Woodford, David M. Livermore
Yiu-Wai Chu
Department of Microbiology, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, New Territories, Hong Kong SAR, China, 1 and
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Mariya Afzal-Shah
Antibiotic Resistance Monitoring and Reference Laboratory, Central Public Health Laboratory, London NW9 5HT, United Kingdom 2
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Elizabeth T. S. Houang
Department of Microbiology, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, New Territories, Hong Kong SAR, China, 1 and
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Marie-France I. Palepou
Antibiotic Resistance Monitoring and Reference Laboratory, Central Public Health Laboratory, London NW9 5HT, United Kingdom 2
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Donald J. Lyon
Department of Microbiology, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, New Territories, Hong Kong SAR, China, 1 and
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Neil Woodford
Antibiotic Resistance Monitoring and Reference Laboratory, Central Public Health Laboratory, London NW9 5HT, United Kingdom 2
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David M. Livermore
Antibiotic Resistance Monitoring and Reference Laboratory, Central Public Health Laboratory, London NW9 5HT, United Kingdom 2
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DOI: 10.1128/AAC.45.3.710-714.2001
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    Fig. 1.

    Comparison of the amino acid sequences of IMP-1, IMP-2, IMP-3, and IMP-4 β-lactamases. The 18 residues that comprise the IMP-1 signal peptide (21) are shaded.

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  • Table 1.

    MICs for bla IMP-4-positive isolates of Acinetobacter spp.

    Isolate type and lab no.SampleDNA groupDate isolated (mo/yr)β-Lactamase pI(s)MIC (μg/ml)a
    IMPMEMATMPIPTZPCTXSUL
    Isolates from which bla IMP-4was sequenced
     116665Blood210/945.40.50.2516>12832>12816
     127091Blood29/967.6, 8.0b 161664>12864>1284
     74510Wound13TU5/955.7, 7.6, 8.0b >32>3232>12832>12816
     104680Blood38/985.7, 7.6, 8.0b 81632>12864>1281
    Collection of 23 bla IMP-4 positive isolates
     MIC range0.25–160.25–162–6464–2564–6432–2561–64
     MIC50 c 4832256321282
     MIC90 d 1616642566425616
    • ↵a ATM, aztreonam; CTX, cefotaxime; IMP, imipenem; MEM, meropenem; PIP, piperacillin; SUL, sulbactam; TZP, piperacillin-tazobactam (tazobactam at 4 μg/ml).

    • ↵b Enzymes with pIs of 8.0 ceased to be detectable if the gel was overlaid with 3 mM EDTA for 10 min before addition of nitrocefin.

    • ↵c MIC50, MIC at which 50% of isolates are inhibited.

    • ↵d MIC90, MIC at which 90% of isolates are inhibited.

  • Table 2.

    Kinetic properties of IMP-4 β-lactamase from isolate 74510

    SubstrateRelative Vmax(%)aKm (μM)
    Benzylpenicillin100365
    Ampicillin52575
    Piperacillin8144
    Carbenicillin621,000
    Oxacillin307420
    Cephaloridine8132
    Cephalothin11171
    Cefuroxime4652
    Cefotaxime918
    Ceftazidime728
    Imipenem5342
    Meropenem812
    Aztreonam0.001Not measured
    • ↵a Based on a predicted molecular mass of 27,087 and a purity of 80%; based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, ak cat of 27.5 s−1 was estimated for IMP-4 against benzylpenicillin.

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IMP-4, a Novel Metallo-β-Lactamase from Nosocomial Acinetobacter spp. Collected in Hong Kong between 1994 and 1998
Yiu-Wai Chu, Mariya Afzal-Shah, Elizabeth T. S. Houang, Marie-France I. Palepou, Donald J. Lyon, Neil Woodford, David M. Livermore
Antimicrobial Agents and Chemotherapy Mar 2001, 45 (3) 710-714; DOI: 10.1128/AAC.45.3.710-714.2001

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IMP-4, a Novel Metallo-β-Lactamase from Nosocomial Acinetobacter spp. Collected in Hong Kong between 1994 and 1998
Yiu-Wai Chu, Mariya Afzal-Shah, Elizabeth T. S. Houang, Marie-France I. Palepou, Donald J. Lyon, Neil Woodford, David M. Livermore
Antimicrobial Agents and Chemotherapy Mar 2001, 45 (3) 710-714; DOI: 10.1128/AAC.45.3.710-714.2001
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