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Mechanisms of Resistance

Novel OXA-10-Derived Extended-Spectrum β-Lactamases Selected In Vivo or In Vitro

P. Mugnier, I. Casin, A. T. Bouthors, E. Collatz
P. Mugnier
Laboratoire de Recherche Moléculaire sur les Antibiotiques, UFR Broussais-Hôtel Dieu and UFR Pitié-Salpêtrière, Université Paris VI, and
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I. Casin
Laboratoire de Recherche Moléculaire sur les Antibiotiques, UFR Broussais-Hôtel Dieu and UFR Pitié-Salpêtrière, Université Paris VI, and
Laboratoire de Bactériologie, Hôpital Saint-Louis, UniversitéParis VII, Paris, France
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A. T. Bouthors
Laboratoire de Recherche Moléculaire sur les Antibiotiques, UFR Broussais-Hôtel Dieu and UFR Pitié-Salpêtrière, Université Paris VI, and
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E. Collatz
Laboratoire de Recherche Moléculaire sur les Antibiotiques, UFR Broussais-Hôtel Dieu and UFR Pitié-Salpêtrière, Université Paris VI, and
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DOI: 10.1128/AAC.42.12.3113
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  • Fig. 1.
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    Fig. 1.

    Amino acid differences between the β-lactamases of the OXA-10 group. Amino acid numbering is according to Huovinen et al. (13); the conserved motifs typical for class D enzymes are boxed. The amino acids shown in boldface contribute to the substrate profile, with asparagine in position 157 leading to extended-spectrum variants. The amino acids of OXA-10 that are not numbered are G20, S27, S50, D55, V89, T107, Y174, A197, E229, T230, S245, and E259; −, absence of an amino acid.

  • Fig. 2.
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    Fig. 2.

    Structure of the integron encoding the β-lactamases OXA-19 and OXA-13-1. Nucleotide sequences are identical in both clusters, except for three differences in the −35 sequences of the promoter and in the aac(6′)-Ib and theoxa genes. Amino acid numbering is from Tran Van Nhieu and Collatz (36) and Huovinen et al. (13), respectively. Arrows represent the following open reading frames:intI1, for integrase;aac(6′)-Ib, for the aminoglycoside acetyltransferases genesaac(6′)-Ib10 on pAZ310 (20) andaac(6′)-Ib9 on pAZ316;oxa, for the OXA variants indicated on the left; andqacEΔ1, for the typically truncated quaternary ammonium resistance-conferring gene associated with the 3′ conserved segment of integrons. The intI1 and qacEΔ1 genes have been only partially sequenced here (indicated in boldface). Data for pAZ309 are from reference 20, and data for pAZ310 and pAZ316 are from the present study. Boldface, differences with respect to the OXA-13-encoding plasmid pAZ309; dashed line, theoxa13-1 region that has been sequenced.

  • Fig. 3.
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    Fig. 3.

    Isoelectric focusing of extended-spectrum OXA-10-related β-lactamases. Enzymes SHV-1 (pIapp, 7.6), SHV-5 (pIapp, 8.2), OXA-13 (pIapp, 8 [18]), and OXA-10 (pIapp, 6.1) were used as pI standards. The two novel β-lactamases, OXA-13-1 and OXA-19, had estimated pIapps of 7.8 and 7.6, respectively. β-Lactamase activity was revealed by overlaying the gel with nitrocefin.

Tables

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  • Table 1.

    Strains and plasmids

    Strain or plasmidGenotype or descriptionResistance phenotypeaReference or source
    Strain
     PAe191Clinical strain ofP. aeruginosaTi Ca Ak Gm Su HgThis work
     DH5αE. coli; F′/endA1 hsdR17 (rk−mk+)supE44 thi-1 recA1 gyrA (Nalr) relA1 D(lacIZYA-argF)U169 deoR[f80 dlacD(lacZ)M15]NalNew England Biolabs
     PAO38RifRifampin-resistant derivative of P. aeruginosa PAO38Ri (MIC, >500 μg/ml)20
    Plasmid
     pHSS62.3-kb plasmid vectorKm32
     pK182.7-kb plasmid vectorKm25
     pNJR3-228-kb E. coli-P. aeruginosa shuttle vectorTc28
     pAZ30523-kbEcoRI fragment obtained from PAe191 total DNA, cloned into pHSS6; oxa19Km Ti Ca GmbThis work
     pAZ3164.0-kb HindIII fragment from pAZ305 cloned into HindIII-digested pNJR3-2;oxa19Tc Ti Ca GmbThis work
     pAZ3271,097-bp NarI-HindIII fragment from pAZ316 cloned intoAccI-HindIII-digested pK18,oxa19Km Ti CaThis work
     pAZ309pNJR3-2 derivative encoding oxa13Tc Ti Ak20
     pAZ310In vitro-selected derivative of pAZ309 selected on ceftazidime; oxa13-1Tc Ti Ca AkThis work
     pAZ3261,097-bpNarI-HindIII fragment from pAZ310 cloned intoAccI-HindIII-digested pK18;oxa13-1Km Ti CaThis work
    • ↵a Ti, ticarcilline; Ca, ceftazidime; Km, kanamicin; Ak, amikacin; Gm, gentamicin; Nal, nalidixic acid; Ri, rifampin; Su, sulfamide; Tc, tetracycline; Hg, mercuric ions.

    • ↵b Gm phenotype conferred by AAC(6′)-Ib9 with Ser at position 119.

  • Table 2.

    MICs of different β-lactams for PAe191 and OXA13-1, OXA-19- and OXA-13-producing transformants

    Antibiotic + inhibitoraMIC (μg/ml) for the following strains (plasmid/enzyme):
    PAe191PAO38 (pAZ310/OXA13-1)PAO38 (pAZ316/OXA-19)PAO38 (pAZ309/OXA-13)bPAO38 (pNJR-32)DH5α (pAZ326/OXA13-1)DH5α (pAZ327/OXA19)DH5α (pK18)
    Ampicillin>512>512>512—c>5128642
    Ticarcillin51264256256168641
     + CLA51264256256168321
    Piperacilin1283264322280.5
     + TAZ12816643220.510.5
    Cefotaxime12832321616———
    Ceftazidime512256256228160.12
     + CLA256128128216220.06
     + IMI3216321616———
    Aztreonam6481682———
    Cefsulodin646464322———
    Imipenem11111———
    Amikacin32168164———
    Gentamicin256464—4———
    • ↵a CLA, clavulanic acid (2 μg/ml); TAZ, tazobactam (4 μg/ml); IMI, imipenem (0.25 μg/ml).

    • ↵b Data are from reference20.

    • ↵c —, not determined.

  • Table 3.

    Specific activities of OXA-13-1 and OXA-19 fromP. aeruginosa and E. coli producers

    Substrate (50 mM)Sp act (mU/mg)
    PAO38DH5α
    pAZ316/ OXA-19pAZ310/ OXA-13-1pAZ327/ OXA-19pAZ326/ OXA-13-1
    Ampicillin9992882630
    Ceftazidime0.91.01.51.8
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Novel OXA-10-Derived Extended-Spectrum β-Lactamases Selected In Vivo or In Vitro
P. Mugnier, I. Casin, A. T. Bouthors, E. Collatz
Antimicrobial Agents and Chemotherapy Dec 1998, 42 (12) 3113-3116; DOI: 10.1128/AAC.42.12.3113

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Novel OXA-10-Derived Extended-Spectrum β-Lactamases Selected In Vivo or In Vitro
P. Mugnier, I. Casin, A. T. Bouthors, E. Collatz
Antimicrobial Agents and Chemotherapy Dec 1998, 42 (12) 3113-3116; DOI: 10.1128/AAC.42.12.3113
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KEYWORDS

Pseudomonas aeruginosa
beta-lactamases

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