OXA-48-like carbapenemases producing Enterobacteriaceae in different niches

  • Assia Mairi
  • Alix Pantel
  • Albert Sotto
  • Jean-Philippe LavigneEmail author
  • Aziz Touati


The emergence of carbapenem-resistant enterobacterial species poses a serious threat to public health worldwide. OXA-48-type carbapenem-hydrolyzing class D β-lactamases are widely distributed among Enterobacteriaceae, with significant geographical differences. To date, 11 OXA-48-like variants have been identified, with classical OXA-48 being the most widespread. These enzymes show high-level hydrolytic activity against penicillins and low-level hydrolysis towards carbapenems. Since the first description of the OXA-48 carbapenemase in Turkey, bacterial strains producing the enzyme have been extensively reported in nosocomial and community outbreaks in many parts of the word, particularly in the Mediterranean area and European countries. The rapid spread of Enterobacteriaceae producing OXA-48-like enzymes in different ecosystems has become a serious issue recently. The number of reservoirs for such organisms is increasing, not only in hospitals, but also in the community, among animals (e.g., livestock, companion animals, and wildlife) and in the environment. This review aims to summarize the main characteristics of the OXA-48-type carbapenemases, covering genetic and enzymatic traits, their epidemiology, clonality and associated genes, correlation with extended-spectrum β-lactamases (ESBLs) or plasmidic AmpC (pAmpC) in different bacterial species worldwide.


Carbapenemase Enterobacteriaceae Environment Niches OXA-48-like Persistence 



We thank Sarah Kabani for her help in the preparation and editing of the manuscript.


This work was supported by the National Institute of Health and Medical Research (INSERM).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

Not applicable.

Informed consent

Not applicable.

Supplementary material

10096_2017_3112_MOESM1_ESM.pdf (28 kb)
Figure S1 Alignment of the amino acid sequences of OXA-48 and its variants. The amino acid sequence modifications between each variant are highlighted in yellow. Possible conserved residues of the active site of the OXA-48-like enzymes are highlighted in gray. (PDF 27 kb)
10096_2017_3112_MOESM2_ESM.pdf (27 kb)
Figure S2 Number of reported cases with OXA-48 producers over the period 2004–2017 with distribution of species. (PDF 27 kb)
10096_2017_3112_MOESM3_ESM.pdf (16 kb)
Figure S3 Change in the number of publications reporting the presence of OXA-48-producers in non-human sources (2004–2017). (PDF 16 kb)


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Copyright information

© Springer-Verlag GmbH Germany 2017

Authors and Affiliations

  • Assia Mairi
    • 1
    • 2
  • Alix Pantel
    • 2
    • 3
  • Albert Sotto
    • 2
  • Jean-Philippe Lavigne
    • 2
    • 3
    Email author
  • Aziz Touati
    • 1
  1. 1.Laboratoire d’Ecologie Microbienne, FSNVUniversité de BejaiaBejaiaAlgeria
  2. 2.Institut National de la Santé et de la Recherche Médicale, U1047Université Montpellier, UFR de MédecineNîmesFrance
  3. 3.Department of MicrobiologyUniversity Hospital of NîmesNîmesFrance

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