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. 2011 Jul;49(7):2667-70.
doi: 10.1128/JCM.00328-11. Epub 2011 May 4.

Sensitive and specific phenotypic assay for metallo-beta-lactamase detection in Enterobacteria by use of a moxalactam disk supplemented with EDTA

Emilie Pluquet  1 , Guillaume Arlet, Edouard Bingen, Laurence Drieux, Hedi Mammeri
Affiliations

Sensitive and specific phenotypic assay for metallo-beta-lactamase detection in Enterobacteria by use of a moxalactam disk supplemented with EDTA

Emilie Pluquet et al. J Clin Microbiol. 2011 Jul.

Abstract

Moxalactam is highly hydrolyzed by plasmid-mediated metallo-β-lactamases (MBLs), whereas it is poorly inactivated by serine-active carbapenemases. This study demonstrated that moxalactam resistance constituted an effective screen for MBL expression in enterobacteria, which could be confirmed, even in low-MBL-producing isolates, by a disk potentiation test using moxalactam and EDTA.

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Figures

Fig. 1.
Fig. 1.
Comparison of the MOX-EDTA synergy test with enterobacterial clinical isolates producing class A, B, C, or D carbapenemases. Lane 1, VIM-1-producing Klebsiella pneumoniae isolate (10); lane 2, KPC-2-producing K. pneumoniae isolate (11); lane 3, CMY-4-producing K. pneumoniae isolate (2), lane 4, OXA-48-producing K. pneumoniae isolate (7). (A) Moxalactam disk supplemented with 5 μl of EDTA (0.5 M); (B) moxalactam disk alone for inhibition zone diameter reference. A significant increase of the inhibition zone in the presence of EDTA (≥10 mm) indicates MBL activity.
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References

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