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Antimicrobial Agents and Chemotherapy, May 2009, p. 1944-1951, Vol. 53, No. 5
0066-4804/09/$08.00+0     doi:10.1128/AAC.01581-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Novel Plasmid-Encoded Ceftazidime-Hydrolyzing CTX-M-53 Extended-Spectrum β-Lactamase from Salmonella enterica Serotypes Westhampton and Senftenberg{triangledown}

Benoît Doublet,1,2 Sophie A. Granier,3 Frédéric Robin,4,5 Richard Bonnet,4,5 Laëtitia Fabre,1 Anne Brisabois,3 Axel Cloeckaert,2 and François-Xavier Weill1*

Institut Pasteur, Centre National de Référence des Salmonella, Laboratoire des Bactéries Pathogènes Entériques, Paris, France,1 INRA, UR1282, Infectiologie Animale et Santé Publique, IASP, Nouzilly F-37380, France,2 Agence Française de Sécurité Sanitaire des Aliments, LERQAP, Unité Caractérisation et Epidémiologie Bactérienne, Maisons-Alfort, France,3 Laboratoire de Bactériologie, CHU de Clermont-Ferrand, Clermont-Ferrand F-63003, France,4 Laboratoire de Bactériologie, UFR de Médecine, Université Clermont1, JE2526 usc INRA2018, Clermont-Ferrand F-63001, France5

Received 28 November 2008/ Returned for modification 10 February 2009/ Accepted 2 March 2009

We describe the characterization of a novel CTX-M β-lactamase from Salmonella enterica. Four S. enterica isolates (three of serotype Westhampton and one of serotype Senftenberg) resistant to extended-spectrum cephalosporins (cefotaxime and ceftazidime) were recovered in 2004 from living cockles in three supermarkets located in distant geographic areas in France, which got their supplies from the same fishery. The isolates were found to produce a novel extended-spectrum β-lactamase (ESBL) belonging to the CTX-M-1 phylogenetic group and named CTX-M-53. The CTX-M-53 β-lactamase harbored the substitution Asp240Gly, like the CTX-M-15 enzyme, which is specifically implicated in a higher catalytic efficiency against ceftazidime. The blaCTX-M-53 gene was located on a mobilizable 11-kb plasmid, pWES-1. The complete sequence of pWES-1 revealed the presence of a novel insertion sequence, ISSen2, and an IS26 element upstream and downstream of the blaCTX-M-53 gene, respectively; however, transposition assays of the blaCTX-M-53 gene were unsuccessful. IS26 elements may have contributed to the acquisition of the blaCTX-M-53 gene. Interestingly, the mobilization module of the pWES-1 plasmid was similar to that of quinolone resistance plasmids (carrying the qnrS2 gene) from aquatic sources. Although belonging to two serotypes differentiated on the basis of the O-antigen structure (E1 or E4 groups), the isolates were found to be genetically indistinguishable by pulsed-field gel electrophoresis. Multilocus sequence typing showed that the isolates of serotype Westhampton had a sequence type, ST14, common among isolates of serotype Senftenberg. This is the first characterization of the CTX-M-53 ESBL, which represents an additional ceftazidime-hydrolyzing CTX-M enzyme.

* Corresponding author. Mailing address: Centre National de Référence des Salmonella, Laboratoire des Bactéries Pathogènes Entériques, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France. Phone: 33-(0)1 45 68 83 45. Fax: 33-(0)1 45 68 88 37. E-mail: fxweill{at}pasteur.fr

{triangledown} Published ahead of print on 9 March 2009.

Antimicrobial Agents and Chemotherapy, May 2009, p. 1944-1951, Vol. 53, No. 5
0066-4804/09/$08.00+0     doi:10.1128/AAC.01581-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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