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Antimicrobial Agents and Chemotherapy, January 2009, p. 242-248, Vol. 53, No. 1
0066-4804/09/$08.00+0     doi:10.1128/AAC.00642-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Sec- and Tat-Dependent Translocation of β-Lactamases across the Escherichia coli Inner Membrane{triangledown} ,{dagger}

N. Pradel,1* J. Delmas,1 L. F. Wu,2 C. L. Santini,2 and R. Bonnet1

Laboratoire de Bactériologie, JE2526, UFR Médecine, Université d'Auvergne, Clermont-Ferrand,1 Laboratoire de Chimie Bactérienne, UPR9043, CNRS, Marseille, France2

Received 16 May 2008/ Returned for modification 2 October 2008/ Accepted 26 October 2008

β-Lactamases represent the major resistance mechanism of gram-negative bacteria against β-lactam antibiotics. The amino acid sequences of these proteins vary widely, but all are located in the periplasm of bacteria. In this study, we investigated the translocation mechanism of representative β-lactamases in an Escherichia coli model. N-terminal signal sequence analyses, antibiotic activity assay, and direct measurement of translocation of a green fluorescent protein (GFP) reporter fused to β-lactamases revealed that most were exported via the Sec pathway. However, the Stenotrophomonas maltophilia L2 β-lactamase was exported via the E. coli Tat translocase, while the S. maltophilia L1 β-lactamase was Sec dependent. These results show the possible Tat-dependent translocation of β-lactamases in the E. coli model system. In addition, the mutation of the cytoskeleton-encoding gene mreB, which may be involved in the spatial organization of penicillin-binding proteins, decreased the MIC of β-lactams for β-lactamase-producing E. coli. These findings provide new knowledge about β-lactamase translocation, a putative new target for addressing β-lactamase-mediated resistance.

* Corresponding author. Mailing address: Laboratoire de Bactériologie, Faculté de Médecine, Université d'Auvergne, 28 Place Henri-Dunant, 63 001 Clermont-Ferrand, France. Phone: (33) 473 754 920. Fax: (33) 473 754 922. E-mail: nathalie.pradel{at}u-clermont1.fr

{triangledown} Published ahead of print on 3 November 2008.

{dagger} Supplemental material for this article may be found at http://aac.asm.org/.

Antimicrobial Agents and Chemotherapy, January 2009, p. 242-248, Vol. 53, No. 1
0066-4804/09/$08.00+0     doi:10.1128/AAC.00642-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Moran-Barrio, J., Limansky, A. S., Viale, A. M. (2009). Secretion of GOB Metallo-{beta}-Lactamase in Escherichia coli Depends Strictly on the Cooperation between the Cytoplasmic DnaK Chaperone System and the Sec Machinery: Completion of Folding and Zn(II) Ion Acquisition Occur in the Bacterial Periplasm. Antimicrob. Agents Chemother. 53: 2908-2917 [Abstract] [Full Text]  


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