Acquired metallo-β-lactamases (MBLs) are resistance determinants of increasing clinical importance in Gram-negative bacterial pathogens, which confer a broad-spectrum β-lactam resistance including carbapenems. Several such enzymes have been described since the 1990s. In this work a novel acquired MBL, named FIM-1, was identified and characterized. The bla(FIM-1) gene was cloned from a multidrug-resistant Pseudomonas aeruginosa clinical isolate (FI-14/157) cultured from a patient with a vascular graft infection in Florence, Italy. The isolate belonged in the sequence type 235 epidemic clonal lineage. The FIM-1 enzyme is a member of subclass B1 and, among acquired MBLs, exhibited the highest similarity (around 40% amino acid identity) with NDM-type enzymes. In P. aeruginosa FI-14/157 the bla(FIM-1) gene was apparently inserted into the chromosome and associated with ISCR19-like elements that were likely involved in the capture and mobilization of this MBL gene. Transfer experiments of the bla(FIM-1) gene to an Escherichia coli or another P. aeruginosa strain by conjugation or electrotransformation were not successful. The FIM-1 protein was produced in Escherichia coli and purified by two chromatography steps. Analysis of the kinetic parameters, carried out with the purified enzyme, revealed that FIM-1 has a broad substrate specificity, with preference for penicillins (except the 6α-methoxy derivative temocillin) and carbapenems. Aztreonam was not hydrolyzed. Detection of this novel type of acquired MBL in a P. aeruginosa clinical isolate underscores the increasing diversity of such enzymes that can be encountered in the clinical setting.

Pollini, S., Maradei, S., Pecile, P., Olivo, G., Luzzaro, F., Docquier, J.D., et al. (2013). FIM-1, a new acquired metallo-beta-lactamase from a Pseudomonas aeruginosa clinical isolate from Italy. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 57(1), 410-416 [10.1128/​AAC.01953-12].

FIM-1, a new acquired metallo-beta-lactamase from a Pseudomonas aeruginosa clinical isolate from Italy

POLLINI, SIMONA;MARADEI, SIMONA;DOCQUIER, JEAN DENIS;ROSSOLINI, GIAN MARIA
2013-01-01

Abstract

Acquired metallo-β-lactamases (MBLs) are resistance determinants of increasing clinical importance in Gram-negative bacterial pathogens, which confer a broad-spectrum β-lactam resistance including carbapenems. Several such enzymes have been described since the 1990s. In this work a novel acquired MBL, named FIM-1, was identified and characterized. The bla(FIM-1) gene was cloned from a multidrug-resistant Pseudomonas aeruginosa clinical isolate (FI-14/157) cultured from a patient with a vascular graft infection in Florence, Italy. The isolate belonged in the sequence type 235 epidemic clonal lineage. The FIM-1 enzyme is a member of subclass B1 and, among acquired MBLs, exhibited the highest similarity (around 40% amino acid identity) with NDM-type enzymes. In P. aeruginosa FI-14/157 the bla(FIM-1) gene was apparently inserted into the chromosome and associated with ISCR19-like elements that were likely involved in the capture and mobilization of this MBL gene. Transfer experiments of the bla(FIM-1) gene to an Escherichia coli or another P. aeruginosa strain by conjugation or electrotransformation were not successful. The FIM-1 protein was produced in Escherichia coli and purified by two chromatography steps. Analysis of the kinetic parameters, carried out with the purified enzyme, revealed that FIM-1 has a broad substrate specificity, with preference for penicillins (except the 6α-methoxy derivative temocillin) and carbapenems. Aztreonam was not hydrolyzed. Detection of this novel type of acquired MBL in a P. aeruginosa clinical isolate underscores the increasing diversity of such enzymes that can be encountered in the clinical setting.
Pollini, S., Maradei, S., Pecile, P., Olivo, G., Luzzaro, F., Docquier, J.D., et al. (2013). FIM-1, a new acquired metallo-beta-lactamase from a Pseudomonas aeruginosa clinical isolate from Italy. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 57(1), 410-416 [10.1128/​AAC.01953-12].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/43970
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