The MOX lineage of beta-lactamases includes a group of molecular class C enzymes (AmpCs) encoded by genes mobilized from the chromosomes of Aeromonas spp. to plasmids. MOX-9, previously identified as a plasmid-encoded enzyme from a Citrobacter freundii isolate, belongs to a novel sublineage of MOX enzymes, derived from the resident Aeromonas media AmpC. The bla(MOX-9) gene was found to be carried on a transposon, named Tn7469, likely responsible for its mobilization to plasmidic context. MOX-9 was overexpressed in Escherichia coli, purified, and subjected to biochemical characterization. Kinetic analysis showed a relatively narrow-spectrum profile with strong preference for cephalosporin substrates, with some differences compared with MOX-1 and MOX-2. MOX-9 was not inhibited by clavulanate and sulbactam, while both tazobactam and avibactam acted as inhibitors in the micromolar range.

Molecular and Kinetic Characterization of MOX-9, a Plasmid-Mediated Enzyme Representative of a Novel Sublineage of MOX-Type Class C β-Lactamases / Piccirilli, Alessandra; Antonelli, Alberto; D'Andrea, Marco Maria; Cherubini, Sabrina; Perilli, Mariagrazia; Rossolini, Gian Maria. - In: ANTIMICROBIAL AGENTS AND CHEMOTHERAPY. - ISSN 1098-6596. - ELETTRONICO. - 66:(2022), pp. 0-0. [10.1128/aac.00595-22]

Molecular and Kinetic Characterization of MOX-9, a Plasmid-Mediated Enzyme Representative of a Novel Sublineage of MOX-Type Class C β-Lactamases

Antonelli, Alberto;D'Andrea, Marco Maria;Rossolini, Gian Maria
2022

Abstract

The MOX lineage of beta-lactamases includes a group of molecular class C enzymes (AmpCs) encoded by genes mobilized from the chromosomes of Aeromonas spp. to plasmids. MOX-9, previously identified as a plasmid-encoded enzyme from a Citrobacter freundii isolate, belongs to a novel sublineage of MOX enzymes, derived from the resident Aeromonas media AmpC. The bla(MOX-9) gene was found to be carried on a transposon, named Tn7469, likely responsible for its mobilization to plasmidic context. MOX-9 was overexpressed in Escherichia coli, purified, and subjected to biochemical characterization. Kinetic analysis showed a relatively narrow-spectrum profile with strong preference for cephalosporin substrates, with some differences compared with MOX-1 and MOX-2. MOX-9 was not inhibited by clavulanate and sulbactam, while both tazobactam and avibactam acted as inhibitors in the micromolar range.
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Piccirilli, Alessandra; Antonelli, Alberto; D'Andrea, Marco Maria; Cherubini, Sabrina; Perilli, Mariagrazia; Rossolini, Gian Maria
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2158/1287044
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