4.7 Article

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

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AMER SOC MICROBIOLOGY
DOI: 10.1128/aac.00595-22

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MOX; beta-lactamases; enzyme kineticss

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  1. University of L'Aquila internal funds [07_PROGETTO_RICERCA_ATENEO]

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The MOX lineage of beta-lactamases includes enzymes encoded by genes mobilized from the chromosomes of Aeromonas spp. to plasmids. MOX-9, a novel sublineage of MOX enzymes, shows a strong preference for cephalosporin substrates with some differences in biochemical characteristics compared to other MOX enzymes.
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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