EBR-5, a Novel Variant of Metallo-β-Lactamase EBR from Multidrug-Resistant Empedobacter stercoris.

ABSTRACT: A novel chromosome-encoded metallo-β-lactamase (MBL) EBR variant, namely, EBR-5, was identified in a multidrug-resistant Empedobacter stercoris strain SCVM0123 that was isolated from chicken anal swab samples. EBR-5 shared 82.13% amino acid identity with the previously known EBR-1. The expression of EBR-5 in Escherichia coli reduced susceptibility to expanded-spectrum cephalosporins and carbapenems. Compared with bla_EBR-1, the recombinant strain harboring bla_EBR-5 exhibited higher minimum inhibitory concentrations of piperacillin, cefotaxime, and meropenem. Despite the genetic diversity, EBR-5 and EBR-1 possessed similar kinetic parameters, except for cefepime, cefotaxime, cefoxitin, cephalothin, and meropenem, which were hydrolyzed more by EBR-5. In add

SUBMITTER: Li P 

PROVIDER: S-EPMC10101081 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature