A single amino acid substitution in SED-2 β-lactamase leads to increased inhibitor resistance and an extended substrate spectrum.

ABSTRACT: β-Lactamases are the leading mechanism of resistance to β-lactam antibiotics in Enterobacterales. Here, we report the detection and characteristics of SED-2, a new member of the Citrobacter sedlakii class A chromosomal β-lactamase SED family. A C. sedlakii isolate recovered during routine screening was subjected to whole genome sequencing. A new variant of SED-1 was identified and named SED-2. blaSED-1 and blaSED-2 were cloned into E. coli DH10β. The donor C. sedlakii and the recombinant Escherichia coli-SED-1 and E. coli-SED-2 were further characterized. Antibiotic susceptibilities were determined using Sensititer. Kinetic assays were performed on purified SED-1 and SED-2. AlphaFold2 was used to predict the structure of SED-2 based o

SUBMITTER: Laviad-Shitrit S 

PROVIDER: S-EPMC12671189 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature