Activity-based protein profiling of serine hydrolases and penicillin-binding proteins in Enterococcus faecium.

ABSTRACT: Enterococcus faecium is a gut commensal bacterium which is gaining increasing relevance as an opportunistic, nosocomial pathogen. Its high level of intrinsic and acquired antimicrobial resistance is causing a lack of treatment options, particularly for infections with vancomycin-resistant strains, and prioritizes the identification and functional validation of novel druggable targets. Here, we use activity-based protein profiling (ABPP), a chemoproteomics approach using functionalized covalent inhibitors, to detect active serine hydrolases across 11 E. faecium and Enterococcus lactis strains. Serine hydrolases are a big and diverse enzyme family, that includes known drug targets such as penicillin-binding proteins (PBPs), whereas other subfamilies are underexplored. Co

SUBMITTER: Grunnvag JS 

PROVIDER: S-EPMC11134295 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature