FP-biotin enrichment of serine hydrolases in Enterococcus faecium

ABSTRACT: In our study, we employed activity-based protein profiling (ABPP), a technique that uses specialized inhibitors to identify active serine hydrolases in different strains of E. faecium (clade A1 and A2) and E. lactis under various growth conditions. Serine hydrolases, a large and diverse family of enzymes that include established drug targets like penicillin-binding proteins, have other less-studied subfamilies. In addition to fluorescent, gel-based profiling, we used a biotin-tagged fluorophosphonate probe for the enrichment and identification of serine hydrolase enzymes via streptavidin enrichment and liquid chromatography/mass spectrometry analysis. This led to the discovery of 11 largely unexplored potential targets (including α,β-hydrolases, SGNH-hydrolases, phospholipases, amidases, and peptidases) that could be exploited for drug developmentagainst the vancomycin-resistant E. faecium strain E745.

INSTRUMENT(S):

ORGANISM(S): Enterococcus Faecium Bacteria

SUBMITTER: Jeanette, Slettnes Grunnvåg  

LAB HEAD: Christian Lentz

PROVIDER: PXD048798 | Pride | 2024-06-22

REPOSITORIES: Pride