Proteomics

Dataset Information

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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): Orbitrap Exploris 480

ORGANISM(S): Enterococcus Faecium Bacteria

SUBMITTER: Jeanette, Slettnes Grunnvåg  

LAB HEAD: Christian Lentz

PROVIDER: PXD048798 | Pride | 2024-06-22

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
220325_E_JGrunnvaag_Ef_FP1.raw Raw
220325_E_JGrunnvaag_Ef_FP2.raw Raw
220325_E_JGrunnvaag_Ef_FP3.raw Raw
220325_E_JGrunnvaag_Ef_ULC1.raw Raw
220325_E_JGrunnvaag_Ef_ULC2.raw Raw
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Publications

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

Grunnvåg Jeanette S JS   Hegstad Kristin K   Lentz Christian S CS  

FEMS microbes 20240515


<i>Enterococcus faecium</i> 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 cov  ...[more]

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