ArticleNature chemical biology2018
Identification of a S. aureus virulence factor by activity-based protein profiling (ABPP).
Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 105 citations in OpenAlex.
- Unique structural and ligand-binding properties of theProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Imaging ofbioRxiv : the preprint server for biology · 2026Article
- Chemoproteomic profiling of adaptive ATP-binding protein activity inFEMS microbes · 2026Article
- Unique structural and ligand binding properties of thebioRxiv : the preprint server for biology · 2025Article
- Activation of themBio · 2025Article
- Identification of covalent inhibitors of Staphylococcus aureus serine hydrolases important for virulence and biofilm formation.Nature communications · 2025Article
- Depletion-dependent activity-based protein profiling using SWATH/DIA-MS detects serine hydrolase lipid remodeling in lung adenocarcinoma progression.Nature communications · 2025Article
- Similar but Distinct-Biochemical Characterization of the Staphylococcus aureus Serine Hydrolases FphH and FphI.Proteins · 2025Article
- Activity-Based Protein Profiling Identifies an α-Amylase Family Protein Contributing to the Virulence of Methicillin-ResistantACS infectious diseases · 2025Article
- An mRNA Display Approach for Covalent Targeting of aJournal of the American Chemical Society · 2025Article
- Bioinformatics Analysis Suggests That SE_1780 Protein FrommicroPublication biology · 2025Article
- Activity-Based Protein Profiling of Serine Hydrolases in Bacteria: Methods and Protocols.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Diversity Oriented Clicking for Modular Synthesis.Nature reviews. Methods primers · 2025Article
- An mRNA Display Approach for Covalent Targeting of abioRxiv : the preprint server for biology · 2024Article
- Single-cell phenotypic profiling and backtracing exposes and predicts clinically relevant subpopulations in isogenic Staphylococcus aureus communities.Communications biology · 2024Article
- Mixed alkyl/aryl phosphonates identify metabolic serine hydrolases as antimalarial targets.Cell chemical biology · 2024Article
- Ligand discovery by activity-based protein profiling.Cell chemical biology · 2024Review
- DecipheringmSystems · 2024Article
- Integrating the analysis of human biopsies using post-translational modifications proteomics.Protein science : a publication of the Protein Society · 2024Review
- Monitoring host-pathogen interactions using chemical proteomics.RSC chemical biology · 2024Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Serine hydrolases play diverse roles in regulating host-pathogen interactions in a number of organisms, yet few have been characterized in the human pathogen Staphylococcus aureus. Here we describe a chemical proteomic screen that identified ten previously uncharacterized S. aureus serine hydrolases that mostly lack human homologs. We termed these enzymes fluorophosphonate-binding hydrolases (FphA-J). One hydrolase, FphB, can process short fatty acid esters, exhibits increased activity in response to host cell factors, is located predominantly on the bacterial cell surface in a subset of cells, and is concentrated in the division septum. Genetic disruption of fphB confirmed that the enzyme is dispensable for bacterial growth in culture but crucial for establishing infection in distinct sites in vivo. A selective small molecule inhibitor of FphB effectively reduced infectivity in vivo, suggesting that it may be a viable therapeutic target for the treatment or management of Staphylococcus infections.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.