ArticleAntimicrobial agents and chemotherapy2013
IreB, a Ser/Thr kinase substrate, influences antimicrobial resistance in Enterococcus faecalis.
Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 65 citations in OpenAlex.
- Phosphorylation of the cell wall hydrolase MltG in response to cell wall stress modulates resistance toward cephalosporins inJournal of bacteriology · 2025Article
- The cell wall hydrolase MltG is essential to maintain cell wall homeostasis ofJournal of bacteriology · 2025Article
- Article
- Dynamic Protein Phosphorylation inMicroorganisms · 2024Article
- Reciprocal regulation of enterococcal cephalosporin resistance by products of the autoregulated yvcJ-glmR-yvcL operon enhances fitness during cephalosporin exposure.PLoS genetics · 2024Article
- Secrets of getting started: Regulation of the first committed step of peptidoglycan synthesis by protein phosphorylation in Enterococcus and other Gram-positive bacteria.Molecular microbiology · 2023Article
- PASTA-kinase-mediated signaling drives accumulation of the peptidoglycan synthesis protein MurAA to promote cephalosporin resistance in Enterococcus faecalis.Molecular microbiology · 2023Article
- Multisite Phosphorylation Regulates GpsB Function in Cephalosporin Resistance of Enterococcus faecalis.Journal of molecular biology · 2023Article
- Conformational changes in the activation loop of a bacterial PASTA kinase.Protein science : a publication of the Protein Society · 2023Article
- A link between STK signalling and capsular polysaccharide synthesis in Streptococcus suis.Nature communications · 2023Article
- GpsB Promotes PASTA Kinase Signaling and Cephalosporin Resistance inJournal of bacteriology · 2022Article
- MurA escape mutations uncouple peptidoglycan biosynthesis from PrkA signaling.PLoS pathogens · 2022Article
- Clostridioides difficile Phosphoproteomics Shows an Expansion of Phosphorylated Proteins in Stationary Growth Phase.mSphere · 2022Article
- Highly Effective Markerless Genetic Manipulation ofFrontiers in microbiology · 2022Article
- Evaluation of small molecule kinase inhibitors as novel antimicrobial and antibiofilm agents.Chemical biology & drug design · 2021Review
- IreK-Mediated, Cell Wall-Protective Phosphorylation inJournal of proteome research · 2021Article
- PASTA kinase-dependent control of peptidoglycan synthesis via ReoM is required for cell wall stress responses, cytosolic survival, and virulence in Listeria monocytogenes.PLoS pathogens · 2021Article
- The enterococcal PASTA kinase: A sentinel for cell envelope stress.Molecular oral microbiology · 2021Review
- Resistance in Vancomycin-Resistant Enterococci.Infectious disease clinics of North America · 2020Review
- Escherichia coli YegI is a novel Ser/Thr kinase lacking conserved motifs that localizes to the inner membrane.FEBS letters · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Enterococcus faecalis is a Gram-positive bacterium that is a major cause of hospital-acquired infections, in part due to its intrinsic resistance to cephalosporins. The mechanism that confers intrinsic cephalosporin resistance in enterococci remains incompletely defined. Previously, we have shown that the Ser/Thr protein kinase and phosphatase pair IreK and IreP act antagonistically to regulate cephalosporin resistance in E. faecalis. We hypothesize that IreK senses antibiotic-induced cell wall damage and activates a signaling pathway leading to antibiotic resistance. However, the factors downstream of IreK have not yet been identified. To discover such factors, suppressor mutations that restored resistance to a ΔireK kinase mutant were identified. Mutations were found in IreB, a highly conserved gene of unknown function that is widespread among low-GC Gram-positive bacteria. We show that IreB plays a negative regulatory role in cephalosporin resistance and is an endogenous substrate of both IreK and IreP. IreB is phosphorylated on conserved threonine residues, and mutations at these sites impair cephalosporin resistance. Our results are consistent with a model in which the activity of IreB is modulated by IreK-dependent phosphorylation in a signaling pathway required for cephalosporin resistance and begin to shed light on the function of this previously uncharacterized protein.
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