Ontology highlight
ABSTRACT:
PROVIDER: PRJNA544265 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Escherichia coli multidrug-resistant sequencing
| PRJNA266657 | ENA
Project description:Multidrug-resistant Escherichia coli genome sequencing
| PRJNA867362 | ENA
Project description:Escherichia coli is an important opportunistic pathogen associated with multidrug-resistant infections in humans and animals. In this study, we performed a global proteomic analysis of the isolateEC15 to characterize its whole-cell protein expression profile. Bacterial cells were cultured under standard laboratory conditions, and total proteins were extracted, digested with trypsin, and analyzed by high-resolution LC–MS/MS. The resulting dataset provides a comprehensive catalog of proteins expressed by Escherichia coli EC15 and a resource for further studies on antimicrobial resistance and virulence mechanisms in this strain.
2026-01-11 | PXD072876 | Pride
Project description:The antibiotic fosfomycin is widely recognized for treatment of lower urinary tract infections caused by Escherichia coli and lately gained importance as a therapeutic option to combat multidrug resistant bacteria. Still, resistance to fosfomycin frequently develops through mutations reducing its uptake. Whereas the inner membrane transport of fosfomycin has been extensively studied in E. coli, its outer membrane (OM) transport remains insufficiently understood. While evaluating minimal inhibitory concentrations in OM porin-deficient mutants, we observed that the E. coli ΔompCΔompF strain is five times more resistant to fosfomycin than the wild type and the respective single mutants. Continuous monitoring of cell lysis of porin-deficient strains in response to fosfomycin additionally indicated the relevance of LamB. Furthermore, the physiological relevance of OmpF, OmpC and LamB for fosfomycin uptake was confirmed by electrophysiological and transcriptional analysis. This study expands the knowledge of how fosfomycin crosses the OM of E. coli.
2024-01-24 | GSE236554 | GEO
Project description:The number and overlapping substrate repertoire of multidrug efflux pumps in the E. coli genome suggest a physiological role apart from multidrug resistance. This role was investigated using transcriptomic analyses of cDNAs labeled from E. coli AG102 mRNA (hyper drug resistant, marR1) and its isogenic major efflux pump mutants. Keywords: Mutation Analysis
2008-03-11 | GSE10757 | GEO
Project description:Multidrug-resistant Escherichia coli isolated from animals
| PRJNA589224 | ENA
Project description:Multidrug-resistant Klebsiella pneumoniae isolated from water samples
| PRJNA563076 | ENA
Project description:<p>Ceftazidime (CAZ) is a critically important broad-spectrum antibiotic widely used in clinical practice. However, the rapid emergence of bacterial resistance to CAZ poses a significant challenge in treating infections caused by multidrug-resistant pathogens. In this study, we employed a metabolism-reprogramming approach to characterize key features of laboratory-evolved CAZ-resistant Escherichia coli K12 and identified repressed glutamate metabolism as a reprogrammable target. Exogenous glutamate effectively resensitized both lab-evolved and clinically isolated multidrug-resistant E. coli strains to CAZ. The resensitization mechanism operates through two synergistic pathways driven by glutamate metabolic flux. First, glutamate conversion to inosine activates the inosine–CpxA–CpxR–OmpF regulatory axis, increasing outer membrane permeability. Second, glutamate entry into the pyruvate cycle restores the proton motive force (PMF), energizing the inner membrane. Together, increased outer membrane permeability and a restored PMF synergistically enhance intracellular accumulation of CAZ—by facilitating its entry through the widened OmpF porin and promoting its active uptake across the cytoplasmic membrane. This dual-mechanism strategy provides a novel two-pronged approach to overcoming CAZ resistance. Our findings underscore the potential of targeting bacterial metabolic pathways to restore susceptibility and extend the utility of existing antibiotics against resistant pathogens.</p><p>Keywords: Multidrug-resistant bacteria; E. coli; glutamate; CpxA/R-OmpF axis; proton motive force; metabolic state-reprogramming</p><p><br></p><p><br></p><p><br></p>
2026-01-20 | MTBLS13732 | MetaboLights