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Explore antimicrobial resistance genes from the literature
multidrug efflux RND transporter periplasmic adaptor subunit MexE
Overview
| Protein Change | Nucleotide Change | Mechanism | Organism | Resistance To | Database | Validation Status |
|---|---|---|---|---|---|---|
| S8F | - | - | Pseudomonas aeruginosa | Ciprofloxacin|Levofloxacin | Reslit | Candidate |
| G195D | - | - | Pseudomonas aeruginosa | Piperacillin/tazobactam|Ceftazidime|Cefepime|Meropenem|Imipenem|Tobramycin|Ciprofloxacin | Reslit | Candidate |
| - | - | Pseudomonas aeruginosa |
Reslit |
| Candidate |
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| MexE | Card DatabaseReference Gene CatalogReslit | 9 | EFFLUX, Tetracycline +9 | Pseudomonas aeruginosa PAO1 +2 | - | 1999, 2009, 2011, 2012, 2013, 2022, 2024 | AE004091.2 | AAG05881.1 |
| mex E | Reslit | 1 | Fluoroquinolone, Aminoglycoside +1 | Pseudomonas aeruginosa | Romania | 2023 | - | - |
Characterization of MexT, the regulator of the MexE-MexF-OprN multidrug efflux system of Pseudomonas aeruginosa.
Characterization of MexT, the regulator of the MexE-MexF-OprN multidrug efflux system of Pseudomonas aeruginosa.
Transcriptome profiling defines a novel regulon modulated by the LysR-type transcriptional regulator MexT in Pseudomonas aeruginosa.
The study identifies a novel regulon modulated by the LysR-type transcriptional regulator MexT in Pseudomonas aeruginosa, including genes such as mexT, mexE, mexF, oprN, and mexS. The conserved DNA motif required for MexT-mediated gene activation was identified, and the binding of MexT to this motif was confirmed through EMSA.
MexEF-OprN efflux pump exports the Pseudomonas quinolone signal (PQS) precursor HHQ (4-hydroxy-2-heptylquinoline).
The study identifies the MexEF-OprN efflux pump as a key player in exporting the Pseudomonas quinolone signal (PQS) precursor HHQ, affecting quorum sensing and virulence in Pseudomonas aeruginosa.
The regulatory repertoire of Pseudomonas aeruginosa AmpC ß-lactamase regulator AmpR includes virulence genes.
AmpR is a global regulator in P. aeruginosa that influences the expression of over 500 genes, including those involved in β-lactam resistance, virulence, and biofilm formation.
Transcriptome profiling reveals links between ParS/ParR, MexEF-OprN, and quorum sensing in the regulation of adaptation and virulence in Pseudomonas aeruginosa.
The study identifies that the ParS/ParR system regulates the mexEF-oprN operon through mexS, which is involved in resistance to fluoroquinolones, trimethoprim, and chloramphenicol.
Antibiotic resistance in plant growth promoting bacteria: A comprehensive review and future perspectives to mitigate potential gene invasion risks.
This review highlights the prevalence of antibiotic resistance genes (ARGs) in plant growth-promoting bacteria (PGPB) and emphasizes the potential risks of ARG dissemination through biofertilizers. Key findings include the identification of various ARGs such as bacA, fosB, ermD, bl2a, vanSA, cat, acrD, mexF, mexD, mexW, mexE, mexY, mexX, mexZ, mexR, mexA, mexB, mexC, mexD, mexE, and mexF, which confer resistance to multiple antibiotics.
Uncovering the Resistance Mechanisms in Extended-Drug-Resistant Pseudomonas aeruginosa Clinical Isolates: Insights from Gene Expression and Phenotypic Tests.
The study identified bla GES-2, bla OXA48-like, bla NDM, bla SPM, and bla VIM as the main carbapenemase genes in MDR P. aeruginosa isolates. Overexpression of mex efflux pumps, particularly mex C, was strongly associated with multidrug resistance.
From Proteome to Potential Drugs: Integration of Subtractive Proteomics and Ensemble Docking for Drug Repurposing against Pseudomonas aeruginosa RND Superfamily Proteins.
The study identifies and characterizes essential proteins in Pseudomonas aeruginosa, particularly RND efflux pumps, which are critical for antibiotic resistance. Computational methods and ensemble docking were used to find potential inhibitors like MK-3207, R-428, and Suramin, showing promise for drug repurposing.
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