ArticleAntimicrobial agents and chemotherapy2013
Mutational activation of the AmgRS two-component system in aminoglycoside-resistant Pseudomonas aeruginosa.
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 29 papers.
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Who cites it
29 citing papers in PubMed, 47 citations in OpenAlex.
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- Activation of the envelope stress-responsive two-component system AmgRS compensates for depletion of the essential lipoprotein signal peptidase LspA inCurrent research in microbial sciences · 2026Article
- An antibiotic-responsive regulator orchestrates chronic-to-acute virulence switch in Pseudomonas aeruginosa.Nucleic acids research · 2025Article
- Regulation, structure, and activity of theAntimicrobial agents and chemotherapy · 2025Review
- RND Efflux Pump Induction: A Crucial Network Unveiling Adaptive Antibiotic Resistance Mechanisms of Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2024Review
- Nationwide genome surveillance of carbapenem-resistantAntimicrobial agents and chemotherapy · 2024Article
- Antimicrobial Resistance: Two-Component Regulatory Systems and Multidrug Efflux Pumps.Antibiotics (Basel, Switzerland) · 2023Review
- Gene-Gene Interactions Reduce Aminoglycoside Susceptibility ofAntibiotics (Basel, Switzerland) · 2023Article
- Mechanistic insights into nanoparticle surface-bacterial membrane interactions in overcoming antibiotic resistance.Frontiers in microbiology · 2023Review
- Targeting the Holy Triangle of Quorum Sensing, Biofilm Formation, and Antibiotic Resistance in Pathogenic Bacteria.Microorganisms · 2022Review
- Article
- Hypermutator Pseudomonas aeruginosa Exploits Multiple Genetic Pathways To Develop Multidrug Resistance during Long-Term Infections in the Airways of Cystic Fibrosis Patients.Antimicrobial agents and chemotherapy · 2020Article
- A large-scale whole-genome comparison shows that experimental evolution in response to antibiotics predicts changes in naturally evolved clinicalAntimicrobial agents and chemotherapy · 2019Article
- Analysis of theAntimicrobial agents and chemotherapy · 2019Article
- Two Component Regulatory Systems and Antibiotic Resistance in Gram-Negative Pathogens.International journal of molecular sciences · 2019Review
- Roles of two-component regulatory systems in antibiotic resistance.Future microbiology · 2019Review
- Article
- Rifampicin potentiation of aminoglycoside activity against cystic fibrosis isolates of Pseudomonas aeruginosa.The Journal of antimicrobial chemotherapy · 2017Article
- Transcriptional and Mutational Profiling of an Aminoglycoside-Resistant Pseudomonas aeruginosa Small-Colony Variant.Antimicrobial agents and chemotherapy · 2017Article
- Two-component systems required for virulence in Pseudomonas aeruginosa.FEMS microbiology letters · 2017Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The amgRS operon encodes a presumed membrane stress-responsive two-component system linked to intrinsic aminoglycoside resistance in Pseudomonas aeruginosa. Genome sequencing of a lab isolate showing modest pan-aminoglycoside resistance, strain K2979, revealed a number of mutations, including a substitution in amgS that produced an R182C change in the AmgS sensor kinase product of this gene. Introduction of this mutation into an otherwise wild-type strain recapitulated the resistance phenotype, while correcting the mutation in the resistant mutant abrogated the resistant phenotype, confirming that the amgS mutation is responsible for the aminoglycoside resistance of strain K2979. The amgSR182 mutation promoted an AmgR-dependent, 2- to 3-fold increase in expression of the AmgRS target genes htpX and PA5528, mirroring the impact of aminoglycoside exposure of wild-type cells on htpX and PA5528 expression. This suggests that amgSR182 is a gain-of-function mutation that activates AmgS and the AmgRS two-component system in promoting modest resistance to aminoglycosides. Screening of several pan-aminoglycoside-resistant clinical isolates of P. aeruginosa revealed three that showed elevated htpX and PA5528 expression and harbored single amino acid-altering mutations in amgS (V121G or D106N) and no mutations in amgR. Introduction of the amgSV121G mutation into wild-type P. aeruginosa generated a resistance phenotype reminiscent of the amgSR182 mutant and produced a 2- to 3-fold increase in htpX and PA5528 expression, confirming that it, too, is a gain-of-function aminoglycoside resistance-promoting mutation. These results highlight the contribution of amgS mutations and activation of the AmgRS two-component system to acquired aminoglycoside resistance in lab and clinical isolates of P. aeruginosa.
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