Aminoglycoside-inducible expression of the mexAB-oprM multidrug efflux operon in Pseudomonas aeruginosa: Involvement of the envelope stress-responsive AmgRS two-component system

Autor: Keith Poole, Michael Fruci
Jazyk: angličtina
Rok vydání: 2018
Předmět:
0301 basic medicine
Operon
Molecular biology
lcsh:Medicine
Gene Expression
Artificial Gene Amplification and Extension
medicine.disease_cause
Pathology and Laboratory Medicine
Biochemistry
Polymerase Chain Reaction
Antibiotics
Nucleic Acids
Gene expression
Medicine and Health Sciences
lcsh:Science
Regulation of gene expression
Multidisciplinary
Chemistry
Antimicrobials
Aminoglycoside
Pseudomonas Aeruginosa
Drugs
Neomycins
Two-component regulatory system
Drug Resistance
Multiple

Cell biology
Bacterial Pathogens
Medical Microbiology
Efflux
Pathogens
Research Article
030106 microbiology
DNA construction
Microbiology
03 medical and health sciences
Bacterial Proteins
Gene Types
Stress
Physiological

Pseudomonas
Microbial Control
medicine
Genetics
Operons
Microbial Pathogens
Pharmacology
Bacteria
Pseudomonas aeruginosa
lcsh:R
Organisms
Biology and Life Sciences
DNA
Gene Expression Regulation
Bacterial

biochemical phenomena
metabolism
and nutrition

Research and analysis methods
Response regulator
Molecular biology techniques
Aminoglycosides
Plasmid Construction
Regulator Genes
lcsh:Q
Antimicrobial Resistance
Zdroj: PLoS ONE
PLoS ONE, Vol 13, Iss 10, p e0205036 (2018)
ISSN: 1932-6203
Popis: Exposure of P. aeruginosa to the aminoglycoside (AG) paromomycin (PAR) induced expression of the PA3720-armR locus and the mexAB-oprM multidrug efflux operon that AmgR controls, although PAR induction of mexAB-oprM was independent of armR. Multiple AGs promoted mexAB-oprM expression and this was lost in the absence of the amgRS locus encoding an aminoglycoside-activated envelope stress-responsive 2-component system (TCS). Purified AmgR bound to the mexAB-oprM promoter region consistent with this response regulator directly regulating expression of the efflux operon. The thiol-active reagent, diamide, which, like AGs, promotes protein aggregation and cytoplasmic membrane damage also promoted AmgRS-dependent mexAB-oprM expression, a clear indication that the MexAB-OprM efflux system is recruited in response to membrane perturbation and/or circumstances that lead to this. Despite the AG and diamide induction of mexAB-oprM, however, MexAB-OprM does not appear to contribute to resistance to these agents.
Databáze: OpenAIRE
Nepřihlášeným uživatelům se plný text nezobrazuje