Acriflavine-binding capacity controlled by the acrA gene of Escherichia coli.
The acrA mutation in Escherichia coli led to a substantial increase of the acriflavine-binding capacity of the cell, whereas the related mutations acrB (gyrB) and arcC did not. Metal ions such as Na+, K+, Mg2+, Ca2+ and Al3+ effectively released the bound acriflavine, in proportion to their ionic strengths. The presence of cations, in fact, increased the survival fraction of the cells in the acriflavine-containing medium. Polymyxin B, an antibiotic which binds to membrane phospholipid, competed with acriflavine for binding sites. Cell wall digestion by treatment with lysozyme and EDTA slightly decreased the acriflavine-binding capacity. Almost no difference was observed in acriflavine-binding capacity between intact cells and cells from which lipopolysaccharide has been extracted (46.9% removed from the acrA cells and 47.4% from the acrA+ cells). Acriflavine bound to the cells was most effectively extracted by ethanol containing 1% HCl or by 2% (w/v) SDS. The difference in the acriflavine-binding capacity between the acrA and acrA+ cells was also observed in the spheroplasts. These facts indicate a relationship between the acrA gene product and the acriflavine-binding capacity of the cells.
D000167:Acriflavine / Q000494:pharmacology*; D000609:Aminoacridines / Q000494:pharmacology*; D001665:Binding Sites / Q000187:drug effects; D001667:Binding, Competitive / Q000187:drug effects; D004926:Escherichia coli / Q000235:genetics*; D005798:Genes, Bacterial; D009154:Mutation; D009994:Osmolar Concentration; D011112:Polymyxin B / Q000494:pharmacology; D012492:Salts / Q000494:pharmacology; D013104:Spheroplasts / Q000187:drug effects
D000609:Aminoacridines; D012492:Salts; D000167:Acriflavine; D011112:Polymyxin B