Aminoglycoside resistance in Pseudomonas aeruginosa due to outer membrane stabilization.
Pseudomonas aeruginosa PAO1 released a significant amount of a cytoplasmic enzyme, glucose-6-phosphate dehydrogenase, in the presence of aminoglycoside and lysozyme. The extent of the enzyme release was inversely related to the MICs of the aminoglycoside. However, the aminoglycoside-resistant strain F3721, treated in the same way; released a less enzyme. The F3721 LPS was extracted in the phenol phase instead of the water phase in which PAO1 LPS was easily extracted. Electrophoretic analysis of the F3721 LPS showed the ladder bands at the high Mr position, suggesting that the LPS of the aminoglycoside-resistant cells has a structural modification(s) which somehow protects the outer membrane from aminoglycoside-mediated damage.
Yoneyama
H
H
Department of Cellular Information Sciences, Tokai University, School of Medicine, Isehara, Japan.
Sato
K
K
Nakae
T
T
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D002462:Cell Membrane / Q000502:physiology; D004352:Drug Resistance, Microbial; D005954:Glucosephosphate Dehydrogenase / Q000032:analysis / Q000378:metabolism*; D006801:Humans; D008070:Lipopolysaccharides / Q000032:analysis; D011550:Pseudomonas aeruginosa / Q000187:drug effects* / Q000201:enzymology
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D008070:Lipopolysaccharides; D005954:Glucosephosphate Dehydrogenase