The role of lipopolysaccharide anionic binding sites in aminoglycoside uptake in Stenotrophomonas (Xanthomonas) maltophilia.
Aminoglycoside resistance was investigated in six clinical isolates of Stenotrophomonas (Xanthomonas) maltophilia by studying the uptake kinetics and by using a radiochemical method to detect aminoglycoside modifying enzymes. Furthermore, the lipopolysaccharides (LPS) were extracted and characterized by SDS-PAGE and chemical analysis. Dansyl-polymyxin displacement experiments confirmed the availability of anionic binding sites. Growing cells of the isolates bound dansyl-polymyxin but were not lysed.
Vanhoof
R
R
Pasteur Institute of Brabant, Antibiotic Research Unit, Brussels, Belgium.
Sonck
P
P
Hannecart-Pokorni
E
E
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents / Q000378:metabolism* / Q000494:pharmacology; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001665:Binding Sites; D004352:Drug Resistance, Microbial; D004591:Electrophoresis, Polyacrylamide Gel; D008070:Lipopolysaccharides / Q000737:chemistry / Q000378:metabolism*; D011113:Polymyxins / Q000494:pharmacology; D014974:Xanthomonas / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*
D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D001425:Bacterial Outer Membrane Proteins; D008070:Lipopolysaccharides; D011113:Polymyxins