Unique structural modifications are present in the lipopolysaccharide from colistin-resistant strains of Acinetobacter baumannii.

ABSTRACT: Acinetobacter baumannii is a nosocomial opportunistic pathogen that can cause severe infections, including hospital-acquired pneumonia, wound infections, and sepsis. Multidrug-resistant (MDR) strains are prevalent, further complicating patient treatment. Due to the increase in MDR strains, the cationic antimicrobial peptide colistin has been used to treat A. baumannii infections. Colistin-resistant strains of A. baumannii with alterations to the lipid A component of lipopolysaccharide (LPS) have been reported; specifically, the lipid A structure was shown to be hepta-acylated with a phosphoethanolamine (pEtN) modification present on one of the terminal phosphate residues. Using a tandem mass spectrometry platform, we provide definitive evidence that the lipid A isolated from colistin-resis

SUBMITTER: Pelletier MR 

PROVIDER: S-EPMC3811424 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature