Six, David, Yuan, Yanqiu, Leeds, Jennifer and Meredith, Timothy (2014) Deletion of the beta-Acetoacetyl Synthase FabY in Pseudomonas aeruginosa induces hypoacylation of lipopolysaccharide. Antimicrobial Agents and Chemotherapy, 58 (1). pp. 153-161. ISSN 1098-6596

Abstract

The beta-acetoacetyl-acyl carrier protein synthase FabY is a key enzyme in the initiation of fatty acid biosynthesis in Pseudomonas aeruginosa. Deletion of fabY results in an increased susceptibility of P. aeruginosa in vitro to a number of antibiotics, including vancomycin and cephalosporins. Because antibiotic susceptibility can be influenced by changes in membrane lipid composition, we determined the total fatty acid profile of the delta fabY mutant which suggested alterations in the lipid A region of the lipopolysaccharide. The majority of lipid A species in the delta fabY mutant lacked a single secondary lauroyl group, resulting in hypoacylated lipid A. Adding exogenous fatty acids to the growth media restored the wild type antibiotic susceptibility profile and the wild-type lipid A fatty acid profile. We suggest that incorporation of hypoacylated lipid A species into the outer membrane contributes to the shift in the antibiotic susceptibility profile of the delta fabY mutant.

Item Type:	Article
Date Deposited:	26 Apr 2016 23:46
Last Modified:	26 Apr 2016 23:46
URI:	https://oak.novartis.com/id/eprint/10011