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PMID:24145528

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Citation

Six, DA, Yuan, Y, Leeds, JA and Meredith, TC (2014) Deletion of the β-acetoacetyl synthase FabY in Pseudomonas aeruginosa induces hypoacylation of lipopolysaccharide and increases antimicrobial susceptibility. Antimicrob. Agents Chemother. 58:153-61

Abstract

The β-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 ΔfabY mutant, which suggested alterations in the lipid A region of the lipopolysaccharide. The majority of lipid A species in the ΔfabY 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 ΔfabY mutant.

Links

PubMed PMC3910788 Online version:10.1128/AAC.01804-13

Keywords


Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

PSEAE:FABY

GO:0009245: lipid A biosynthetic process

ECO:0000315:

P

Figure 4: Spectra for wild-type and fabY-complemented mutant strain were similar, spectrum for fabY deficient strain was different

Table 2: almost every lipid A species in fabY deficient strain was modified with L-Ara4N

complete
CACAO 9515

PSEAE:FABY

involved_in

GO:0009245: lipid A biosynthetic process

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

See also

References

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