Enterobactin

Enterobactin is a catecholate siderophore that has been found in P. aeruginosa and has iron uptake activities.^1,2 It increases iron(III) uptake by P. aeruginosa grown in iron-deficient media supplemented with various concentrations of iron III chloride when used at a concentration of 4 µM.¹ Enterobactin (30 µM) increases the survival percentage of E. coli exposed to human lactoperoxidase and hydrogen peroxide.² In vivo, enterobactin secretion from E. coli is necessary for E. coli replication and invasion into the blood, as well as the spleen, liver, and lungs, of E. coli-infected chickens.³ Enterobactin iron-chelating and bacterial re-import activities are inhibited by albumin or neutrophil gelatinase-associated lipocalin (NGAL) binding and sequestration.^4,5

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1. Poole, K., Young, L., and Neshat, S. Enterobactin-mediated iron transport in Pseudomonas aeruginosa. J. Bacteriol. 172(12), 6991-6996 (1990).

2. Singh, V., Yeoh, B.S., Xiao, X., et al. Interplay between enterobactin, myeloperoxidase and lipocalin 2 regulates E. coli survival in the inflamed gut. Nat. Commun. 6, 7113 (2015).

3. Caza, M., Lépine, F., and Dozois, C.M. Secretion, but not overall synthesis, of catecholate siderophores contributes to virulence of extraintestinal pathogenic Escherichia coli. Mol. Microbiol. 80(1), 266-282 (2011).

4. Konopka, K., and Neilands, J.B. Effect of serum albumin on siderophore-mediated utilization of transferrin iron. Biochemistry 23(10), 2122-2127 (1984).

5. Goetz, D.H., Holmes, M.A., Borregaard, N., et al. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 10(5), 1033-1043 (2002).