Salmochelin, the long-overlooked catecholate siderophore of Salmonella
Salmochelin is a C-glucosylated enterobactin produced by Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains. It was the first glucosylated siderophore described. The glucosylation has been interpreted as a bacterial evasion mechanism against the mammalian catecholate siderophore-binding protein siderocalin (NGAL-lipocalin). The synthesis, excretion, and uptake of salmochelin requires five genes, iroBCDEN, and also the enterobactin biosynthesis and utilization system. Some salmochelin-producing strains also secrete microcins, which possess a C-terminal, linear glucosyl-enterobactin moiety. These microcins recognize the catecholate siderophore receptors IroN, Cir, Fiu, and FepA, and may inhibit the growth of competitors for catecholate siderophores.
KeywordsSalmochelin Iron transport Siderocalin Salmonella C-glucosylation Microcin E492
- Fischbach MA, Lin H, Zhou L, Yu Y, Abergel RJ, Liu DR, Raymond KN, Wanner BL, Strong RK, Walsh CT, Aderem A, Smith KD (2006) The pathogen-associated iroA gene cluster mediates bacterial evasion of lipocalin 2. Proc Natl Acad Sci USA 103:16502–16507. doi:10.1073/pnas.0604636103 PubMedCrossRefGoogle Scholar
- Fu JM (1985) The structure elucidation of methyl pacifarinic acid. Thesis, University of Illinois at ChicagoGoogle Scholar
- Thomas X, Destoumieux-Garzon D, Peduzzi J, Afonso C, Blond A, Birlirakis N, Goulard C, Dubost L, Thai R, Tabet JC, Rebuffat S (2004) Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity. J Biol Chem 279:28233–28242. doi:10.1074/jbc.M400228200 PubMedCrossRefGoogle Scholar
- Wawszkiewicz EJ (1975) Riddle of pacifarins. In: Schlesinger MJ (ed) Microbiology—1974. ASM, Washington D.C., pp 299–305Google Scholar