Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN
Open accessAbstract
Members of a family of catecholate siderophores, called salmochelins, were isolated by reversed-phase HPLC from Salmonella enterica serotype Typhimurium and structurally characterized by Fourier transform ion cyclotron resonance-MSMS and GC-MS. The tentative structure of salmochelin 1 contained two 2,3- dihydroxybenzoylserine moieties bridged by a glucose residue, bound to the serine hydroxyl group of one moiety and the carboxylate of the second moiety. Salmochelin 2 contained in addition a second glucose residue linked to a third 2,3-dihydroxybenzoylserine moiety. Salmochelins were not produced by an iroBC mutant, which indicated that the IroB protein might be responsible for the glucosyl transfer predicted by sequence similarities to known glycosyltransferases. Uptake experiments with radiolabeled (55)Fe-salmochelin and growth promotion tests with salmochelins showed that the IroN outer membrane receptor, encoded in the iroA locus of S. enterica and uropathogenic Escherichia coli strains, was the main receptor for ferric salmochelin transport.
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Salmonella typhimurium secretes a heavily glycosylated siderophore, salmochelin, which is not recognized by lipocalin-2, making these bacteria unresponsive to this host defense strategy.
“However, pathogens are constantly evolving and adapting to host responses and have created modified siderophores, such as the heavily glycoslyated siderophore, salmochelin, secreted by Salmonella typhimurium, which is not recognized and targeted by lipocalin-2 thus making these bacteria unresponsive to this host defense strategy (Hantke et al., 2003).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Hantke et al., 2003
Some pathogens avoid lipocalin 2 by making modified stealth siderophores that it does not recognize.
“Some pathogens evade this defense through production of modified ‘stealth siderophores’, which are not recognized by lipocalin 2 52, 53.”
From Buried Treasure: Evolutionary Perspectives on Microbial Iron Piracy (2015) · cites this paper as [52]
Salmochelin is synthesized and mobilized by the Fur-regulated tandem iroN iroABCDE gene cluster.
“Salmochelin is synthesized and mobilized by the Fur‐regulated tandem iroN iroABCDE gene cluster. 130 , 131”
From The battle for iron in enteric infections (2020) · cites this paper as [130]
Salmonella produces salmochelin, a glucosylated form of enterobactin that avoids capture by LCN2.
“Demonstrating the strong selective pressure that LCN2 has placed on pathogenic bacteria, Salmonella also produces salmochelin, a glucosylated form of enterobactin that avoids capture by LCN2.”
From The battle for iron in enteric infections (2020) · cites this paper as [130]
Siderophores such as enterobactin are essential for iron acquisition by many bacterial pathogens including E. coli and Salmonella, coupled with siderophore receptor expression.
“Siderophores such as Enterobactin are essential for Fe acquisition by many bacterial pathogens such as E. coli or Salmonella, a strategy coupled to the expression of siderophore receptors by these pathogens (85, 86).”
From Innate Nutritional Immunity (2018) · cites this paper as [86]
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- Authors
- Hantke, K., Nicholson, G., Rabsch, W., & Winkelmann, G.
- Affiliations
- Robert Koch Institute (DE)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2003-03-24
- Volume
- 100
- Issue
- 7
- Pages
- 3677-3682
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC152981
- OpenAlex
- W2081256428
- Cited by
- 359
- References
- 23
- Citations by year
- 2026: 11 · 2025: 11 · 2024: 14 · 2023: 14 · 2022: 10 · 2021: 26 · 2020: 17 · 2019: 16 · 2018: 11 · 2017: 12 · 2016: 20 · 2015: 18 · 2014: 18 · 2013: 12 · 2012: 15
- FWCI
- 7.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Enterobacteriaceae and Cronobacter Research
- Keywords
- salmochelin, catecholate siderophores, Salmonella typhimurium, uropathogenic Escherichia coli, siderophore structure, iron acquisition
- MeSH terms
- Cell Membrane, Escherichia coli, Iron, Receptors, Cell Surface, Siderophores, Salmonella enterica, Spectrometry, Mass, Electrospray Ionization, Escherichia coli Proteins
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