Regulation of mammalian siderophore 2,5-DHBA in the innate immune response to infection
Open accessAbstract
Competition for iron influences host-pathogen interactions. Pathogens secrete small iron-binding moieties, siderophores, to acquire host iron. In response, the host secretes siderophore-binding proteins, such as lipocalin 24p3, which limit siderophore-mediated iron import into bacteria. Mammals produce 2,5-dihydroxy benzoic acid, a compound that resembles a bacterial siderophore. Our data suggest that bacteria use both mammalian and bacterial siderophores. In support of this idea, supplementation with mammalian siderophore enhances bacterial growth in vitro. In addition, mice lacking the mammalian siderophore resist E. coli infection. Finally, we show that the host responds to infection by suppressing siderophore synthesis while up-regulating lipocalin 24p3 expression via TLR signaling. Thus, reciprocal regulation of 24p3 and mammalian siderophore is a protective mechanism limiting microbial access to iron.
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A principal component of mammalian siderophores is 2,5-DHBA, whose synthesis requires BDH2.
“A principal component of mammalian siderophores is 2,5-DHBA whose synthesis requires BDH2 (for butyrate dehydrogenase type 2) (Liu et al., 2014).”
From Iron in infection and immunity (2020) · cites this paper as Liu et al., 2014
The consequent reduction of 2,5-DHBA levels may be an antimicrobial strategy.
“The consequent reduction of 2,5-DHBA levels may be an antimicrobial strategy because mice lacking BDH2 are more resistant to systemic infection with E. coli yet not with other relevant pathogens such as M. tuberculosis or S. aureus (Liu et al., 2014).”
From Iron in infection and immunity (2020) · cites this paper as Liu et al., 2014
Mice lacking BDH2 are more resistant to systemic infection with E. coli but not with M. tuberculosis or S. aureus.
“mice lacking BDH2 are more resistant to systemic infection with E. coli yet not with other relevant pathogens such as M. tuberculosis or S. aureus (Liu et al., 2014).”
From Iron in infection and immunity (2020) · cites this paper as Liu et al., 2014
Macrophages reduce synthesis of the siderophore 2,5-dihydroxybenzoic acid while increasing Lcn2 formation upon bacterial infection to limit microbial iron access.
“Recent evidence suggests that macrophages reduce the synthesis of the siderophore 2,5-dihydroxybenzoic acid while increasing Lcn2 formation upon bacterial infection to limit microbial iron access (213), the relevance of this finding in M. tuberculosis infection remains to be shown.”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [213]
E. coli can use the mammalian siderophore 2,5-DHBA as an iron source, and macrophages respond to bacterial challenge by downregulating 2,5-DHBA synthesis, leading to its depletion and enhanced resistance to E. coli infection.
“Of note, E. coli can use the mammalian siderophore, 2,5-dihydroxy-benzoic acid (2,5-DHBA) as Fe source [137].Accordingly, Mø respond to bacterial challenge by downregulating 2,5-DHBA synthesis, leading to 2,5-DHBA depletion and enhanced resistance to E. coli infection.”
From The Iron age of host–microbe interactions (2015) · cites this paper as [137]
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Li, L., Li, Y., Hao, Y., Yu, M., Xia, S., Wang, J., Ye, H., & Gao, Q. F. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27156972
- Authors
- Liu, Z., Reba, S., Chen, W.-D., Porwal, S. K., Boom, W. H., Petersen, R. B., Rojas, R., Viswanathan, R., & Devireddy, L.
- Affiliations
- Case Comprehensive Cancer Center (US)
- National Institutes of Health (US)
- Corresponding author
- Devireddy, L.
- ORCID
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2014-05-26
- Volume
- 211
- Issue
- 6
- Pages
- 1197-1213
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC4042634
- OpenAlex
- W2147688415
- Cited by
- 70
- References
- 62
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4 · 2023: 7 · 2022: 9 · 2021: 5 · 2020: 6 · 2019: 5 · 2018: 2 · 2017: 7 · 2016: 6 · 2015: 9 · 2014: 6
- FWCI
- 6.62
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R21AI099494, R01AI027243)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK081395)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- 2,5-dihydroxybenzoic acid, iron acquisition, host-pathogen interaction, innate immunity, Escherichia coli infection, Toll-like receptor signaling, iron competition, bacterial growth
- MeSH terms
- Lipocalin-2, Positive Regulatory Domain I-Binding Factor 1, Acute-Phase Proteins, Animals, Bacterial Infections, Bacterial Outer Membrane Proteins, Candida albicans, Candidiasis, Carrier Proteins, Cell Line, Enterobactin, Escherichia coli, Female, Gentisates, Hydroxybutyrate Dehydrogenase, Immunity, Innate, Male, Mice, Inbred C57BL, Mutation, Receptors, Cell Surface, Staphylococcus aureus, Transcription Factors, Immunoblotting, Oncogene Proteins, Siderophores, Mice, Knockout, Reverse Transcriptase Polymerase Chain Reaction, RNA Interference, Mice, Kaplan-Meier Estimate, Lipocalins
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