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Inverse stable isotope labeling (InverSIL) links predicted catecholate siderophore gene clusters to their products in diverse bacteria
Open accessPublished version of a preprint
Abstract
Bacteria produce high-affinity, iron-chelating secondary metabolites called siderophores to access insoluble Fe(III) in their environments. Genome mining has revealed many predicted siderophore biosynthetic gene clusters (BGCs) in bacterial genomes; however, the structures of their siderophore products remain mostly undetermined. This limits our molecular-level understanding of how bacteria acquire iron. Here, we apply inverse stable isotope labeling (InverSIL) to rapidly connect predicted siderophore BGCs to their products. With InverSIL, bacteria are grown on 13 C-substituted carbon sources and then fed predicted biosynthetic precursors at their natural isotopic abundance to identify BGC products by mass spectrometry, removing issues with the availability of isotopically substituted precursors. We use InverSIL to determine the structures of the siderophore products of predicted BGCs from the methylotrophic genera Methylophilus and Methylorubrum , as well as the siderophores produced by the opportunistic pathogen Chromobacterium violaceum , which were previously shown to be essential for virulence yet remained structurally uncharacterized. We next use this approach to reveal the unexpected production of enterobactin by the genera Kushneria and Paracoccus , which was difficult to predict from genome sequences due to the distributed nature of the biosynthetic genes within the genomes. Finally, we use InverSIL to discover new siderophores, the cellulochelins, from the cellulose-degrading plant symbiont Cellulomonas sp. strain Leaf334. These findings demonstrate the utility of InverSIL for functional BGC characterization and expand our molecular understanding of bacterial iron acquisition strategies. IMPORTANCE: Iron acquisition is important for microbial survival, and bacteria produce secondary metabolites called siderophores to scavenge iron from the environment. While bacterial genome sequences show many predicted genes for making siderophores, most remain unlinked to their metabolic products. Understanding which siderophores bacteria produce is critical for elucidating microbial iron acquisition strategies, ecological interactions, and potential roles in host-microbe interactions. Here, we demonstrate how inverse stable isotope labeling (InverSIL) can rapidly link predicted siderophore gene clusters to their corresponding metabolites. By applying InverSIL to diverse bacterial strains, we validate known siderophore products and uncover unexpected products, highlighting the limitations of current in silico predictions. This study highlights the value of combining experimental approaches with genome mining to advance our understanding of how bacteria acquire iron from their environment.
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![Fig 1 Inverse stable isotope labeling (InverSIL) for linking predicted catecholate siderophore BGCs with their products. (A) Enzymes responsible for the biosynthesis of catechols 3,4-DHB and 2,3-DHB. (B) Scheme of an InverSIL experiment: (1) genome mining for DHB biosynthesis genes; (2) addition of 2,3-DHB at its natural isotopic abundance to a bacterial culture grown on a 13C-substituted carbon source [indicated as (13C)]; (3) high-resolution mass spectrometry to detect DHB incorporation; and (4) identification of the siderophore aided by MS2 fragmentation. The siderophore enterobactin is shown as an example.](/paper-figures/bcf01438ad9e49aa99bf52bf3b456a63/inverse-stable-isotope-labeling-inversil-links-predicted-catecholate-siderophore-figure-1.jpg)
![Fig 2 Using InverSIL to link an NRPS-dependent catecholate siderophore BGC with its product, cepaciachelin. (A) Comparison of an NRPS-dependent BGC in Methylophilus sp. strain 5, Burkholderia ambifaria BAA-244, and Chromobacterium violaceum CV017. Numbers indicate percent amino acid identity. Arrow colors indicate predicted 2,3-DHB biosynthesis genes (orange), predicted NRPS genes (green), and other genes (gray). Circles indicate predicted NRPS domains C (condensation domain), A (adenylation domain), CP (acyl-carrier protein), and TE (thioesterase domain), with the predicted adenylation domain substrates listed below. (B) Overlaid mass spectra of Methylophilus sp. strain 5 supernatant extract showing incorporation of two 2,3-DHB units into a metabolite with the same high-resolution mass and carbon count as cepaciachelin. (C) Structure of cepaciachelin showing MS2 fragments from different InverSIL conditions. The colors match the growth conditions indicated in panel B. (D) Extracted ion chromatograms of supernatant extracts of B. ambifaria BAA-244, Methylophilus sp. strain 5, and Chromobacterium violaceum CV017 for m/z 489.2340, corresponding to the [M+H]+ of cepaciachelin. Mass tolerance <5 ppm.](/paper-figures/1ed93fa80ab54bc2ad7e12a470a97b3d/inverse-stable-isotope-labeling-inversil-links-predicted-catecholate-siderophore-figure-2.jpg)
![Fig 3 Using InverSIL to link a NIS catecholate siderophore BGC with its product, rhodopetrobactin B. (A) Comparison of a NIS siderophore BGC in Methylorubrum extorquens PA1 and Rhodopseudomonas palustris CGA009. Numbers indicate percent amino acid identity. Arrow colors indicate predicted iucA/iucC genes (red), a conserved hypothetical protein in petrobactin biosynthesis (yellow), and a predicted asbF gene (orange). (B) Overlaid mass spectra of M. extorquens PA1 supernatant extract showing incorporation of two 3,4-DHB units into a metabolite with the same high-resolution mass and carbon count as rhodopetrobactin B. (C) Structure of rhodopetrobactin B showing MS2 fragments from different InverSIL conditions. The colors match the growth conditions indicated in panel B. (D) Extracted ion chromatograms of supernatant extracts of R. palustris CGA009 and M. extorquens PA1 for m/z 831.4228, corresponding to the [M+H]+ of rhodopetrobactin B. Mass tolerance < 5 ppm.](/paper-figures/f16dceee10e8472ab03c8be1c09562ff/inverse-stable-isotope-labeling-inversil-links-predicted-catecholate-siderophore-figure-3.jpg)

![Fig 5 Non-colocalized enterobactin BGCs in Kushneria konosiri JCM16805 and Paracoccus denitrificans PD1222. (A) Comparison of a predicted dhb operon, NIS BGC, and distant entF gene in K. konosiri JCM16805 with the enterobactin BGC in E. coli MG1655 and another non-colocalized enterobactin BGC in Paracoccus denitrificans PD1222. Numbers indicate percent amino acid identity. Arrow colors indicate predicted 2,3-DHB biosynthesis genes (orange), predicted iucA/iucC genes (red), predicted NRPS genes (green), and other genes (gray). Circles indicate predicted NRPS domains C (condensation domain), A (adenylation domain), CP (acyl-carrier protein), and TE (thioesterase domain), with the predicted adenylation domain substrates listed below. (B) Overlaid mass spectra of K. konosiri JCM16805 supernatant extract showing incorporation of three 2,3-DHB units into a metabolite with the same high-resolution mass and carbon count as enterobactin. (C) Structure of enterobactin showing MS2 fragments from different InverSIL conditions. The colors match the growth conditions indicated in panel B. (D) Extracted ion chromatograms of supernatant extracts from K. konosiri JCM 16805, P. denitrificans PD1222, and E. coli MG1655 for m/z 670.1502, corresponding to the [M+H]+ of enterobactin. Mass tolerance < 5 ppm.](/paper-figures/be868009900542a490b27b7a96b3dee6/inverse-stable-isotope-labeling-inversil-links-predicted-catecholate-siderophore-figure-5.jpg)

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Citations
Cites
Iron in infection and immunity
Cassat, J. E., & Skaar, E. P. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.04.010 · Cited by 1,214
Bacterial siderophores in community and host interactions
Kramer, J., Özkaya, Ö., & Kümmerli, R. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0284-4 · Cited by 998
Solution equilibria of enterobactin and metal-enterobactin complexes
Loomis, L. D., & Raymond, K. N. (1991) · Inorganic Chemistry · doi:10.1021/ic00005a008 · Cited by 321
ChelomEx: Isotope-Assisted Discovery of Metal Chelates in Complex Media Using High-Resolution LC-MS
Baars, O., Morel, F. M. M., & Perlman, D. H. (2014) · Analytical Chemistry · doi:10.1021/ac503000e · Cited by 57
Research works printed but not linked: 65
- 10.3389/fmicb.2012.00383 · DOI
- 10.1039/b906679a · DOI · Paper page
- 10.1038/s41579-024-01090-6 · DOI
- 10.1007/s00775-018-1617-x · DOI
- 10.1080/10409238.2025.2476476 · DOI
- 10.1016/bs.mie.2024.06.007 · DOI
- 10.1016/j.copbio.2022.102757 · DOI
- 10.1093/nar/gkaf334 · DOI
- 10.1038/s41467-020-19986-1 · DOI
- 10.7554/eLife.109154 · DOI
- 10.1021/acschembio.5b00801 · DOI
- 10.1016/j.chembiol.2010.01.011 · DOI
- 10.1021/ja1109453 · DOI
- 10.1038/s41557-021-00803-1 · DOI · Paper page
- 10.1073/pnas.1516878112 · DOI
- 10.1016/j.chembiol.2006.11.007 · DOI
- 10.1038/s41589-021-00949-6 · DOI · Paper page
- 10.1128/mbio.01999-23 · DOI
- 10.1016/bs.mie.2024.06.005 · DOI
- 10.1002/anie.200501942 · DOI
- 10.1021/np060409n · DOI
- 10.1039/c7mt00111h · DOI
- 10.1007/s00775-002-0375-x · DOI
- 10.1099/00221287-144-7-1747 · DOI
- 10.1039/D3NP00037K · DOI
- 10.1074/jbc.M009140200 · DOI
- 10.1073/pnas.0808118105 · DOI
- 10.1021/bi801876q · DOI
- 10.1021/acs.analchem.4c03528 · DOI
- 10.1073/pnas.2507323122 · DOI
- 10.1007/s00253-015-6713-z · DOI
- 10.1128/mBio.02430-17 · DOI
- 10.1002/mbo3.347 · DOI
- 10.1128/AEM.03160-15 · DOI
- 10.1371/journal.pone.0102458 · DOI
- 10.1134/S0026261711040047 · DOI
- 10.1128/JCM.03561-13 · DOI
- 10.1073/pnas.2322096121 · DOI
- 10.1111/1462-2920.14078 · DOI
- 10.1007/s00248-010-9725-3 · DOI
- 10.1128/JB.01009-12 · DOI
- 10.1128/IAI.00577-19 · DOI
- 10.1002/1873-3468.14539 · DOI
- 10.1021/np200126z · DOI
- 10.1128/JB.180.17.4435-4441.1998 · DOI · Paper page
- 10.1128/genomeA.00080-16 · DOI
- 10.1099/ijsem.0.002897 · DOI
- 10.3390/microorganisms11122910 · DOI
- 10.1186/s40793-018-0324-0 · DOI
- 10.1073/pnas.0630018100 · DOI · Paper page
- 10.1007/BF00447011 · DOI
- 10.1016/S0040-4039(01)86717-4 · DOI
- 10.1042/bj1460191 · DOI
- 10.1073/pnas.1401734111 · DOI
- 10.1099/00221287-148-2-353 · DOI
- 10.1038/s41564-021-00997-7 · DOI
- 10.1073/pnas.0805451105 · DOI
- 10.1039/c8mt00252e · DOI
- 10.1021/acschembio.7b00597 · DOI
- 10.1099/00221287-128-9-1959 · DOI
- 10.1016/j.tim.2025.05.002 · DOI
- 10.1128/JB.06817-11 · DOI
- 10.1093/nar/gkr1044 · DOI
- 10.1186/s12859-023-05311-2 · DOI
- 10.1016/0003-2697(87)90612-9 · DOI
Metadata
- Authors
- Robes, J. M. D., Liebergesell, T. C. E., Medvedeva, V. P., & Puri, A. W.
- Affiliations
- University of Utah (US)
- University of California, Irvine (US)
- Corresponding author
- Puri, Aaron W.
- Venue
- mBio
- Publisher
- American Society for Microbiology
- Published
- 2026-06-10
- Volume
- 17
- Issue
- 6
- Pages
- e0339125-e0339125
- ISSN
- 2150-7511 (ISSN-L)
- PMC
- PMC13251462
- OpenAlex
- W4415946583
- Cited by
- 0
- References
- 4
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- mBio (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (submittedVersion, cc-by-nc)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institute of General Medical Sciences (R35 GM147018)
- Simons Foundation Early Career Investigator in Aquatic Microbial Ecology and Evolution (00006628)
- NIH training (T32 AI055434)
- Topics
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Microbial Metabolism and Applications
- Keywords
- siderophores, iron acquisition, enterobactin, Methylobacterium, Methylophilus, Chromobacterium violaceum, Paracoccus, Cellulomonas, bacterial secondary metabolites
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- CoChat. (2026). Citation check: Inverse stable isotope labeling (InverSIL) links predicted catecholate siderophore gene clusters to their products in diverse bacteria. https://app.cochat.ai/papers/10.1128/mbio.03391-25
- The paper
- Robes, J. M. D., Liebergesell, T. C. E., Medvedeva, V. P., & Puri, A. W. (2026). Inverse stable isotope labeling (InverSIL) links predicted catecholate siderophore gene clusters to their products in diverse bacteria. mBio. https://doi.org/10.1128/mbio.03391-25