Fimsbactin siderophores from a South African marine sponge symbiont, marinomonas sp. PE14-40

dc.contributor.authorIkegwuoha, Nompumelelo Philile Praiseworth
dc.contributor.authorHanekom, Thea
dc.contributor.authorBooysen, Elzaan
dc.contributor.authorJason, Corbyn
dc.contributor.authorvan Zyl, Leonardo Joaquim
dc.contributor.authorTrindade, Marla
dc.date.accessioned2025-09-04T12:38:10Z
dc.date.available2025-09-04T12:38:10Z
dc.date.issued2025
dc.description.abstractLow iron levels in marine habitats necessitate the production of structurally diverse siderophores by many marine bacterial species for iron acquisition. Siderophores exhibit bioactivities ranging from chelation for iron reduction in hemochromatosis sufferers to antimicrobial activity either in their own right or when coupled to known antibiotics for targeted delivery or for molecular imaging. Thus, marine environments are a sought-after resource for novel siderophores that could have pharmaceutical or industrial application. The fimsbactins A-F (1–6) are mixed catechol-hydroxamate siderophores that have only been reported to be produced by Acinetobacter species with the fimsbactin biosynthetic gene clusters (BGCs) widespread among species within this genus. Here, we identified a putative fimsbactin BGC from an uncharacterized marine isolate, Marinomonas sp. PE14-40. Not only was the gene synteny not conserved when comparing the pathway from Marinomonas sp. PE14-40 to the fimsbactin BGC from Acinetobacter sp., but five of the core biosynthetic genes found in the canonical fimsbactin BGC are located elsewhere on the genome and do not form part of the core cluster in Marinomonas sp. PE14-40, with four of these, fbsBCDL, colocalized. Through ESI-MS/MS analysis of extracts from Marinomonas sp. PE14-40, the known fimsbactin analogues 1 and 6 were identified, as well as two new fimsbactin analogues, 7 and 8, containing a previously unreported L-lysine-derived hydroxamate moiety, N1-acetyl-N1-hydroxycadaverine. Feeding experiments using stable isotope-label L-lysine provided further evidence of the N1-acetyl-N1-hydroxycadaverine moiety in 7 and 8. The study demonstrates functional conservation in seemingly disparate biosynthetic pathways and enzyme promiscuity's role in producing structurally diverse compounds.
dc.identifier.citationIkegwuoha, N.P.P., Hanekom, T., Booysen, E., Jason, C., Parker‐Nance, S., Davies‐Coleman, M.T., van Zyl, L.J. and Trindade, M., 2025. Fimsbactin Siderophores From a South African Marine Sponge Symbiont, Marinomonas sp. PE 14‐40. Microbial Biotechnology, 18(5), p.e70155.
dc.identifier.issnhttps://doi.org/10.1111/1751-7915.70155
dc.identifier.urihttps://hdl.handle.net/10566/20832
dc.language.isoen
dc.publisherJohn Wiley and Sons Ltd
dc.subjectbiosynthetic gene cluster (BGC)
dc.subjectfimsbactin
dc.subjecthydroxamate
dc.subjectLC–MS
dc.subjectmarine bacteria
dc.titleFimsbactin siderophores from a South African marine sponge symbiont, marinomonas sp. PE14-40
dc.typeArticle

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