title: Plasticity of the malleobactin pathway and its impact on siderophore action in human pathogenic bacteria.
abstract: The human pathogenic bacteria Burkholderia mallei, Burkholderia pseudomallei, and Burkholderia thailandensis harbor a highly conserved gene cluster coding for the biosynthesis of the long sought-after malleobactins. Four new, unexpected congeners of the malleobactin family that were isolated and fully characterized in this study feature unusual deviations from the parent, ornibactin-like architecture. Thus, the malleobactin non-ribosomal peptide synthetase (NRPS) has a rare flexibility that yields diverse peptide backbones, of which one candidate confers pronounced siderophore activity (EC50: 8.4 μM, CAS assay). These findings not only unveil a highly diverse assembly line but also are an important addition to the knowledgebase of the pathogens' metabolomes.
authors: Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Beutenbergstr. 11a, 07745 Jena (Germany).
authors: Jakob
authors: J
authors: Franke
authors: Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Beutenbergstr. 11a, 07745 Jena (Germany).
authors: Keishi
authors: K
authors: Ishida
authors: Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI), Beutenbergstr. 11a, 07745 Jena (Germany). Christian.Hertweck@hki-jena.de.|Chair of Natural Product Chemistry, Friedrich Schiller University, Jena (Germany). Christian.Hertweck@hki-jena.de.
authors: Christian
authors: C
authors: Hertweck
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism*; D019117:Burkholderia / Q000737:chemistry / Q000378:metabolism*; D019121:Burkholderia Infections / Q000382:microbiology*; D006801:Humans; D055442:Metabolome; D017262:Siderophores / Q000032:analysis / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D017262:Siderophores
keywords: Burkholderia; chelators; iron; non-ribosomal peptides; siderophores