Two Types of Threonine-Tagged Lipopeptides Synergize in Host Colonization by Pathogenic Burkholderia Species
| Autor: | Emilia Oueis, Evgeni V Bratovanov, Tawatchai Thongkongkaew, Rolf Müller, Youming Zhang, Christian Hertweck, Kirsten Harmrolfs, Nestor Zaburannyi, Kirstin Scherlach, Wei Ding, Marı A Garcı A-Altares |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Crops Agricultural Threonine Burkholderia gladioli Burkholderia Proton Magnetic Resonance Spectroscopy 01 natural sciences Biochemistry Genome Mass Spectrometry Microbiology 03 medical and health sciences chemistry.chemical_compound Lipopeptides Nonribosomal peptide Burkholderia glumae Peptide Synthases Pathogen 2. Zero hunger chemistry.chemical_classification biology 010405 organic chemistry fungi food and beverages Lipopeptide Oryza General Medicine biology.organism_classification Orphan gene 0104 chemical sciences 030104 developmental biology chemistry Multigene Family Host-Pathogen Interactions Molecular Medicine Heterologous expression Agaricales Genome Bacterial |
| Zdroj: | ACS chemical biology. 13(5) |
| ISSN: | 1554-8937 |
| Popis: | Bacterial infections of agriculturally important mushrooms and plants pose a major threat to human food sources worldwide. However, structures of chemical mediators required by the pathogen for host colonization and infection remain elusive in most cases. Here, we report two types of threonine-tagged lipopeptides conserved among mushroom and rice pathogenic Burkholderia species that facilitate bacterial infection of hosts. Genome mining, metabolic profiling of infected mushrooms, and heterologous expression of orphan gene clusters allowed the discovery of these unprecedented metabolites in the mushroom pathogen Burkholderia gladioli (haereogladin, burriogladin) and the plant pathogen Burkholderia glumae (haereoglumin and burrioglumin). Through targeted gene deletions, the molecular basis of lipopeptide biosynthesis by nonribosomal peptide synthetases was revealed. Surprisingly, both types of lipopeptides feature unusual threonine tags, which yield longer peptide backbones than one would expect based on the canonical colinearity of the NRPS assembly lines. Both peptides play an indirect role in host infection as biosurfactants that enable host colonization by mediating swarming and biofilm formation abilities. Moreover, MALDI imaging mass spectrometry was applied to investigate the biological role of the lipopeptides. Our results shed light on conserved mechanisms that mushroom and plant pathogenic bacteria utilize for host infection and expand current knowledge on bacterial virulence factors that may represent a new starting point for the targeted development of crop protection measures in the future. |
| Databáze: | OpenAIRE |
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