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Christian Hertweck

About Christian Hertweck:
No description specified

SEEK ID: https://data.chembiosys.de/people/4

Location:  Germany

Expertise: Not specified

Tools: Not specified

ORCID: Not specified

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Project positions

A1 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; A2 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; A3 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; A4 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; B05 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; Total ChemBioSys (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; B1 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; B2 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; B3 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; B4 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; B6 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; C1 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; C2 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; C3 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; C4 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; C5 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; INF (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; Z01 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute) ; Z02 (Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute)

Related items

C2

Are Plant Defenses Chemicals Commonly Sequestered and Metabolized by their Herbivores to Function as Infochemicals in Higher Trophic Level Interactions in Nature?

Public web page: Not specified

Total ChemBioSys
No description specified

Public web page: Not specified

INF

Information Infrastructure / Bio- and cheminformatics

Responsible for administration of https://cheminf.uni-jena.de/ - Maria Sorokina

Public web page: https://cheminf.uni-jena.de/

C1

Algicidal Bacteria in Plankton Communities: Resistance, Lysis and Heterotrophy

Public web page: Not specified

C3

Thiopeptide Signals in Actinomycete Communities

Public web page: Not specified

1 hidden item
Helper bacteria halt and disarm mushroom pathogens by linearizing structurally diverse cyclolipopeptides.
Total ChemBioSys, B1

Abstract (Expand)

The bacterial pathogen Pseudomonas tolaasii severely damages white button mushrooms by secretion of the pore-forming toxin tolaasin, the main virulence factor of brown blotch disease. Yet, fungus-associated … helper bacteria of the genus Mycetocola (Mycetocola tolaasinivorans and Mycetocola lacteus) may protect their host by an unknown detoxification mechanism. By a combination of metabolic profiling, imaging mass spectrometry, structure elucidation, and bioassays, we found that the helper bacteria inactivate tolaasin by linearizing the lipocyclopeptide. Furthermore, we found that Mycetocola spp. impair the dissemination of the pathogen by cleavage of the lactone ring of pseudodesmin. The role of pseudodesmin as a major swarming factor was corroborated by identification and inactivation of the corresponding biosynthetic gene cluster. Activity-guided fractionation of the Mycetocola proteome, matrix-assisted laser desorption/ionization (MALDI) analyses, and heterologous enzyme production identified the lactonase responsible for toxin cleavage. We revealed an antivirulence strategy in the context of a tripartite interaction that has high ecological and agricultural relevance.

Authors: R. Hermenau, S. Kugel, A. J. Komor, C. Hertweck

Date Published: 31st Aug 2020

Publication Type: Not specified

Food-Poisoning Bacteria Employ a Citrate Synthase and a Type II NRPS To Synthesize Bolaamphiphilic Lipopeptide Antibiotics.
Total ChemBioSys, B1

Abstract (Expand)

Mining the genome of the food-spoiling bacterium Burkholderia gladioli pv. cocovenenans revealed five nonribosomal peptide synthetase (NRPS) gene clusters, including an orphan gene locus (bol). Gene … inactivation and metabolic profiling linked the bol gene cluster to novel bolaamphiphilic lipopeptides with antimycobacterial activity. A combination of chemical analysis and bioinformatics elucidated the structures of bolagladin A and B, lipocyclopeptides featuring an unusual dehydro-beta-alanine enamide linker fused to an unprecedented tricarboxylic fatty acid tail. Through a series of targeted gene deletions, we proved the involvement of a designated citrate synthase (CS), priming ketosynthases III (KS III), a type II NRPS, including a novel desaturase for enamide formation, and a multimodular NRPS in generating the cyclopeptide. Network analyses revealed the evolutionary origin of the CS and identified cryptic CS/NRPS gene loci in various bacterial genomes.

Authors: B. Dose, C. Ross, S. P. Niehs, K. Scherlach, J. P. Bauer, C. Hertweck

Date Published: 11th Aug 2020

Publication Type: Not specified

Insect-Associated Bacteria Assemble the Antifungal Butenolide Gladiofungin by Non-Canonical Polyketide Chain Termination.
Total ChemBioSys, B1

Abstract (Expand)

Genome mining of one of the protective symbionts ( Burkholderia gladioli ) of the invasive beetle Lagria villosa revealed a cryptic gene cluster coding for the biosynthesis of a novel antifungal … polyketide with a glutarimide pharmacophore. Targeted gene inactivation, metabolic profiling and bioassays led to the discovery of the gladiofungins as yet overlooked components of the antimicrobial armory of the beetle symbiont, specifically against the entomopathogenic fungus Purpureocillium lilacinum . By mutational analyses, isotope labeling and in silico analyses of the modular polyketide synthase, we found that the rare butenolide moiety of gladiofungins derives from an unprecedented polyketide chain termination reaction involving a glycerol-derived C3 building block. The key role of an A-factor synthase (AfsA)-like offloading domain was corroborated by CRISPR-Cas-mediated gene editing, which facilitated the precise excision within a PKS domain.

Authors: S. P. Niehs, J. Kumpfmuller, B. Dose, R. F. Little, K. Ishida, L. V. Florez, M. Kaltenpoth, C. Hertweck

Date Published: 26th Jun 2020

Publication Type: Not specified

Mining Symbionts of a Spider-Transmitted Fungus Illuminates Uncharted Biosynthetic Pathways to Cytotoxic Benzolactones
Total ChemBioSys, B1

Abstract (Expand)

A spider-transmitted fungus (Rhizopus microspo- rus) that was isolated from necrotic human tissue was found to harbor endofungal bacteria (Burkholderia sp.). Metabolic profiling of the symbionts revealed … a complex of cytotoxic agents (necroximes). Their structures were characterized as oxime-substituted benzolactone enamides with a peptidic side chain. The potently cytotoxic necroximes are also formed in symbiosis with the fungal host and could have contributed to the necrosis. Genome sequencing and computational analyses revealed a novel modular PKS/NRPS assembly line equipped with several non-canonical domains. Based on gene-deletion mutants, we propose a biosynthetic model for bacterial benzolactones. We identified specific traits that serve as genetic handles to find related salicylate macrolide pathways (lobata- mide, oximidine, apicularen) in various other bacterial genera. Knowledge of the biosynthetic pathway enables biosynthetic engineering and genome-mining approaches.

Authors: Sarah Niehs, Benjamin Dose, Sophie Richter, Sacha J. Pidot, Timothy P. Stinear, Hans-Martin Dahse, Christian Hertweck

Date Published: 10th Feb 2020

Publication Type: Not specified

Genome Mining Reveals Endopyrroles from a Nonribosomal Peptide Assembly Line Triggered in Fungal-Bacterial Symbiosis
Total ChemBioSys, B1

Abstract (Expand)

The bacterial endosymbiont (Burkholderia rhizoxinica) of the rice seedling blight fungus (Rhizopus microsporus) harbors a large number of cryptic biosynthesis gene clusters. Genome mining and sequence … similarity networks based on an encoded nonribosomal peptide assembly line and the associated pyrrole- forming enzymes in the symbiont indicated that the encoded metabolites are unique among a large number of tentative pyrrole natural products in diverse and unrelated bacterial phyla. By performing comparative metabolic pro fi ling using a mutant generated with an improved pheS Burkholderia counterselection marker, we found that the symbionts ’ biosynthetic pathway is mainly activated under salt stress and exclusively in symbiosis with the fungal host. The cryptic metabolites were fully characterized as novel pyrrole-substituted depsipeptides (endopyrroles). A broader survey showed that endopyrrole production is a hallmark of geographically distant endofungal bacteria, which produce the peptides solely under symbiotic conditions.

Authors: Sarah Niehs, Benjamin Dose, Kirstin Scherlach, Sacha J. Pidot, Timothy P. Stinear, Christian Hertweck

Date Published: 8th Jul 2019

Publication Type: Not specified

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