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

project_administrator
help Their tags

This person has not yet tagged anything.

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

B05

Role of Basidiomycete Small Molecules on Habitat-sharing Microbes

Public web page: http://www.chembiosys.de/en/research/projects/project-b05.html

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/

B2

Mechanisms of Bacteria-triggered Activation of Fungal Silent Gene Clusters and Impact of Produced Compounds on Microorganisms

Public web page: Not specified

Z02

Raman Based Analysis of Natural Products in Complex Biosystems

Public web page: Not specified

B1

Cryptic Mediators at the Bacterial-Fungal Interface: Mushroom Soft Rot Diseases as Infection Model

Public web page: Not specified

2 hidden items
1 hidden item
Multimodal Molecular Imaging and Identification of Bacterial Toxins Causing Mushroom Soft Rot and Cavity Disease
Z02

Abstract (Expand)

Soft rot disease of edible mushrooms leads to rapid degeneration of fungal tissue and thus severely affects farming productivity worldwide. The bacterial mushroom pathogen Burkholderia gladioli pv. … agaricicola has been identified as the cause. Yet, little is known about the molecular basis, the spatial distribution and the biological role of antifungal agents and toxins involved in this infectious disease. We combine genome mining, metabolic profiling, MALDI-Imaging and UV Raman spectroscopy, to detect, identify and visualize a complex of chemical mediators and toxins produced by the pathogen during the infection process, including toxoflavin, caryoynencin, and sinapigladioside. Furthermore, targeted gene knockouts and in vitro assays link antifungal agents to prevalent symptoms of soft rot, mushroom browning, and impaired mycelium growth. Comparisons of related pathogenic, mutualistic and environmental Burkholderia spp. indicate that the arsenal of antifungal agents may have paved the way for ancestral bacteria to colonize niches where frequent, antagonistic interactions with fungi occur. Our findings not only demonstrate the power of label-free, in vivo detection of polyyne virulence factors by Raman imaging, but may also inspire new approaches to disease control.

Authors: Benjamin Dose, Tawatchai Thongkongkaew, David Zopf, Hak Joong Kim, Evgeni V. Bratovanov, María García-Altares Pérez, Kirstin Scherlach, Jana Krabbe, Claudia Ross, Ron Hermenau, Sarah P. Niehs, Anja Silge, Julian Hniopek, Michael Schmitt, Jürgen Popp, Christian Hertweck

Date Published: 7th Jul 2021

Publication Type: Journal

Biosynthesis of Sinapigladioside, an Antifungal Isothiocyanate from Burkholderia Symbionts.
Total ChemBioSys, B1

Abstract (Expand)

Sinapigladioside is a rare isothiocyanate-bearing natural product from beetle-associated bacteria ( Burkholderia gladioli ) that may protect the beetle offspring against entomopathogenic fungi. The … biosynthetic origin of sinapigladioside has been elusive, and little is known about bacterial isothiocyanate biosynthesis in general. On the basis of stable-isotope labeling, bioinformatics, and mutagenesis we identified the sinapigladioside biosynthesis gene cluster in the symbiont and found that an isonitrile synthase plays a key role in the biosynthetic pathway. Genome mining and network analyses indicate that related gene clusters are distributed across various bacterial phyla including producers of both nitriles and isothiocyanates. Our findings support a model for bacterial isothiocyanate biosynthesis by sulfur transfer onto isonitrile precursors.

Authors: B. Dose, S. P. Niehs, K. Scherlach, S. Shahda, L. V. Florez, M. Kaltenpoth, C. Hertweck

Date Published: 19th Mar 2021

Publication Type: Journal

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

11 hidden items
Powered by
 (v.1.11.0)
About | ChemBioSys | Funding and Programmes | Credits
Copyright © 2008 - 2021 The University of Manchester and HITS gGmbH