0000000000160865

AUTHOR

Luis Antelo

Omphalotins E-I, Five Oxidatively Modified Nematicidal Cyclopeptides fromOmphalotus olearius

Omphalotins E–I, oxidatively modified cyclic dodecapeptides, were isolated from mycelial extracts of the basidiomycete Omphalotus olearius, and their structures were determined by NMR spectroscopic and MS methods. Four of the five omphalotins contained an unprecedented N-hydroxylated tricyclic tryptophan derivative. All compounds exhibited strong and selective nematicidal activity against the plant pathogen Meloidogyne incognita with LD90 values between 2 and 5 μg mL–1. Cytotoxic activities were not detected up to 50 μg mL–1. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)

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Magnaporthe oryzae as an expression host for the production of the unspecific peroxygenase AaeUPO from the basidiomycete Agrocybe aegerita.

Abstract The filamentous fungus Magnaporthe oryzae has the potential to be developed as an alternative platform organism for the heterologous production of industrially important enzymes. M. oryzae is easy to handle, fast‐growing and unlike yeast, posttranslational modifications like N‐glycosylations are similar to the human organism. Here, we established M. oryzae as a host for the expression of the unspecific peroxygenase from the basidiomycete Agrocybe aegerita (AaeUPO). Note, UPOs are attractive biocatalysts for selective oxyfunctionalization of non‐activated carbon‐hydrogen bonds. To improve and simplify the isolation of AaeUPO in M. oryzae, we fused a Magnaporthe signal peptide for pr…

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A new member of the fusaricidin family – structure elucidation and synthesis of fusaricidin E

Two hitherto unknown fusaricidins were obtained from fermentation broths of three Paenibacillus strains. After structure elucidation based on tandem mass spectrometry and NMR spectroscopy, fusaricidin E was synthesized to confirm the structure and the suggested stereochemistry. The synthesis was based on a new strategy which includes an efficient access to the 15-guanidino-3-hydroxypentadecanoyl (GHPD) side chain from erucamide.

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Rapid adaptation of signaling networks in the fungal pathogen Magnaporthe oryzae

Abstract Background One fundamental question in biology is how the evolution of eukaryotic signaling networks has taken place. “Loss of function” (lof) mutants from components of the high osmolarity glycerol (HOG) signaling pathway in the filamentous fungus Magnaporthe oryzae are viable, but impaired in osmoregulation. Results After long-term cultivation upon high osmolarity, stable individuals with reestablished osmoregulation capacity arise independently from each of the mutants with inactivated HOG pathway. This phenomenon is extremely reproducible and occurs only in osmosensitive mutants related to the HOG pathway – not in other osmosensitive Magnaporthe mutants. The major compatible so…

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MOESM7 of Rapid adaptation of signaling networks in the fungal pathogen Magnaporthe oryzae

Additional file 7: Figure S6. qPCR results of selected genes. qRT-PCR analysis of putative genes in MoWT, the “lof” mutants ΔMohog1 and ΔMohog1(adapted). The M. oryzae cultures were grown for 96 h in CM at 26 °C and 100 rpm. Each of the cultures was separated into two samples, one mixed with 0.5 M KCl and one untreated control further grown in CM at 26 °C and 100 rpm). Samples were taken after 25 min. The RNA was isolated from the mycelium samples and the results of transcript abundance given relative to quantification in the MoWT untreated control. Three biological replicates were used of each.

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Native Electrospray-based Metabolomics Enables the Detection of Metal-binding Compounds

AbstractMetals are essential for the molecular machineries of life, and microbes have evolved a variety of small molecules to acquire, compete for, and utilize metals. Systematic methods for the discovery of metal-small molecule complexes from biological samples are limited. Here we describe a two-step native electrospray ionization mass spectrometry method, in which double-barrel post-column metal-infusion and pH adjustment is combined with ion identity molecular networking, a rule-based informatics workflow. This method can be used to identify metal-binding compounds in complex samples based on defined mass (m/z) offsets of ion features with the same chromatographic profiles. As this nati…

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MOESM3 of Rapid adaptation of signaling networks in the fungal pathogen Magnaporthe oryzae

Additional file 3: Figure S2. Investigation of the â adaptation-frequencyâ in Magnaporthe oryzae mutants with inactivated components of the HOG signaling cascade.

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MOESM4 of Rapid adaptation of signaling networks in the fungal pathogen Magnaporthe oryzae

Additional file 4: Figure S3. Mycelium dry weight of the Magnaporthe oryzae wildtype strain, mutants with inactivated components of the HOG signaling cascade and the “adapted” strains after growth in liquid culture upon sorbitol-stress. The fungal colonies were grown in 250 ml complete medium inclusive 1,5 M sorbitol for 6 d at 26 °C and 120 rpm. Error bars represent the standard deviation of three biological replicates of each strain.

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MOESM6 of Rapid adaptation of signaling networks in the fungal pathogen Magnaporthe oryzae

Additional file 6: Figure S5. VENN diagram of putative structural variations in promotor [A] and in coding sequences (CDS) [B] within the genome of ΔMohog1, ΔMohog1(adapted) and ΔMopbs2(adapted). Numbers in the intersection regions represent overlapping SNPs among the strains. Numbers in parentheses show the corresponding relative percentage of genes harbouring the SNPs.

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ChemInform Abstract: Omphalotins E-I, Five Oxidatively Modified Nematicidal Cyclopeptides from Omphalotus olearius.

Omphalotins E–I, oxidatively modified cyclic dodecapeptides, were isolated from mycelial extracts of the basidiomycete Omphalotus olearius, and their structures were determined by NMR spectroscopic and MS methods. Four of the five omphalotins contained an unprecedented N-hydroxylated tricyclic tryptophan derivative. All compounds exhibited strong and selective nematicidal activity against the plant pathogen Meloidogyne incognita with LD90 values between 2 and 5 μg mL–1. Cytotoxic activities were not detected up to 50 μg mL–1. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)

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MOESM5 of Rapid adaptation of signaling networks in the fungal pathogen Magnaporthe oryzae

Additional file 5: Figure S4. Pathogenicity assay of the MoWT, the lof mutants and the â adaptedâ strains. The plant infection assays were carried out as described in experimental procedures. The error bars represent the standard deviation of three experiments with three replicates each.

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MOESM2 of Rapid adaptation of signaling networks in the fungal pathogen Magnaporthe oryzae

Additional file 2: Figure S1. Schematic presentation and verification of the MoWT, the lof-mutants and the adapted strains by southern hybridization within the Magnaporthe oryzae genome. Southern blot analysis of gene deletion/disruption mutants in M. oryzae with gene specific probes. Genomic DNA of M. oryzae strain 70â 15 and the mutants was isolated and restricted with restriction enzymes. The probes which we used for hybridization with the genomic DNA of the wildtype strain and the corresponding mutant strains were always identical.

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Identification of factors involved in dimorphism and pathogenicity of Zymoseptoria tritici

A forward genetics approach was applied in order to investigate the molecular basis of morphological transition in the wheat pathogenic fungus Zymoseptoria tritici. Z. tritici is a dimorphic plant pathogen displaying environmentally regulated morphogenetic transition between yeast-like and hyphal growth. Considering the infection mode of Z. tritici, the switching to hyphal growth is essential for pathogenicity allowing the fungus the host invasion through natural openings like stomata. We exploited a previously developed Agrobacterium tumefaciens-mediated transformation (ATMT) to generate a mutant library by insertional mutagenesis including more than 10,000 random mutants. To identify gene…

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MOESM1 of Rapid adaptation of signaling networks in the fungal pathogen Magnaporthe oryzae

Additional file 1: SVs summary.

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