Biology subjects

Rosso, M.-N.

Publications and source records attributed to Rosso, M.-N..

5 recordsLinked to original sources

bioRxiv2026

The coculture of Fomitopsis betulina with Escherichia coli induces a nutritional stress and triggers secondary metabolism pathways.

Basidiomycete fungi are an underexplored source of specialized metabolites with significant biotechnological potential. However, the environmental cues that activate their biosynthetic pathways remain poorly understood. Here, we investigated the response of the wood-decaying fungus Fomitopsis betulina, to nutritional competition using co-cultures with Escherichia coli. On solid medium, F. betulina inhibited the bacterial growth. Using a mass spectrometry-based metabolomics approach, we identified a Sumikis acid derivative, calcium diformate, and sulfuric acid among the compounds enriched within the inhibition zone and hypothesized that these compounds were associated with the acidification of the medium. Although F. betulina has previously been reported to produce the antibacterial compound piptamine, neither piptamine nor related derivatives were detected under our experimental conditions. In liquid medium, the co-culture with E. coli caused the rapid depletion of the available glucose, resulting in the establishment of carbon-starvation conditions and a 44% reduction in fungal biomass. Transcriptomic analyses revealed extensive metabolic reprogramming in response to bacterial competition, including the induction of genes involved in carbon acquisition, nutrient transport, redox homeostasis, and stress adaptation. Notably, a homolog of the Velvet regulatory complex, a central regulator of fungal development and specialized metabolism, was upregulated. The co-culture induced the expression of genes associated with multiple biosynthetic gene clusters, including terpene, polyketide, and fungal RiPP. Taken together, our results demonstrate that bacterial competition acts as a potent trigger of nutritional stress and secondary metabolism in F. betulina. More broadly, fungal-bacterial co-culture represents a promising alternative to extractions to identify high-value added metabolites pathways from basidiomycetes.

microbiology↗

bioRxiv2025

Global mapping of thioredoxin interacting proteins in Neurospora crassa

Thioredoxins (Trx) are essential thiol-oxidoreductases that regulate redox homeostasis by reducing oxidized cysteines in a wide range of target proteins. However, the Trx system and other redox regulation mechanisms remain poorly characterized in saprotrophic filamentous fungi. Here, we identified the components of the Neurospora crassa Trx system and uncovered potential redox-regulated proteins using Trx affinity chromatography. Genome search identified three Trx and a single thioredoxin reductase that we named TRX1, TRX2 TRX3 and TRR. Notably, TRX1 carries a C-terminal disordered extension of unknown function, conserved in two ascomycete taxa (Leotiomycetes and Sordariomycetes). Using recombinant cysteine-to-serine mutants of each Trx, we performed affinity chromatography and identified 1,998 proteins - approximately 19% of the N. crassa proteome. To rank the putative Trx targets, we applied a fold enrichment metric, comparing protein abundance before and after affinity chromatography. The average fold enrichment was four, with values reaching up to 117 for the most enriched protein, a DEAD/DEAH box helicase. Among the top-enriched proteins, we identified homologs of known human and plant Trx targets, like peroxiredoxins, as well as 93 transcription factors and 38 kinases. Additional potential Trx targets encompass, ubiquitination-related enzymes, Fe-S cluster assembly proteins, phospholipases, exonucleases, and chitin synthases. Moreover, components of multiprotein complexes were co-purified, reflecting both direct Trx interactions and indirect co-association. Overall, this study provides a global map of potential redox regulated proteins and Trx targets in N. crassa, laying the ground for future investigations into redox signaling in filamentous fungi.

microbiology↗

bioRxiv2021

The ectomycorrhizal basidiomycete Laccaria bicolor releases a GH28 polygalacturonase that plays a key role in symbiosis establishment

O_LIIn ectomycorrhiza, root penetration and colonization of the intercellular space by symbiotic hyphae is thought to rely on the mechanical force that results from hyphal tip growth, enhanced by the activity of secreted cell-wall-degrading enzymes. C_LIO_LIHere, we characterize the biochemical properties of the symbiosis-induced polygalacturonase LbGH28A from the ectomycorrhizal fungus Laccaria bicolor. The transcriptional regulation of LbGH28A was measured by qPCR. The biological relevance of LbGH28A was confirmed by generating RNAi-silenced LbGH28A mutants. We localized the LbGH28A protein by immunofluorescence confocal and immunogold cytochemical microscopy in poplar ectomycorrhizal roots. C_LIO_LIqPCR confirmed the induced expression of LbGH28A during ectomycorrhiza formation. L. bicolor RNAi mutants have a lower ability to establish ectomycorrhiza confirming the key role of this enzyme in symbiosis. The purified recombinant LbGH28A has its highest activity towards pectin and polygalacturonic acid. In situ localization of LbGH28A indicates that this endopolygalacturonase is located in both fungal and plant cell walls at the symbiotic hyphal front. C_LIO_LIThe present findings suggest that the symbiosis-induced pectinase LbGH28A is involved in the Hartig net formation and is an important determinant for successful symbiotic colonization. C_LI

plant biology↗

bioRxiv2021

Distribution of methionine sulfoxide reductases in fungi and conservation of the free-methionine-R-sulfoxide reductase in multicellular eukaryotes

Methionine, either as a free amino acid or included in proteins, can be oxidized into methionine sulfoxide (MetO), which exists as R and S diastereomers. Almost all characterized organisms possess thiol-oxidoreductases named methionine sulfoxide reductase (Msr) enzymes to reduce MetO back to Met. MsrA and MsrB reduce the S and R diastereomers of MetO, respectively, with strict stereospecificity and are found in almost all organisms. Another type of thiol-oxidoreductase, the free-methionine-R-sulfoxide reductase (fRMsr), identified so far in prokaryotes and a few unicellular eukaryotes, reduces the R MetO diastereomer of the free amino acid. Moreover, some bacteria possess molybdenum-containing enzymes that reduce MetO, either in the free or protein-bound forms. All these Msrs play important roles in the protection of organisms against oxidative stress. Fungi are heterotrophic eukaryotes that colonize all niches on Earth and play fundamental functions, in organic matter recycling, as symbionts, or as pathogens of numerous organisms. However, our knowledge on fungal Msrs is still limited. Here, we performed a survey of msr genes in almost 700 genomes across the fungal kingdom. We show that most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. However, several fungi living in anaerobic environments or as obligate intracellular parasites were devoid of msr genes. Sequence inspection and phylogenetic analyses allowed us to identify non-canonical sequences with potentially novel enzymatic properties. Finaly, we identified several ocurences of msr horizontal gene transfer from bacteria to fungi. HighlightsO_LIFree and protein-bound methionine can be oxidized into methionine sulfoxide (MetO). C_LIO_LIMethionine sulfoxide reductases (Msr) reduce MetO in most organisms. C_LIO_LISequence characterization and phylogenomics revealed strong conservation of Msr in fungi. C_LIO_LIfRMsr is widely conserved in unicellular and multicellular fungi. C_LIO_LISome msr genes were acquired from bacteria via horizontal gene transfers. C_LI

genomics↗

bioRxiv2018

Integrative visual omics of the white-rot fungus Polyporus brumalis exposes the biotechnological potential of its oxidative enzymes for delignifying raw plant biomass.

White-rot fungi are wood decayers able to degrade all polymers from lignocellulosic biomass including cellulose, hemicelluloses, and lignin. The white-rot fungus Polyporus brumalis efficiently breaks down lignin and is regarded as having a high potential for the initial treatment of plant biomass in its conversion to bio-energy. We performed integrative multi-omics analyses by combining data from the fungal genome, transcriptomes, and secretomes. We found the fungus possessed an unexpectedly large set of genes coding for enzymes related to lignin degradation, and that these were highly expressed and massively secreted under solid-state fermentation conditions. The examination of interrelated multi-omics patterns revealed the coordinated regulation of lignin-active peroxidases and H2O2-generating enzymes along with the activation of cellular mechanisms for detoxification, which combined to result in the efficient lignin breakdown by the fungus.\n\nImportancePlant biomass conversion for green chemistry and bio-energy is a current challenge for a modern sustainable bioeconomy. The complex polyaromatic lignin polymers in raw biomass feedstocks (i.e. agriculture and forestry by-products) are major obstacles for biomass conversions. From a biotechnological aspect, these compounds could be a potential source of aromatic platform molecules for bio-based polymers. Here we describe the extraordinary ability of Polyporus brumalis for lignin degradation using its enzymatic arsenal to break down wheat straw, a lignocellulosic substrate that is considered as a biomass feedstock worldwide. We observed unusual expansions of gene families coding for; 1) Class II peroxidases involved in lignin degradation; and 2) GMC oxidoreductases/dehydrogenases involved in generating the hydrogen peroxide required for lignin peroxidase activity. Our findings suggested the fungus massively mobilizes this oxidative machinery during growth on wheat straw. Overall, we identified sets of co-regulated enzymes, which could potentially augment the efficiency of biotechnological plant biomass conversions.

bioengineering↗