Fungal Biology and Biotechnology最新文献

{"title":"A superfamily of bioactive proteins from fungi - are these secondary metabolites?","authors":"Claudia Feurstein, Lisa Bachmann, Lena Heber, Birgit Dobbert, Sascha Jung","doi":"10.1186/s40694-026-00219-x","DOIUrl":"10.1186/s40694-026-00219-x","url":null,"abstract":"<p><strong>Background: </strong>Since decades, fungi are leveraged in biotechnology to produce high-value compounds used in multiple economic sectors. Strain and process optimisation is based on a comprehensive understanding of the production organism on the cellular and molecular level. Among three antifungal protein families in fungi, consisting of small cysteine-stabilised proteins, it has been shown that, for some family members, bioactivities are also associated with additional functions in their hosts, e.g., carbon metabolism, autophagy, or asexual development. These proteins are interesting as alternative source of novel antifungal drugs. However, their potential impact on biotechnological production is not yet elucidated.</p><p><strong>Results: </strong>In this study, we introduce the antifungal bubble protein \"AgBP\", from Aspergillus giganteus and further elucidate the reservoir of bioactive proteins in fungi. We used NCBI PSI-BLAST and subsequent phylogenetic and structural analyses of the Antifungal Protein (AFP), Bubble Protein (BP), and Neosartorya fischeri antifungal protein 2 (NFAP2) family members. We could identify further putative members: 165 AFP-, 102 BP-, and 219 NFAP2-like proteins. Six of the AFP and all 219 NFAP2 family members are not yet assigned on InterPro. All proteins were exclusively identified in fungi. To our best knowledge, this is the first study to report this group of bioactive proteins is shared among the two divisions of Ascomycetes and Basidiomycetes. Phylogenetic tree analyses demonstrate restricted taxonomic distribution within single genera. Furthermore, the comparison of the tertiary structures of all members of the three AFP families clearly separates them from each other and from non-fungal small cysteine-stabilised antifungal proteins.</p><p><strong>Conclusion: </strong>We hypothesise that the three protein families represent a distinct superfamily of evolutionary related proteins. We further hypothesise that these proteins could be categorised as secondary metabolite like molecules of ribosomal origin. For brevity, we named this superfamily BPF (bioactive proteins from fungi). The distribution of BPF members is presumably driven by horizontal gene transfer. Furthermore, we hypothesise that BPF members likely serve rather different biological roles than merely acting as antimicrobials. Their hypothetical classification as potential secondary metabolite like proteins in combination with their occurrence among several biotechnologically relevant fungal genera, e.g., Aspergillus, Penicillium, Trichoderma, Schizophyllum, etc., emphasises their potential relevance for genetic and metabolic engineering.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-08-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13525654/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148857919","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fungal morphotype detection and quantification in microscopic images with TU_MyCo-vision: a user-friendly deep learning object detection tool.","authors":"Kartik J Deopujari, Matthias Schmal, Caroline Danner, Zainab Abdul Qayyum, Jordy T Zwerus, Julian Kopp, Mihail Besleaga, Roghayeh Shirvani, Astrid R Mach-Aigner, Robert L Mach, Christian Zimmermann","doi":"10.1186/s40694-026-00215-1","DOIUrl":"10.1186/s40694-026-00215-1","url":null,"abstract":"<p><p>Morphological switching in response to environmental stimuli is a well-known phenomenon in fungi, leading to diverse morphotypes. Microscopic observation remains a widely used approach to study these phenotypes, but variation in sample preparation and operator skill can limit the scale of sample processing or introduce operator bias. Although several image-based cell detection tools have been developed, most are tailored to specific applications or limited to a particular taxon. To address the need for a tool applicable to the polymorphic, yeast-like fungus Aureobasidium pullulans, and with potential applicability to other taxa, we developed TU_MyCo-Vision, an Ultralytics YOLO (You Only Look Once) based object detection tool for identifying 13 fungal morphotypes in bright-field microscopic images. Identification of 13 fungal morphotypes, including variation of vacuolated single cells, cells with granular cytoplasmic appearance, and diverse hyphal forms, is achieved by integrating a YOLOv11m-based object detector trained on a custom dataset of 1,504 annotated images and a standalone graphical user interface that enables downstream data analysis and visualization of results. The best-performing model (Zulu_s3) achieved a mean precision of 73.4%, a recall of 66.5%, a mean average precision at 50% IoU (mAP@50) of 73.5%, and a mean average precision at varying IoU thresholds between 50 and 90% IoU (mAP@50-95) of 54.5% across all 13 classes. The single-group analysis pipeline was validated on a 90-image test set, generating six quantitative summaries that capture the distribution and co-occurrence of fungal morphotypes, including absolute counts, relative and mean relative abundance plots, stacked bar plots and clustered heatmaps. Multi-group evaluation on previously unseen datasets comprising Candida albicans, Komagataella phaffi, and Aspergillus niger spores demonstrated that these morphotype profiles can be compared across biologically distinct genera, highlighting the tool's potential applicability for studying fungal morphological diversity.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-08-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13459361/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148714519","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Genetic tools for transformation of Xyleborus ambrosia beetle fungal symbionts.","authors":"Ross A Joseph, Abolfazl Masoudi, Nemat O Keyhani","doi":"10.1186/s40694-026-00217-z","DOIUrl":"10.1186/s40694-026-00217-z","url":null,"abstract":"<p><strong>Background: </strong>Ambrosia beetles rely on obligate fungal partners for survival, and these associations are emerging as model systems for examining the development and evolution of fungal-animal mutualism. However, genetic tools for the manipulation of such mutualistic fungi remain largely lacking, and consequently the genetic basis employed by these fungi to establish associations with their beetle partners remains almost completely unexplored. Here, we provide methods for protoplast generation and transformation of several major filamentous fungal partners of Xyleborus ambrosia beetles including Raffaela arxii, R. fusca, Harringtonia aguacate, and Graphium ambrosium using reporter constructs driven by the H. lauricola gpd promoter sequence. In addition, we developed inducible expression systems for the beetle symbiont, but plant pathogen, H. lauricola, responsible for laurel wilt disease, and show that these constructs are also functional in G. ambrosium. This work demonstrates the utility of H. lauricola genetic parts in transforming diverse groups of fungi and offers a toolbox for their genetic dissection.</p><p><strong>Results: </strong>Fungal strains showed sensitivity to hygromycin, and protoplasts derived from the fungi were transformed with plasmids expressing the hygromycin selective marker (HPH) along with either green- or red-fluorescent proteins (GFP/RFP), with expression driven by the constitutive H. lauricola gpd promoter. Transformed strains for the fungal species described above showing expression of either GFP or RFP were obtained. A series of inducible plasmids using the H. lauricola alcA_p-RFP-(ethanol) and glaA_p-RFP-(maltose) inducible promoters were also tested and validated.</p><p><strong>Conclusions: </strong>Our data provide methods and tools for genetic manipulation of a wide range of ambrosia beetle fungal symbionts, including marking cells with fluorescent proteins and use of inducible expression systems. Intriguingly, the method/plasmids developed did not result in transformation of the related Xyleborus fungal symbiont, Neocosmospora affinis. The fluorescent strains developed can be used to monitor symbiotic colonization of the beetle host, fungal development in host galleries, host preferences, and a range of other applications, and promoters may be used for further knockout and expression studies.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-07-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13393879/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148563542","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fungal expression strategies for heterologous production of antimicrobial peptides.","authors":"Anna Donnan, Samuel M M Prudence, Sarah A Kessans","doi":"10.1186/s40694-026-00220-4","DOIUrl":"10.1186/s40694-026-00220-4","url":null,"abstract":"<p><p>Antimicrobial peptides (AMPs) are promising candidates for next-generation therapeutics due to their broad-spectrum activity and reduced propensity for resistance, making them valuable in medicine, agriculture, and biotechnology. However, traditional AMP production methods including isolation from natural sources and chemical synthesis are costly, inefficient, and environmentally unsustainable, particularly for longer or post-translationally modified peptides. While heterologous expression has emerged as a scalable and versatile alternative, its success depends strongly on host selection and tailored optimisation strategies. This review examines recent advances in fungal systems as platforms for AMP production. Fungal systems, and particularly yeasts such as Pichia pastoris, offer rapid growth, low-cost fermentation, secretion capacity, and the ability to perform key post-translational modifications (PTMs), making them leading hosts for recombinant AMPs. We outline strain choice and engineering strategies that enhance AMP yield and bioactivity, including promoter and codon optimisation, secretion signal choice, fusion partners, and the construction of tandem or chimeric AMPs. By integrating current methodologies and case studies, this review aims to guide future efforts toward efficient, scalable, and commercially viable AMP manufacturing in fungal hosts, positioning fungal biotechnology as a key enabler in the development of next-generation antimicrobial solutions.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13317432/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148363888","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Reintroduction of lignin-modifying enzymes in the brown-rot fungus Gloeophyllum trabeum restores ligninolytic activities but diminishes lignocellulose degradation.","authors":"Nandin Ganjoloo, Weiran Li, Jiwei Zhang","doi":"10.1186/s40694-026-00218-y","DOIUrl":"10.1186/s40694-026-00218-y","url":null,"abstract":"<p><p>Fungi have evolved two distinct strategies, white-rot and brown-rot, to degrade lignocellulose in plant biomass. White-rot fungi utilize lignin-modifying enzymes (LMEs) to deconstruct lignin and access carbohydrates, whereas brown-rot fungi, which arose from white-rot ancestral lineages, have largely lost LME activities. Instead, brown-rot fungi rely on a small redox metabolite-mediated Fenton system that generates reactive oxygen species (ROS) to rapidly deconstruct lignocellulose and selectively remove carbohydrates. The abandonment of LMEs in brown-rot fungi suggests an intriguing evolutionary strategy to streamline decay machinery, but it remains unclear why fungi evolved this way. Here, we reintroduced LME genes from the white-rot fungus Trametes versicolor into the model brown-rot fungus Gloeophyllum trabeum to create hybrid fungal systems and evaluate LME function within the Fenton-dominant brown-rot context. Analysis of lignocellulose degradation showed that lignin disruption can be partially restored in LME mutants, thereby shifting the typical carbohydrate-selective decay mode of G. trabeum. However, constitutive LME expression also caused pronounced growth defects and reduced the overall rate of lignocellulose degradation, specifically decreasing cellulose and hemicellulose removal. Correlation analysis between genotypes and phenotypes indicates that LMEs, although prevalently used for delignification in fungi, are fundamentally incompatible with the carbohydrate-selective brown-rot system.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13312777/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148347412","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multilayered control of hexose uptake and phosphorylation through specialized sugar kinases in Nakaseomyces glabratus.","authors":"Jolien Vreys, Eline Schraepen, Tia Peterson, Stefanie Wijnants, Patrick Van Dijck","doi":"10.1186/s40694-026-00216-0","DOIUrl":"10.1186/s40694-026-00216-0","url":null,"abstract":"<p><p>The opportunistic pathogenic fungus Nakaseomyces glabratus inhabits diverse host niches with fluctuating nutrient availability. Therefore, efficient control of glycolytic entry is essential, yet the regulatory principles governing hexose phosphorylation in this species remain incompletely understood. Here, we investigated the functional organization of sugar kinases in N. glabratus. Among five predicted sugar kinases, only three (Hxk2, Hxk2b and Glk1) catalyzed phosphorylation of glucose, fructose or mannose, whereas Hxk1 and Glk1b lacked detectable activity. Kinetic analyses revealed a functional specialization, with the hexokinases acting as high-capacity enzymes and Glk1 functioning as a high-affinity, low-capacity kinase optimized for low-sugar concentrations. Despite similar intrinsic kinetics among the hexokinases, Hxk2b emerged as the physiologically dominant enzyme, reflecting differential regulation rather than catalytic properties alone. Both hexokinases, but not Glk1, were strongly inhibited by trehalose-6-phosphate, linking glycolytic entry to trehalose metabolism. Consistent with this, perturbation of trehalose synthesis modulated hexose uptake, revealing that phosphorylation capacity is a major driver of sugar import, while metabolic feedback further constrains uptake. Nuclear localization of sugar kinases and condition-dependent expression patterns indicate additional regulatory layers. Together, our results demonstrate that N. glabratus controls glycolytic entry through a multilayered architecture integrating enzyme specialization, transcriptional tuning, trehalose-6-phosphate-mediated feedback and uptake coupling. This systems-level organization results in robust growth across fluctuating and often sugar-limited host environments.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13282861/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148297279","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Investigating the versatility of cytochalasan cytochrome P450 monooxygenases using combinatorial biosynthesis reveals stereochemical restrictions.","authors":"Lei Li, Tahir Ali, Jacob Goralczyk, Sameera Jayasundara, Ayan Paul, Marcelo Rodrigues de Amorim, Christine Beemelmanns, Elizabeth Skellam","doi":"10.1186/s40694-026-00214-2","DOIUrl":"10.1186/s40694-026-00214-2","url":null,"abstract":"<p><strong>Background: </strong>Cytochalasans are a large family of fungal metabolites which inhibit actin polymerization and ultimately lead to a broad range of biological effects in different assays. Investigations into the biosynthesis of cytochalasans has revealed that the cytochrome P450 monooxygenase (P450s) tailoring enzymes possess a somewhat relaxed substrate-specificity and may accept structurally-related intermediates for oxidation, partly explaining the variety of structural variations observed in this family of molecules. In this study, we investigate a broad range of P450 enzymes via combinatorial biosynthesis to better understand their substrate scope and potential applications as biocatalysts.</p><p><strong>Results: </strong>Genome mining enabled us to identify cryptic cytochalasan biosynthetic gene clusters (BGCs) in six different species of fungi, each with at least two P450 enzymes encoded. Comparative genomics identified a cryptic thioredoxin-like enzyme encoded in cytochalasan BGCs that co-occurs with the gene encoding a Baeyer-Villiger monooxygenase. Heterologous expression of seven P450s in Magnaporthe grisea mutant strains, lacking P450s required for pyrichalasin H biosynthesis, enabled functional characterization of three P450s, two of which were previously cryptic. The experimental results, combined with phylogenetic analysis of the P450 sequences, reveal subtle information regarding the structures of the associated cytochalasans and begins to explain why some P450s are inactive on the substrates available to them.</p><p><strong>Conclusions: </strong>The P450 enzymes involved in cytochalasan biosynthesis are known to be site-selective in their native host but also possess intrinsic promiscuity due to being able to modify structurally-related analogues. By investigating a diverse set of P450s from characterized and cryptic BGCs, we were able to identify that the stereochemistry of functional groups around the cytochalasan backbone is more restrictive than the size of the macrocycle when introducing the P450 enzyme to non-native substrates.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13281438/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148284763","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"What makes a mycoparasite? Candidate effectors from fungi that parasitize other fungi exhibit structural homology to those of fungal plant pathogens.","authors":"Alexandros G Sotiropoulos, Matthias Heuberger, Thomas Wicker, Levente Kiss","doi":"10.1186/s40694-026-00211-5","DOIUrl":"10.1186/s40694-026-00211-5","url":null,"abstract":"<p><strong>Background: </strong>Fungi that feed and thrive on other living fungi and damage those through specific adaptations to this lifestyle are known as mycoparasites. Despite its ecological significance and practical applications in crop protection, this type of parasitism is still poorly understood. Here, we hypothesize that aggressive fungal-fungal parasitic interactions are similar to those between plants and their fungal pathogens.</p><p><strong>Results: </strong>We tested this hypothesis in two ways. First, we analyzed the genetic signatures of the mycoparasitic nutrition mode through the predicted Carbohydrate-Active enZYme (CAZyme) profiles of more than 50 fungi with high-quality reference genomes across the Fungal Kingdom, including mycoparasites and their close relatives. Two predicted CAZyme families, AA3-2 and AA9, appeared to be associated with mycoparasitism. Second, we searched for candidate effectors in protein datasets of three specialist mycoparasites and closely related fungi. Based on the tertiary structures of selected proteins predicted by AlphaFold, we identified protein clusters. Surprisingly, several tertiary structures predicted in three, phylogenetically diverse mycoparasites were homologous to well-studied candidate effectors in a model plant pathogen. One of these protein clusters belonged to the AA9 CAZyme family.</p><p><strong>Conclusions: </strong>These results supported our hypothesis and may represent the first steps towards a unified molecular concept to understand mycoparasitism as a specific nutrition mode guided by candidate effectors.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13188720/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147984308","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Glutamate dehydrogenases in fungi: From biology to biotechnology.","authors":"Ejaj K Pathan, Himal Sapkota, Subrata Dasgupta, Narayan S Punekar","doi":"10.1186/s40694-026-00212-4","DOIUrl":"10.1186/s40694-026-00212-4","url":null,"abstract":"<p><p>Glutamate dehydrogenases (GDH; EC 1.4.1.2 and EC 1.4.1.4) play a pivotal role in fungal nitrogen metabolism by catalyzing the reversible conversion of 2-ketoglutarate to L-glutamate. In fungi, NAD- as well as NADP-dependent GDHs function at the interface of ammonia assimilation and glutamate catabolism, contributing to growth, differentiation, and morphogenesis. The evolution of fungi to adapt and occupy various ecological niches is closely aligned to the diversity of regulations of the functions of GDHs, their localisation and biochemical characteristics. This review explores the biochemical, molecular, and structural studies on fungal GDHs, emphasizing their catalytic diversity, coenzyme specificity, and regulatory mechanisms, including phosphorylation, thiol modulation, and allosteric control. Structural elucidations of NADP-GDHs from Aspergillus niger, Aspergillus terreus, and Candida albicans provide new insights into cofactor binding, substrate recognition, and inhibitor interactions. Molecular analyses reveal distinct evolutionary trajectories for NAD- and NADP-GDHs across fungal taxa, with GDH-mediated transitions linked to morphogenetic processes such as the yeast-to-hypha (Y-H) switch, highlighting GDHs as promising antifungal drug targets. The comprehensive survey of fungal GDHs presented here emphasises their biochemical versatility, evolutionary significance, and translational potential in agriculture, biosensor development and in industry. The review also highlights gaps in our understanding of fungal GDHs and potential areas for further research.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13179614/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147960551","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A scalable PDMS extraction method for profiling fungal volatile compounds.","authors":"Rashaduz Zaman, Isaac Peetoom Heida, Heather T K Anderson, Guncha Ishangulyyeva, Nadir Erbilgin, James F Cahill","doi":"10.1186/s40694-026-00213-3","DOIUrl":"10.1186/s40694-026-00213-3","url":null,"abstract":"<p><strong>Background: </strong>Fungal volatile organic compounds (FVOCs) play key roles in fungal ecology, physiology, and biotechnological applications, but inconsistent sampling and analytical methods limit biological interpretation and cross-study comparability, underscoring the need for a standardized, validated workflow.</p><p><strong>Results: </strong>We developed and validated a polydimethylsiloxane (PDMS)-based volatilomics workflow and evaluated its performance across key methodological dimensions, including solvent extraction bias, static versus dynamic sampling, sorbent reuse, temporal emission resolution, and discrimination of physiological states. Solvent choice (dichloromethane vs. diethyl ether) influenced the quantitative recovery of individual compounds but did not affect the overall FVOC composition detected. Static PDMS and dynamic push-pull sampling produced distinct yet complementary volatilome profiles, with method-specific enrichment across compound classes. Reconditioned PDMS tubing performed equivalently to fresh tubing across repeated deployments, with no detectable decline in compound recovery and multivariate structure. Sequential 96-h sampling captured clear temporal emission patterns in both Trichoderma atroviride and Grosmannia clavigera, revealing species-specific emission trajectories consistent with metabolic stages. Application of the optimized workflow further distinguished T. atroviride morphotypes (white vs. green), which maintained distinct volatile profiles over time and exhibited morphotype-specific emission dynamics in key compounds.</p><p><strong>Conclusions: </strong>The PDMS-based workflow presented here provides a robust and reproducible framework for FVOC analysis, effectively addressing methodological biases, resolving temporal emission dynamics, and discriminating among physiological states. Standardizing PDMS sampling and extraction substantially enhance the biological interpretability and comparability of FVOC data, enabling broader and more reliable applications in fungal ecology, physiology, and biotechnology.</p>","PeriodicalId":52292,"journal":{"name":"Fungal Biology and Biotechnology","volume":"13 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13159281/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147876547","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}