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Genome sequence and annotation of the fungus Periconia digitata

ABSTRACT: The Periconia genus belongs to the phylum Ascomycota, order Pleosporales, family Periconiaceae. Periconia is widespread in many habitats but little is known about its ecology. Several species produce bioactive molecules, among them, Periconia digitata extracts were shown to be deadly active against the pine wilt nematode. The strain CNCM I-4278, here identified as P. digitata was able to inhibit the plant pathogen Phytophthora parasitica. Since P. digitata has great potential as biocontrol agent and the only other genome available in the Periconiaceae family is that of Periconia macrospinosa, which is quite fragmentary, we generated long-read genomic data for P. digitata. Thanks to the PacBio Hifi sequencing technology, we obtained a high-quality genome with a total length of 38,967,494 bp, represented by 13 haploid chromosomes. The transcriptomic and proteomic data strengthen and support the genome annotation. Besides representing a new reference genome within the Periconiaceae, this work will also contribute in our understanding of the Eukaryotic tree of life. Not least, opens new possibilities to the biotechnological use of the species.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Periconia Digitata

TISSUE(S): Mycelium

SUBMITTER: Cyril Van Ghelder

LAB HEAD: Aurélie Seassau

PROVIDER: PXD038175 | Pride | 2023-08-04

REPOSITORIES: Pride

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Genome sequence and annotation of the fungus Periconia digitata

Project description:The Periconia genus belongs to the phylum Ascomycota, order Pleosporales, family Periconiaceae. Periconia is widespread in many habitats but little is known about its ecology. Several species produce bioactive molecules, among them, Periconia digitata extracts were shown to be deadly active against the pine wilt nematode. The strain CNCM I-4278, here identified as P. digitata was able to inhibit the plant pathogen Phytophthora parasitica. Since P. digitata has great potential as biocontrol agent and the only other genome available in the Periconiaceae family is that of Periconia macrospinosa, which is quite fragmentary, we generated long-read genomic data for P. digitata. Thanks to the PacBio Hifi sequencing technology, we obtained a high-quality genome with a total length of 38,967,494 bp, represented by 13 haploid chromosomes. The transcriptomic and proteomic data strengthen and support the genome annotation. Besides representing a new reference genome within the Periconiaceae, this work will also contribute in our understanding of the Eukaryotic tree of life. Not least, opens new possibilities to the biotechnological use of the species.

2023-08-04 | PXD038112 | Pride

Deep Proteome profiling reveals signatures of age and sex differences in paw skin and sciatic nerve of naïve mice

Project description:The age and sex of studied animals profoundly impacts experimental outcomes in animal-based biomedical research. However, most preclinical studies in mice use a wide-spanning age range from 4 to 14 weeks and do not assess study parameters in male and female mice in parallel. This raises concerns regarding reproducibility and neglect of potentially relevant age and sex differences. Furthermore, the molecular setup of tissues in dependence of age and sex is unknown in naïve mice precluding efficient translational research. Here, we first compared two different mass spectrometric acquisition methods – DDA- and DIA-PASEF – in order to maximize the depth of proteome quantitation. We then employed an optimized workflow of quantitative proteomics based on DIA-PASEF followed by DIA-NN data analysis, and revealed significant differences in mouse paw skin and sciatic nerve (SCN) when comparing (i) male and female mice, and, in parallel, (ii) adolescent mice (4 weeks) with adult mice (14 weeks).

2022-11-29 | PXD034476 | Pride

Antler stem cell-conditioned medium data independent acquisition

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2023-04-11 | PXD041259 | Pride

DIA analysis of paired primary and recurrent breast cancers

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2023-02-03 | PXD032266 | Pride

Neddylation tunes peripheral blood mononuclear cells immune response in COVID-19 patients

Project description:The COVID-19 pandemic caused by SARS-CoV-2 has reached 5.5 million deaths worldwide, causing a huge impact globally. This highly contagious viral infection produces a severe acute respiratory syndrome that includes cough, mucus, fever and pneumonia. Likewise, many hospitalized patients develop severe pneumonia associated with acute respiratory distress syndrome (ARDS), besides an exacerbated and uncontrolled systemic inflammation which in some cases induce lethal cytokine storm. Although vaccines have clearly had a beneficial effect on disease development, there is still a high percentage of patients who develop pathology related to ineffective immune system response. Therefore, a thorough understanding of the modulatory mechanisms that regulate the response to SARS-CoV-2 is crucial to find effective therapeutic alternatives. Previous studies describe the relevance of Neddylation in immune system activation further its implications in viral infection. In this context, the present study postulates Neddylation, a reversible ubiquitin-like post-translational modification of proteins and controls their stability, localization and activity, as a key regulator in the immune response against SARS-CoV-2. For the first time, we describe an increase of serum global neddylation levels of COVID-19 patients particularly associated in the early response of the infection. In addition, the results showed that overactivation of neddylation control activation, proliferation, and response of peripheral blood mononuclear cells (PBMCs) derived from COVID-19 patients. Inhibition of neddylation and subsequent avoidance of activation of PBMCs, which reduces cytokine production and proteome modulation, may therefore be a critical mechanism and an efficient therapeutic approach to immunomodulate COVID -19 patients and avoid the much-feared cytokine storm.

2022-08-02 | PXD033673 | Pride

prm-PASEF and g-dia-PASEF analysis of plasma samples from colorectal cancer and control patients

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2023-04-11 | PXD036594 | Pride

Cross-linked amyloidogenic proteins as potential aggregation inhibitors

Project description:Amyloidogenic proteins, characterized by their ability to form fibrillar aggregates with β sheet structure play an important role in several degenerative diseases, including Parkinson’s disease. Numerous amyloidogenic proteins, such as α synuclein, are intrinsically disordered (or contain ID regions, hence they also present as highly dynamic conformational ensembles in these regions. Aggregation is an inherent property of the polypeptide chains and under non physiological, appropriate conditions most of the proteins can aggregate and form polymers of various structures. Since amyloid fib ril s and oligomers are associated with a great variety of human diseases, inhibition of protein aggregation has great importance and it can be addressed by using small molecules, peptides or proteins. Our research aim was to study the potential application of modified forms of different amyloidogenic proteins as inhibitor molecules by introducing structural constraints in them. Under various conditions, different amyloidogenic proteins’ (α-synuclein and β2-microglobulin) monomer molecules have been cross linked intramolecularly and the heterogeneous mixtures has been fractionated by HPLC. The inhibitory potential of the isolated and effective molecules has been experimentally investigated by various methods ThT assay, TEM, CD spectroscopy). Furthermore, the locations of the crosslinks in the molecules were determined by mass spectrometry, and their structures are modeled in silico. Our results revealed that conformational constrains applied by cross linking on amyloidogenic proteins block their amyloid formation. Moreover, these molecules exhibited inhibitory effect on the aggregation of the unmodified proteins, as well.

2023-10-24 | PXD042501 | Pride

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2022-02-16 | PXD028805 | Pride

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2023-02-03 | PXD037428 | Pride

First identification of a large set of serine hydrolases by activity-based protein profiling in dibutyl phthalate-exposed zebrafish larvae

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