Lepista sordida is a valuable edible mushroom rich in natural bioactive compounds. In the present study, a high-quality whole-genome of a domesticated strain of L. sordida was sequenced, revealing a 40.67 Mb genome in 13 contigs. Phylogenetic analysis revealed that L. sordida is evolutionarily closely related to edible mushroom Lyophyllum decastes and Hypsizygus marmoreus. Heat stress has a significant effect on the yield and quality of mushrooms, but the molecular basis for this is poorly understood in L. sordida. A label-free comparative proteomic analysis was performed under different heat stress conditions. The growth of L. sordida mycelia was inhibited, and nuclear apoptosis occurred under heat stress. Ca²⁺ and MAPK signaling pathways were found to be involved in heat stress signal transduction. It is hypothesized that the expression of various heat shock proteins plays a crucial role in the response to heat stress. In addition, the components of the ubiquitin-proteasome system and the thioredoxin system were upregulated, preventing the accumulation of misfolded proteins and possibly supporting the response to heat stress. In summary, these results provide a fundamental insight into the evolution and heat stress-responsive mechanisms in L. sordida and may facilitate the breeding of heat-tolerant strains for artificial cultivation.

Lepista sordida is a valuable edible mushroom rich in natural bioactive compounds. In the present study, a high-quality whole-genome of a domesticated strain of L. sordida was sequenced, revealing a 40.67 Mb genome in 13 contigs. Phylogenetic analysis revealed that L. sordida is evolutionarily closely related to edible mushroom Lyophyllum decastes and Hypsizygus marmoreus. Heat stress has a significant effect on the yield and quality of mushrooms, but the molecular basis for this is poorly understood in L. sordida. A label-free comparative proteomic analysis was performed under different heat stress conditions. The growth of L. sordida mycelia was inhibited, and nuclear apoptosis occurred under heat stress. Ca²⁺ and MAPK signaling pathways were found to be involved in heat stress signal transduction. It is hypothesized that the expression of various heat shock proteins plays a crucial role in the response to heat stress. In addition, the components of the ubiquitin-proteasome system and the thioredoxin system were upregulated, preventing the accumulation of misfolded proteins and possibly supporting the response to heat stress. In summary, these results provide a fundamental insight into the evolution and heat stress-responsive mechanisms in L. sordida and may facilitate the breeding of heat-tolerant strains for artificial cultivation.

Background: An oligonucleotide drug named nusinersen sodium is used to treat Spinal Muscular Atrophy (SMA), requires accurate detection for therapeutic research. There are no published reports on liquid chromatography-tandem mass spectrometry (LC-MS/MS) methods for detecting nusinersen in rat cerebrospinal fluid (CSF). An LC-MS/MS method has been created and verified to detect nusinersen in Sprague-Dawley (SD) rat CSF. The method employed solid-phase extraction for post-extraction analysis and used dT20 as an internal standard. Negative ion multiple reaction monitoring (MRM) mode scanning and the electrospray ionization (ESI) source were used. The method was validated over a concentration range of 5–2000 ng/mL with a Lower Limit of Quantification (LLOQ) of for nusinersen at 5 ng/mL. The method achieves extremely high accuracy and precision, good linearity, high extraction recovery, and provides a useful approach for evaluating the pharmacokinetics of nusinersen in rats.

Background: An oligonucleotide drug named nusinersen sodium is used to treat Spinal Muscular Atrophy (SMA), requires accurate detection for therapeutic research. There are no published reports on liquid chromatography-tandem mass spectrometry (LC-MS/MS) methods for detecting nusinersen in rat cerebrospinal fluid (CSF). An LC-MS/MS method has been created and verified to detect nusinersen in Sprague-Dawley (SD) rat CSF. The method employed solid-phase extraction for post-extraction analysis and used dT20 as an internal standard. Negative ion multiple reaction monitoring (MRM) mode scanning and the electrospray ionization (ESI) source were used. The method was validated over a concentration range of 5–2000 ng/mL with a Lower Limit of Quantification (LLOQ) of for nusinersen at 5 ng/mL. The method achieves extremely high accuracy and precision, good linearity, high extraction recovery, and provides a useful approach for evaluating the pharmacokinetics of nusinersen in rats.

The identifed succinylated peptides in G. lucidum (Table S1); Conservative analysis of the succinylated proteins (Table S2); Analysis the sequence motifs of the succinylpeptides (Table S3); GO functional annotation of the succinylproteins (Table S4); Subcellular localizations of the succinylated proteins (Table S5); The related proteins based on GO enrichment analysis (Table S6); The modified proteins based on KEGG pathway enrichment analysis (Table S7); The succinylated proteins based on domain enrichment analysis (Table S8); The proteins obtained from PPI network analysis (Table S9); Lysine succinylated enzymes related to triterpenoid and polysaccharide metabolism (Table S10). (XLSX 280 kb)

The identifed succinylated peptides in G. lucidum (Table S1); Conservative analysis of the succinylated proteins (Table S2); Analysis the sequence motifs of the succinylpeptides (Table S3); GO functional annotation of the succinylproteins (Table S4); Subcellular localizations of the succinylated proteins (Table S5); The related proteins based on GO enrichment analysis (Table S6); The modified proteins based on KEGG pathway enrichment analysis (Table S7); The succinylated proteins based on domain enrichment analysis (Table S8); The proteins obtained from PPI network analysis (Table S9); Lysine succinylated enzymes related to triterpenoid and polysaccharide metabolism (Table S10). (XLSX 280 kb)