{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/checksum.txt"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/full_search_pea_roots.msf"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/full_search_pea_roots.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/2.raw"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069618/full_search_pea_roots.mzTab"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["ea.dolgikh@arriam.ru"],"submitter":["Tatiana Leonova"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Legume-rhizobial symbiosis","medicago truncatula gaerth","reactive oxygen species","pisum sativum l.","immune response regulation","pattern-recognizing receptors","jasmonic acid","nod factors","Legume-rhizobial symbiosis; immune response regulation; nod factors; reactive oxygen species; jasmonic acid; pattern-recognizing receptors; pisum sativum l.; medicago truncatula gaerth"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069618"],"tissue":["Root"],"sample_protocol":["Samples of frozen ground root material from Pisum sativum L. were taken for proteomic experiments. Total protein fractions were isolated using the phenol extraction method according to the established protocol.  Dry protein isolates were reconstituted in a 10% (w/v) aqueous (aq.) sodium dodecyl sulphate (SDS), after which the protein concentration in individual samples was determined using a commercial 2D Quant Kit (GE Healthcare, Chicago, USA) according to the manufacturer’s protocol.  Protein concentration was verified by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE).  Based on the measured protein concentrations in the extracts, aliquots containing 100 μg of protein from each root sample were subjected to tryptic digestion using centrifugal filters, according to the filter-assisted sample preparation (FASP) protocol with modifications adapted for plant-derived material. Desalting and pre-cleaning of the tryptic hydrolysates were performed by reverse-phase solid-phase extraction (rpSPE) employing 200 µL tips containing six layers of C18 material (Empower™ SPE discs, CDS Analytical, USA), as implemented in the in-house established protocol. The dried tryptic hydrolysates were sequentially reconstituted in 60%, 20%, and 3% (v/v) aqueous acetonitrile containing 0.1% (v/v) formic acid and loaded onto a PepMap 100 C18 trap column (300 μm × 5 mm, 3 μm particle size; Thermo Fisher Scientific, Bremen, Germany). Peptide analysis (1 μg, 10 μL injection volume) was performed using an Ultimate 3000 RSLC nanoHPLC system (Thermo Fisher Scientific) equipped with a nano-electrospray ionization (nanoESI) source and coupled online to an Orbitrap Fusion Tribrid mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) operated in positive ion mode. Chromatographic separation was achieved on a PepMap RSLC C18 analytical column (75 μm × 100 mm, 2 μm particle size; Thermo Fisher Scientific). Samples were loaded onto the trap column at a flow rate of 30 μL/min using the full-loop injection mode and washed for 15 min with 0.1% (v/v) trifluoroacetic acid (TFA) at the same flow rate prior to separation on the analytical column. Eluents consisted of (A) 0.1% (v/v) aqueous formic acid and (B) 0.08% (v/v) formic acid in acetonitrile. The analytical separation was performed at a flow rate of 0.3 μL/min and a column temperature of 40 °C using the following gradient: 3–35% eluent B over 120 min, 35–85% B over 10 min, 85–3% B over 5 min, followed by an isocratic hold at 3% B for 10 min. Mass spectrometry was performed with a spray voltage of 1900 V and a capillary temperature of 275 °C. Full MS scans were acquired in the Orbitrap analyzer at a resolution of 120,000 (at m/z 200), with one microscan per spectrum, an AGC target of 4 × 10⁵, a maximum injection time of 50 ms, and an m/z scan range of 300–1700. The default charge state was set to 2. Data-dependent MS/MS acquisition was conducted using a parallel strategy combining Orbitrap-HCD (higher-energy collisional dissociation) and linear ion trap-CID (collision-induced dissociation) fragmentation. Orbitrap MS/MS scans were acquired at a resolution of 15,000 with an AGC target of 5 × 10⁴ and a maximum injection time of 120 ms, while ion trap MS/MS scans used an AGC target of 1 × 10⁴ and a maximum injection time of 35 ms. The instrument operated in Top3s mode, selecting the most intense precursor ions for fragmentation within a total cycle time of 3 s. The isolation window was set to 1.5 Th (HCD) and 2 Th (CID), with normalized collision energies of 28% and 35%, respectively. Peptide ions with unassigned charge states or charge states between +1 and +7 were excluded. The intensity threshold for precursor selection was 3 × 10⁴. Peptide match was set to “preferred,” isotopes were excluded, and dynamic exclusion was enabled for 60 s."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Protein identification and quantification were performed using Proteome Discoverer v2.2 (Thermo Fisher Scientific, Bremen, Germany), while differential expression analysis was conducted with Progenesis QI software (Waters GmbH, Eschborn, Germany). Peptide identification and subsequent protein annotation were carried out against the Pisum sativum protein sequence database (URGI database). The SEQUEST search engine was used in Proteome Discoverer with the following parameters: enzyme specificity was set to trypsin, allowing up to three missed cleavages; precursor mass tolerance was 10 ppm, and fragment mass tolerance was 0.8 m/z. The false discovery rate (FDR) thresholds were set to 0.01 (strict) and 0.05 (relaxed), with validation based on q values. Fixed modification included carbamidomethylation of cysteine (+57.021 Da), and variable modifications included oxidation of methionine and tryptophan (+15.995 Da). Differential protein abundance was assessed in Progenesis QI with the following criteria: ANOVA p ≤ 0.05, maximum fold change ≥ 1.5, q ≤ 0.05, maximum coefficient of variation (CV) ≤ 60.5%, rank ≤ 3, and charge states between 2 and 6. Post-processing of proteomic data was performed in the R programming environment v3.6.3. Functional annotation of identified proteins was carried out using Mercator4 (v4.0, https://www.plabipd.de/mercator_main.html"],"omics_type":["Proteomics"],"labhead":["Dr. Elena Dolgikh"],"instrument_platform":[""],"labhead_affiliation":["Laboratory of Signal Regulation, All-Russia Research Institute for Agricultural Microbiology, St. Petersburg, Russia"],"submission_type":["COMPLETE"],"species":["Pisum Sativum (garden Pea)"],"submitter_mail":["tleonova@ipb-halle.de"],"publication":["10.1007/S11103-026-01692-Z"],"submitter_affiliation":["Leibniz Institute of Plant Biochemistry"],"submitter_country":["Germany"],"doi":["10.6019/PXD069618"],"additional_accession":[]},"is_claimable":false,"name":"Rhizobial Nod factors modulate reactive oxygen species, jasmonates, and pattern-recognizing receptors to suppress immune response","description":"Fine-tuning of the immune response plays a key role in legume-rhizobial symbiosis. Rhizobial Nod factors can suppress the defense responses during symbiosis, but the possible mechanisms of such regulation remain poorly understood. Here, we observe that Nod factors effectively suppress the expression of genes encoding defense markers (WRKYs, PRs, PALs), the reactive oxygen species (ROS) formation, and reduce the content of pattern recognition receptor (PRR) LYK9 induced by treatment with deacetylated chitooligosaccharide CO8-DA in pea roots. Since PRR LYK9 may recognize both chitin/COs and peptidoglycan, it likely plays an important role in the activation of defense responses during rhizobial inoculation. To identify potential regulators through which Nod factors suppress the immune response in plants during symbiosis with rhizobia, proteome and transcriptome analyses were performed. This allowed identifying several potential candidates activated by Nod factors, such as superoxide dismutase and catalase enzymes, which prevent excessive ROS accumulation and the development of oxidative stress. We also found ubiquitin ligases and ubiquitin-conjugating enzymes that may target PRRs activated in response to rhizobial inoculation. LYK9 degradation via ubiquitinylation was shown to prevent a hypersensitive response in plants. Nod factors activate enzymes involved in jasmonic acid biosynthesis, which in turn activates the transcription factor ABR1, suppressing the abscisic acid-induced responses and decreasing the immune response. Finally, we showed that LysM-receptor-like kinases PsLYK11/MtLYK11, probable homologs of Arabidopsis AtLYK3 in pea and Medicago, are involved in regulation of the immune 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