{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077559/peptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077559/proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077559/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077559/P20220602815_LCM_3_Slot1-84_1_7024.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077559/P20220602815_SFM_2_Slot1-86_1_7026.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077559/P20220602815_SFM_1_Slot1-85_1_7025.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077559/P20220602815_LCM_1_Slot1-82_1_7022.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077559/P20220602815_SFM_3_Slot1-87_1_7027.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077559/P20220602815_LCM_2_Slot1-83_1_7023.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["zhang@bio.uminho.pt"],"submitter":["Shuang Liu"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Biomarker discovery","Lueyang silky fowl","Multi‑omics","White leghorn","Immunometabolic resistance","Avian disease resistance"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077559"],"tissue":["Breast"],"sample_protocol":["Muscle tissue (100 mg) was homogenized in SDT lysis buffer containing protease inhibitors, and the lysate was clarified by centrifugation. Protein concentration was determined using a BCA assay. For sample preparation, 100 µg of protein was processed by FASP: proteins were reduced with DTT, alkylated with iodoacetamide, and digested overnight with trypsin (1:50, enzyme:protein) at 37 °C. The resulting peptides were desalted on C18 StageTips, lyophilized, and resuspended in 0.1% formic acid, and peptide content was measured by UV absorbance at 280 nm. For separation, 1 µg of peptide from each sample was analyzed by nanoLC on an Easy-nLC 1200 using a 25 cm × 75 µm C18 column. Mobile phase A was 0.1% formic acid in water and mobile phase B was 0.1% formic acid in acetonitrile. Peptides were separated with a 120 min gradient from 5% to 30% B at a flow rate of 300 nL/min. The main enrichment/cleanup strategy was peptide desalting and purification using FASP and C18 StageTips; no specific PTM-enrichment step was described. Mass spectrometric analysis was performed in positive ion mode with a scan range of 100–1700 m/z. Data were acquired in DDA mode, with full MS scans followed by top 20 MS/MS scans using HCD fragmentation. The raw data were searched against the UniProt Gallus gallus database with MaxQuant (v2.2.0.0) with LFQ enabled and a 1% FDR at peptide and protein levels. Differential proteins were defined using FC > 2.0 or FC < 0.5 with p < 0.05."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The raw LC–MS/MS files were searched against the UniProt Gallus gallus database using MaxQuant v2.2.0.0 with label-free quantification (LFQ) enabled. Peptide and protein identifications were filtered at 1% FDR at both levels. The search was performed under a data-dependent acquisition (DDA) workflow, with full MS scans (m/z 100–1,700) followed by top 20 MS/MS scans using HCD fragmentation (NCE 28). The MS1 and MS/MS resolutions were 60,000 and 15,000, respectively. For protein quantification, LFQ intensity was used, and differential abundance was defined using fold change > 2.0 or < 0.5 together with p < 0.05.  In addition, the proteomics sample preparation followed FASP-based digestion: proteins were extracted from muscle tissue, reduced with DTT, alkylated with iodoacetamide, digested overnight with trypsin, and desalted on C18 StageTips before LC–MS/MS analysis. The manuscript does not report a more complex proteomics-specific downstream bioinformatics pipeline beyond database searching, LFQ-based quantification, and differential protein screening in MaxQuant."],"omics_type":["Proteomics"],"labhead":["Xiaoying Zhang"],"instrument_platform":[""],"labhead_affiliation":["Shaanxi University of Technology"],"submission_type":["PARTIAL"],"species":["Gallus Gallus (chicken)"],"submitter_mail":["13572623262@163.com"],"publication":["Not available"],"submitter_affiliation":["Shaanxi University of Technology"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Multi-Omics profiling reveals immunometabolic adaptations underlying disease resilience in indigenous Lueyang Silky Fowl compared to White Leghorns","description":"Sustainable avian production demands genetic strategies beyond vaccines to enhance disease resilience, particularly in indigenous breeds like Lueyang Silky Fowl (LSF), which show superior resistance compared to commercial White Leghorn chickens (WLC) but lack molecular characterization. We hypothesized LSF breast muscle harbors integrated immune–metabolic adaptations absent in WLC, reflecting evolutionary divergences and physiological ecology. We performed RNA-seq, LC-MS/MS proteomics and untargeted metabolomics on sex- and age-matched LSF and WLC breast muscle (n=3/group). Differentially expressed genes (DEGs), proteins (DAPs), and metabolites (DAMs) were identified and integrated via pathway enrichment and network analyses. LSF muscle showed 2,577 DEGs (949 up, 1,628 down), 262 DAPs (48 up, 214 down), and 197 DAMs (52 up, 145 down). Concordant enrichments spanned mitochondrial oxidative phosphorylation; amino-acid metabolism (arginine/proline; alanine/aspartate/glutamate); MAPK and calcium signaling; and antioxidant pathways (notably glutathione). Integrated networks revealed 66 shared KEGG pathways, including convergent hubs in calcium/MAPK signaling, apelin, and focal adhesion, nominating candidate markers like NOS1, GOT1, PRKCA, MAP2K6, and ATP6V1E1. These bulk-tissue signatures likely integrate myocyte-intrinsic, stromal, and resident immune-cell programs; thus, offering testable signatures for avian immunometabolic resilience. We propose validation through single-cell/spatial transcriptomics, immunohistochemistry, targeted LC-MS and metabolomics, and pathogen challenge assays. This study advances ornithological understanding by revealing breed-specific physiological adaptations in poultry, positioning muscle as proxy for systemic resilience, and providing biomarkers for genomic selection to conserve and enhance genetic diversity in resilient avian lines under intensive farming 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