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The resulting peptides were fractionated using an Ultimate 3000 nanoHPLC system in line with an LTQ-Orbitrap Velos mass spectrometer (Thermo Scientific). In brief, peptides in 1% (vol/vol) formic acid were injected onto an Acclaim PepMap C18 nano-trap column (Thermo Scientific). After washing with 0.5% (vol/vol) acetonitrile 0.1% (vol/vol) formic acid peptides were resolved on a 250 mm × 75 μm Acclaim PepMap C18 reverse phase analytical column (Thermo Scientific) over a 150 min organic gradient, using 7 gradient segments (1-6% solvent B over 1min., 6-15% B over 58min., 15-32%B over 58min., 32-40%B over 5min., 40-90%B over 1min., held at 90%B for 6min and then reduced to 1%B over 1min.) with a flow rate of 300 nl min−1. Solvent A was 0.1% formic acid and Solvent B was aqueous 80% acetonitrile in 0.1% formic acid. Peptides were ionized by nano-electrospray ionization at 2.1 kV using a stainless-steel emitter with an internal diameter of 30 μm (Thermo Scientific) and a capillary temperature of 250°C. Tandem mass spectra were acquired using an LTQ- Orbitrap Velos mass spectrometer controlled by Xcalibur 2.1 software (Thermo Scientific) and operated in data-dependent acquisition mode. The Orbitrap was set to analyze the survey scans at 60,000 resolution (at m/z 400) in the mass range m/z 300 to 2000 and the top ten multiply charged ions in each duty cycle selected for MS/MS in the LTQ linear ion trap. Charge state filtering, where unassigned precursor ions were not selected for fragmentation, and dynamic exclusion (repeat count, 1; repeat duration, 30s; exclusion list size, 500) were used. Fragmentation conditions in the LTQ were as follows: normalized collision energy, 40%; activation q, 0.25; activation time 10ms; and minimum ion selection intensity, 500 counts."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The raw data files were processed and quantified using Maxquant 1.5.3.30 and searched against the Galgal6a proteome (GCF_000002315.6) in addition to the Infectious Bursal Disease virus (GCA_000855485.1) proteome using the built-in Andromeda search engine. Peptide precursor mass tolerance was set at 4.5ppm, and MS/MS tolerance was set at 0.5Da. Search criteria included carbaminomethylation of cysteine as a fixed modification. Oxidation of methionine and N-terminal acetylation were selected as variable modifications. Quantification was based on Light (Arg 0, Lys 0), Medium (Arg 6, Lys 4) and Heavy (Arg 10, Lys 8) SILAC labels. Searches were performed with full tryptic digestion, a minimum peptide length of 7 amino acids, and a maximum of 2 missed cleavages were allowed. The reverse database search option was enabled and the maximum false discovery rate for both peptide and protein identifications were set to 0.01. Quantitation was performed using a mass precision of 2ppm and the iBAQ parameter was enabled. Identification and quantifications were based on a minimum of two unique peptides per protein. Contaminants (as defined in the default Maxquant list), reverse identifications, and proteins only identified by site were excluded from further analysis."],"omics_type":["Proteomics"],"labhead":["Ian Goodfellow"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["University of Cambridge"],"species":["Gallus Gallus (chicken)"],"submitter_mail":["frederic.sorgeloos@gmail.com"],"publication":["Not available"],"submitter_affiliation":["Institut national de la recherche scientifique"],"submitter_country":["Canada"],"additional_accession":[]},"is_claimable":false,"name":"Combined transcriptomic and proteomic analysis of chicken DF-1 cells following innate immune stimulations","description":"The goal of our study was to experimentally quantify both at the transcriptomic and proteomic level the effects of comprehensive innate immune stimulations in chicken. To this end, SILAC-labeled chicken DF-1 cells were mock-treated or treated with either ChIFN1 (1000 IU/mL for 6h), transfected poly (I:C) (4,25 ug/mL for 6 h) or infected with Infectious Bursal Disease Virus strain PBG-98 (IBDV, MOI 5 for 8h). Total cellular RNA was extracted using RNeasy Mini Kit (QIAGEN) and Illumina libraries were prepared and sequenced. In parallel, proteins were extracted and processed for SILAC-based quantitative mass-spectrometry. Samples were run on a LTQ-Velos Orbitrap tandem mass spectrometer and the data processing and quantification were performed by the MaxQuant 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