{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep3-control.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep1-ubp.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep2-control.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep1-control.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep2-ubp.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep3-ubp.raw"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep2-control.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep3-control.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep1-ubp.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep1-control.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep3-ubp.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep2-ubp.mgf"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep3-control.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep1-control.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep3-ubp.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep1-ubp.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep2-ubp.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067094/morph-ms-lnc455-rep2-control.mzTab"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["kmagor@ualberta.ca"],"submitter":["Renald James  Legaspi"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Type i ifn","Duck","Lncrna","Morph-ms"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067094"],"tissue":["Fibroblast"],"sample_protocol":["Antisense (complimentary) probes against lnc455 were designed using ChIRP probe designer tool (LGC Biosearch) with a masking level of 2, minimum spacing length of 60 nt and oligo length of 25 nt. To ensure specificity, all the oligos were manually screened for non-specific binding using NCBI blast. A common binding sequence 5’- TTACACTCGGACCTCGTCGACATGCATT-3’ was added towards the 3’ end of all oligos. The probes with standard desalting purification were ordered from Integrated DNA Technologies (IDT). The biotinylated universal oligo, which had TEG-biotin attached to both the 5’ and 3’ ends, was designed to be complementary to the common sequence was HPLC purified and ordered from Integrated DNA Technologies (IDT). Oligos were dissolved in IDT Duplex buffer to a final concentration of 100 μM. To achieve an equimolar concentration of all the complementary probes with the biotinylated oligo, 5 μL from each were pooled together, resulting in a final concentration of 100 μM. The probes were annealed to the universal biotinylated oligo at 94°C for 2 minutes followed by cooling. Annealing was confirmed using 5% agarose gel electrophoresis.  DF1 cells were seeded at 7 × 106 cells in 100 mm petri dish. After 24 hours, cells were transfected with 1.0 µg of duck MAVS using Lipofectamine 2000. After 24 hours post-seeding, cells were washed with PBS and irradiated with 200mJ of UV. Cells were washed twice with PBS and lysed with IP lysis buffer (Pierce™ MS-Compatible Magnetic IP Kit) containing a proteinase inhibitor cocktail (Roche). Cell lysates were then incubated with 1000 pmol of the annealed probes at 37°C overnight at 4°C followed by streptavidin magnetic bead pulldown. The beads were washed according to manufacturer’s instructions. Final wash was done with 25 mM ammonium bicarbonate, and 10% of the beads was the subjected to qRT-PCR. The rest of the samples were sent to Alberta Proteomics and Mass Spectrometry Facility for mass spectrometry analysis.  Trypsin digestions were performed on the beads.  The beads were washed 3 times (20mM ammonium bicarbonate), reduced (10mM DTT in 50mM ammonium bicarbonate), alkylated (50mM iodoacetamide in 50mM ammonium bicarbonate) and washed twice before digestion overnight at at 37C  (Promega sequencing grade modified trypsin).  Digestion was stopped by lowering the pH to 2 with the addition of 25% TFA.  Samples were cleaned up before analysis using C18 ZipTip pipette tips (ZTC18S, Millipore).Peptides were separated and analysed using a Vanquish Neo UHPLC system (Thermo Scientific) and an EASY-Spray capillary HPLC column (ES75150, Thermo Scientific) coupled to an Orbitrap Exploris 480 mass spectrometer (Thermo Scientific). The mass spectrometer was operated in data-dependent acquisition mode with a resolution of 60,000 and m/z range of 350–1700. Multiply charged ions were fragmented via HCD dissociation with an NCE of 28, and spectra of their fragments were recorded in the orbitrap at a resolution of 15,000."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data was processed using Proteome Discoverer (Thermo Scientific, version 3.0) and the database (Uniprot, Gallus gallus, UP000000539) was searched using SEQUEST (Thermo Scientific).  Search parameters included a strict false discovery rate (FDR) of .01, a relaxed FDR of .05, a precursor mass tolerance of 10ppm and a fragment mass tolerance of 0.02Da.  Peptides were searched with carbamidomethyl cysteine as a static modification and oxidized methionine, and deamidated glutamine and asparagine as dynamic modifications."],"omics_type":["Proteomics"],"labhead":["Katharine Edens Magor"],"instrument_platform":[""],"labhead_affiliation":["1 Department of Biological Sciences, University of Alberta, Edmonton, AB, Canada 2 Li Ka Shing Institute of Virology, University of Alberta, Edmonton, AB, Canada"],"submission_type":["COMPLETE"],"species":["Gallus Gallus (chicken)"],"submitter_mail":["renaldja@ualberta.ca"],"publication":["41807513 Legaspi RJ, Magor KE. Duck lncRNA lnc455 enhances RIG-I/MAVS type I interferon signaling by modulating hnRNPAB-mediated regulation of MAVS signaling. Sci Rep. 2026 16(1):12925 10.1038/s41598-026-42849-6"],"submitter_affiliation":["University of Alberta"],"submitter_country":["Canada"],"doi":["10.6019/PXD067094"],"pubmed_title":["Duck lncRNA lnc455 enhances RIG-I/MAVS type I interferon signaling by modulating hnRNPAB-mediated regulation of MAVS signaling."],"pubmed_authors":["Legaspi Renald James RJ, Magor Katharine E KE"],"additional_accession":[]},"is_claimable":false,"name":"Identification of RNA-binding protein interactors of duck lncrna (lnc455) using Multiple Oligo-assisted RNA Pulldown with Hybridization followed by Mass Spectrometry (MORPH-MS)","description":"This project used MORPH-MS to identify proteins that interact with a duck lncRNA called lnc455, which is linked to antiviral responses. While lnc455 was predicted to enhance RIG-I/MAVS signaling, its effects appeared to be indirect. Using MORPH-MS, we mapped the lncRNA’s binding partners and uncovered several proteins known to suppress interferon signaling. This highlights how lnc455 may support antiviral immunity by blocking these negative regulators. The study also shows how MORPH-MS can uncover RNA–protein interactions in non-model species like 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