{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD059662/128_OF_mousebrain_KI_vs_C57_Prp_interactome_iTRAQ_3_6_4_7_5_8_9KO_1KO_C18_1-3_Trypsin.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD059662/128_OF_mousebrain_KI_vs_C57_Prp_interactome_iTRAQ_3_6_4_7_5_8_9KO_1KO_C18_1_Trypsin.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD059662/128_OF_mousebrain_KI_vs_C57_Prp_interactome_iTRAQ_3_6_4_7_5_8_9KO_1KO_C18_2_Trypsin.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD059662/128_OF_mousebrain_KI_vs_C57_Prp_interactome_iTRAQ_3_6_4_7_5_8_9KO_1KO_C18_3_Trypsin.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["joel.watts@utoronto.ca"],"submitter":["Gerold Schmitt-Ulms"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Prion Disease"],"software":[""],"submitter_keywords":["Knock-in mice","Prion","Bank voles","Mass spectrometry","Protein-protein interactions"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD059662"],"tissue":["Brain"],"sample_protocol":["Time-controlled transcardiac perfusion crosslinking TcTPC was performed as previously described (Schmitt-Ulms et al., 2004). Briefly, male WT C57BL/6 mice, kiBVM, and PrP-/- mice at approximately 3 months of age were anesthetized with isoflurane and then perfused via the transcardiac route with PBS for 2 min. Following this, mice were perfused with freshly made 2% (w/v) formaldehyde (pH 7.3 in 1X PBS) for 6 min. Successful perfusion was gauged by the development of tail rigidity. The brains were then dissected and post-fixed in 2% formaldehyde for a total of 9 min (includes dissection time). Following fixation, brains were snap frozen in liquid nitrogen and stored at -80 C.    Immunoprecipitation of crosslinked PrPC-containing complexes KappaSelect beads (Cytiva #17-5458-01) beads were washed, equilibrated, and then conjugated with HuM-D18 Fab by rotation overnight at 4 C in lysis buffer [150 mM Tris-HCl pH 8.3, 150 mM NaCl, 0.5% (w/v) deoxycholic acid, 0.5% (v/v) NP-40]. The crosslinked brains were homogenized as described above in lysis buffer and then ultracentrifuged at 100,000x g for 1 h at 4 C to remove debris. The brain homogenates were then quantified using the BCA assay and then normalized to the lowest protein concentration amongst all replicates. Homogenates were then incubated with the HuM-D18-conjugated KappaSelect beads overnight at 4 C in an end-over-end rotator. Following capture, beads were washed 3 times with lysis buffer and then 3 times with a more stringent lysis buffer containing a higher salt concentration (500 mM NaCl). Prior to elution, beads were washed briefly with a buffer containing 10 mM HEPES, pH 8. Captured proteins were eluted by pH drop using a buffer containing 0.2% (v/v) trifluoroacetic acid in 20% (v/v) acetonitrile.  Sample reduction, alkylation, trypsinization, and iTRAQ labeling Eluates from the immunoprecipitation of PrPC-containing complexes were dried to a volume of 5 µL using a SpeedVac centrifuge set at 37 C. The dried eluates were denatured by addition of 9 M deionized urea and then reduced by incubation with Tris(2-carboxyethyl)phosphine (TCEP) in 500 mM triethyl ammonium bicarbonate buffer at 60 C for 30 min. After allowing the samples to cool, sulfhydryl groups were alkylated by treatment with 4-vinylpyridine for 1 h at 22 C. Urea concentration was diluted to 1.25 M in 500 mM triethylammonium bicarbonate buffer prior to the addition of mass spectrometry grade trypsin (Thermo Fisher Scientific #90057). Trypsin digestions were done overnight at 37 C. The digested mixture was purified with reverse phase resin, paired with or without a strong cation exchange. A portion of the trypsinized samples were reacted with 8-plex iTRAQ reagents (SCIEX #4390811) according to the manufacturer’s instructions and then combined. Prior to LC-MS/MS, peptides were purified using OMIX C18 pipette tips (Agilent #A57003100)."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Protein identification and quantification The MS2 data sets were analyzed and converted into peptide sequences with Proteome Discoverer software (version 1.4) using the built-in Mascot and Sequest HT search algorithms and search parameters as previously described (Ghodrati et al., 2018). The mouse Uniprot database was used as a reference with the manual inclusion of the BVPrP sequence. To stringently filter the mass spectra, the Percolator algorithm within Proteome Discoverer was used to estimate the false discovery rate based on the q-value. The Reporter Ions Quantifier algorithm in Proteome Discoverer was utilized to determine the relative quantification of iTRAQ-labeled peptides using the MS3 data. For the unlabeled datasets, the number of PSMs for the 3 biological replicates of the kiBVM samples, the 3 biological replicates of the WT C57BL/6 samples, and the two biological replicates of the PrP-/- samples were averaged for each identified protein. Hits were then sorted by the average number of PSMs in the kiBVM or WT samples minus the average number of PSMs in the PrP-/- samples. For a protein to be included in the list of identified interactors, its identification had to be supported by at least 2 unique peptides as well as an average kiBVM:average PrP-/- or an average WT:average PrP-/- PSM ratio of at least 3.  Statistical analysis Statistical comparisons were conducted using GraphPad Prism software (version 10), with a significance threshold of P < 0.05. iTRAQ reporter ion enrichment ratios, relative PrPC levels in brain homogenates, and levels of detergent-insoluble PrP were compared using two-tailed Welch’s t-tests, which do not assume equal standard deviations between sample groups."],"omics_type":["Proteomics"],"labhead":["Joel Watts amd Gerold Schmitt-Ulms"],"instrument_platform":[""],"labhead_affiliation":["Biochemistry"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["10.1016/J.NBD.2025.106802"],"submitter_mail":["g.schmittulms@utoronto.ca"],"submitter_affiliation":["University of Toronto"],"submitter_country":["Canada"],"additional_accession":[]},"is_claimable":false,"name":"The brain interactome of a permissive prion replication substrate","description":"Bank voles are susceptible to prion strains from many different species, yet the molecular mechanisms underlying the ability of bank vole prion protein (BVPrP) to function as a universal prion acceptor remain unclear. Potential differences in molecular environments and protein interaction networks on the cell surface of brain cells may contribute to BVPrP’s unusual behavior. To test this hypothesis, we generated knock-in mice that express physiological levels of BVPrP (M109 isoform) and employed mass spectrometry to compare the interactomes of mouse (Mo) PrP and BVPrP following mild in vivo crosslinking of brain tissue. Substantial overlap was observed between the top interactors for BVPrP and MoPrP, with established PrP-interactors such as neural cell adhesion molecules, subunits of Na+/K+-ATPases, and contactin-1 being equally present in the two interactomes. We conclude that the molecular environments of BVPrP and MoPrP in the brains of mice are very similar. This suggests that the unorthodox properties of BVPrP are unlikely to be mediated by differential interactions with other 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