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Heller"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry"],"software":[""],"submitter_keywords":["Semliki forest virus","Mouse hepatitis virus","Stress granules","Proximity labeling"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077432"],"tissue":["Cell Culture","Fibroblast"],"sample_protocol":["Recombinant mouse fibroblast cells (17Cl1) expressing a G3BP1-APEX2-GFP fusion protein were propagated in two batches on SILAC medium containing normal (L-arginine: 12C6, 14N4; L-lysine: 12C6, 14N2; Thermo Fisher) or heavy isotope labeled (L-arginine: 13C6, 15N4; L-lysine: 13C6, 15N2; Cambridge Isotope laboratories) L-arginine and L-lysine. For the experiments, cells were seeded in 10cm dishes and infected after two days with MHV at MOI 5 (Exp 1) or 10 (Exp 2/3) or SFV at an MOI of 10. For oxidative stress samples, cells were treated with sodium arsenite (250uM) for 30min. APEX2-based proximity labeling was performed at different time points (SG peak: MHV 8hpi / SFV 5hpi; pre SG: MHV 4hpi / SFV 2.5hpi; post SG: MHV 14hpi / SFV 9hpi) by incubating cells with biotin phenol (Exp 1: 0.5mM; Exp 2/3: 2.5mM) for 30min before adding 1uM H2O2. For negative labeling control samples, no BP was added to the labeling medium. Labeling reaction was quenched after 1min by three washes with quencher solution (5mM Trolox, 10mM sodium ascorbate, 10mM sodium azide in PBS) and cells were lysed in 1ml lysis buffer (50 mM Tris-HCl pH 7.4, 500mM NaCl, 0.2% SDS, 2% Triton X-100, 1x cOmplete Mini Protease inhibitor cocktail Roche, 5 mM Trolox, 10 mM sodium ascorbate, and 10 mM sodium azide in H2O). Lysates were homogenized using sonicator or MagNA lyser tubes and protein concentration was determined by 660nm protein assay (Pierce). Heavy and light lysates to compare were mixed in a 1:1 protein ratio (500ug each) and affinity capture of biotinylated proteins was performed by incubation of lysate mixtures on streptavidin-coated magnetic beads (Exp 1: 100ul / Exp 2/3: 500ul, Pierce) over night at 4C. Beads were subjected to a stringent wash procedure: two washes with buffer 1 (2% SDS in H2O), one wash with buffer 2 (2M Urea, 10mM Tris-HCl pH 7.4), two washes with buffer 3 (0.1% (w/v) deoxycholate, 1% (vol/vol) Triton X-100, 1mM EDTA, 500mM NaCl, 50mM HEPES pH 7.5 in H2O), two washes with buffer 4 (0.5% (w/v) deoxycholate, 0.5% (vol/vol) NP-40, 1mM EDTA, 250mM LiCl, 10mM Tris-HCl pH 7.4 in H2O) and a final wash with 50mM Tris-HCl pH 7.4. Purified proteins were eluted in elution buffer (75mM Tris pH 6.8, 12% glycerol, 3% SDS, 6% β-mercaptoethanol, 10mM biotin). Eluates were fractionated by SDS-PAGE.   The samples were digested in-gel and subjected to liquid chromatography tandem mass spectrometry (LC-MS/MS). In short, the gel cubes were reduced, alkylated and digested by trypsin as described previously [1]. After loading, peptides were eluted in back flush mode onto the analytical self-packed nano-column (AcquityTM CSH C18, 1.7µm, 100A, 0.075 mm i.d. x 200mm length, Waters, Baden, Switzerland) using an acetonitrile gradient of 5% to 40% solvent B (0.1% Formic Acid in water/acetonitrile 4,9:95) in 60 min at a flow rate of 350nL/min. The column effluent was directly coupled to a Fusion LUMOS mass spectrometer (Thermo Fischer, Bremen; Germany) via a nano-spray ESI source. Data acquisition was made in data dependent mode with precursor ion scans recorded in the orbitrap with resolution of 120’000 (at m/z=250) parallel to top speed fragment spectra of the most intense precursor ions in the Linear trap for a cycle time of 3 seconds maximum.  [1] Gunasekera K, Wüthrich D, Braga-Lagache S, Heller M, Ochsenreiter T. Proteome remodelling during development from blood to insect-form Trypanosoma brucei quantified by SILAC and mass spectrometry. BMC Genomics. 2012;13(1):556."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Mass spectrometry data was analyzed as previously described [1]. Briefly, proteins were identified by MaxQuant [versions 1.5.4.1, 1.6.14.0, and 2.5.1.0 for the 2019 (Exp 1), 2023 (Exp 2), and 2025 (Exp 3) data, repectively] against mouse protein database (SwissProt, releases 2018_04, 2023_03, and 2025_01), MHV strain A59 database (UniprotKB, release March 2023) and a curated list of SFV proteins. The initial precursor mass tolerance was set to 10 ppm, and that of the fragment peaks to 0.4 Da. Enzyme specificity was set to strict trypsin, and a maximum of three missed cleavages were allowed. Carbamidomethylation on cysteine was set as a fixed modification, while methionine oxidation, and protein N-terminal acetylation were set as variable modifications. After removal of common contaminants and inversing reversed ratios, 1-sample t-tests were performed on the MaxQuant normalized ratios, provided the ratios were measured in all replicates. Adjusted p-values for multiple testing were corrected by the R fdrtool package [2]. Protein intensities were furthermore calculated as the median of the log2-transform of the intensities of all peptides allocated to the protein, using the heavy and light channels as separate samples, as previously described [3]. Normalization was performed by the global median method, whereby the viral proteins as well as any previously known SG proteins (Curated list by Markmiller and colleagues [3]) were excluded from the calculation of the normalization coefficients. Missing protein intensities were imputed in the following manner, provided there was at least two identifications in at least one group: if there was at most two identifications in the group of replicates, the missing values were drawn from a Gaussian distribution of width 0.3 centered at the sample distribution mean minus 2.5x the sample standard deviation, otherwise the Maximum Likelihood Estimation (MLE) method was used [4]. Log2 fold changes (Log2FC) between given conditions were calculated by using mean Log2 of the respective conditions. Differential expression tests were performed by applying an Empirical Bayes test [5], and the FDR-adjusted p-values (Benjamini and Hochberg multiple test correction [6]) were calculated.  [1] Heller M, Braga S, Müller N, Müller J. Transfection With Plasmid Causing Stable Expression of a Foreign Gene Affects General Proteome Pattern in Giardia lamblia Trophozoites. Front Cell Infect Microbiol. 2020 Dec 18;10:1–8. [2] Strimmer K. fdrtool: a versatile R package for estimating local and tail area-based false discovery rates. Bioinformatics. 2008 Jun 15;24(12):1461–2. [3] Markmiller S, Soltanieh S, Server KL, Mak R, Jin W, Fang MY, et al. Context-Dependent and Disease-Specific Diversity in Protein Interactions within Stress Granules. Cell. 2018;172(3):590–604.e13. [4] Silver JD, Ritchie ME, Smyth GK. Microarray background correction: maximum likelihood estimation for the normal-exponential convolution. Biostatistics. 2009 Apr 1;10(2):352–63. [5] Kammers K, Cole RN, Tiengwe C, Ruczinski I. Detecting significant changes in protein abundance. EuPA Open Proteom. 2015 Jun 1;7:11–9. [6] Benjamini Y, Hochberg Y. Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing. J R Stat Soc Series B Stat Methodol. 1995 Jan 1;57(1):289–300."],"omics_type":["Proteomics"],"labhead":["Volker Thiel"],"instrument_platform":[""],"labhead_affiliation":["Institute of Virology and Immunology (IVI), Bern and Mittelhäusern, Switzerland  Department of Infectious Diseases and Pathobiology (DIP), Vetsuisse Faculty, University of Bern, Bern, Switzerland"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["pmscf.dbmr@unibe.ch"],"publication":["10.1371/JOURNAL.PBIO.3003363"],"submitter_affiliation":["Proteomics and Mass Spectrometry Core Facility,\nDepartement for Biomedical Research,\nUniversity of Berne"],"submitter_country":["Switzerland"],"additional_accession":[]},"is_claimable":false,"name":"Proximity labeling and LC-MS/MS based identification of the stress granule microenvironment induced by different viruses","description":"To dissect and compare the protein composition of stress granules formed during infections with two different RNA viruses as well as oxidative stress, we developed a recombinant mouse fibroblast cell line stably expressing a fusion protein of the stress granule marker G3BP1 with APEX2 and GFP. When stress granules are induced in these cells, the fusion protein accumulates in the cytoplasmic condensates and allows the biotinylation of the SG proteome based on the APEX2 peroxidase. The proximity labeled proteins can then be affinity purified and identified by quantitative LC-MS/MS.  To directly compare different stressed and unstressed conditions, we combined the proximity labeling approach with stable isotope labeling of amino acids in cell culture (SILAC).   In the first experiment (Exp 1, 2019 data), we compared the SGs induced by MHV infection with canonical SGs induced by sodium arsenite treatment or the unstressed cells. In a second and third experiment (Exp 2 and 3, 2023 and 2025 data), we expanded our investigations to SGs induced by SFV infection to directly compare the SG proteome between different viruses and at different time points during infection.","dates":{"publication":"2026-08-07","submission":"2026-04-21"},"accession":"PXD077432","cross_references":{"TAXONOMY":["NEWT:3555","NEWT:71647","NEWT:35554","NEWT:32046","NEWT:544496","NEWT:2042546","NEWT:32049","NEWT:1392696","NEWT:259447","NEWT:295546","NEWT:45351","NEWT:445974","NEWT:43179","NEWT:180454","NEWT:5722","NCBITaxon:1280","NEWT:1129","NEWT:309807","NEWT:55153","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:10036","NEWT:1590","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:1147161","NEWT:638632","NEWT:263737","NEWT:224326","NEWT:1333499","NCBITaxon:79857","NEWT:1096976","NEWT:5702","NEWT:95648","NEWT:1589","NEWT:135622","NEWT:1349","NEWT:96731","NEWT:383379","NEWT:10029","NEWT:913645","NEWT:44491","NEWT:556484","NEWT:317447","NEWT:4688","NEWT:7955","NEWT:7959","NEWT:2261","NEWT:31156","NEWT:3112","NEWT:4442","NEWT:192875","NEWT:1214915","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:108061","NEWT:1316931","NEWT:224308","NEWT:3347","NEWT:511145","NEWT:931281","NEWT:4432","NEWT:658457","NEWT:1310161","NEWT:77133","NEWT:295358","NEWT:145481","NCBITaxon:79824","NEWT:2246","NCBITaxon:4563","NEWT:5755","NEWT:44689","NEWT:44447","NEWT:752555","NEWT:498211","NEWT:5759","NEWT:1736231","NEWT:5518","NEWT:398007","NEWT:1392","NEWT:498217","NEWT:498216","NEWT:2242","NEWT:11320","NEWT:286","NEWT:391619","NEWT:246196","NEWT:287","NEWT:246197","NEWT:633149","NEWT:10239","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:5507","NEWT:410661","NEWT:55571","NEWT:35500","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:4896","NEWT:1287689","NEWT:1390","NEWT:11557","NEWT:1094343","NEWT:1336795","NEWT:644042","NEWT:294","NEWT:1773","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:3711","NEWT:935293","NEWT:375146","NEWT:118698","NEWT:1616117","NEWT:263","NEWT:118696","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:408169","NEWT:44664","NEWT:47946","NEWT:3702","NEWT:243277","NEWT:7067","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:33548","NEWT:274","NEWT:408172","NEWT:408170","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:1436733","NEWT:460519","NEWT:1247411","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:9483","NEWT:333760","NEWT:1513458","NEWT:1233681","NCBITaxon:40559","NEWT:506599","NEWT:84588","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:300852","NEWT:1502","NEWT:376686","NEWT:95486","NEWT:508771","NEWT:1883446","NEWT:253","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:93062","NCBITaxon:4932","NEWT:644223","NEWT:235443","NEWT:108458","NEWT:272623","NEWT:272624","NEWT:320637","NEWT:983964","NEWT:118499","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:3988","NEWT:1255228","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:3983","NEWT:352472","NEWT:1071661","NEWT:360094","NEWT:470","NEWT:41364","NEWT:1313","NEWT:39491","NCBITaxon:5811","NEWT:29491","NEWT:2014887","NEWT:33952","NEWT:261756","NEWT:571256","NEWT:40483","NEWT:63366","NEWT:63367","NEWT:272634","NEWT:9031","NEWT:1872122","NEWT:7091","NEWT:141262","NEWT:108931","NEWT:1055524","NEWT:4087","NEWT:9778","NEWT:306","NEWT:150475","NEWT:303","NEWT:267872","NEWT:7111","NEWT:347515","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:4090","NEWT:4092","NEWT:9541","NEWT:8694","NEWT:4093","NEWT:4096","NEWT:8692","NEWT:185579","NEWT:941442","NEWT:13076","NEWT:1226408","NEWT:7108","NEWT:40479","NEWT:43989","NEWT:4076","NEWT:317","NEWT:1006581","NEWT:885318","NEWT:39488","NEWT:550","NEWT:4081","NEWT:273068","NEWT:554","NEWT:98334","NEWT:451516","NEWT:4084","NEWT:63577","NEWT:36185","NEWT:1225786","NEWT:7574","NEWT:1715256","NEWT:30640","NEWT:575412","NEWT:929793","NEWT:29204","NEWT:28112","NEWT:114155","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:6239","NEWT:162425","NEWT:216257","NEWT:102169","NEWT:9986","NEWT:4054","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8655","NEWT:1263854","NEWT:118503","NEWT:2059687","NEWT:160488","NEWT:28104","NEWT:207559","NEWT:407821","NCBITaxon:2","NEWT:985076","NEWT:1215323","NEWT:986","NEWT:52641","NEWT:7159","NEWT:28532","NEWT:353152","NEWT:8496","NEWT:27448","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:243230","NEWT:1080772","NEWT:519","NEWT:8479","NEWT:8485","NEWT:6063","NEWT:49240","NEWT:104395","NEWT:6289","NEWT:6287","NEWT:300641","NEWT:727","NEWT:9796","NEWT:725","NEWT:469008","NEWT:256318","NEWT:9321","NEWT:206411","NCBITaxon:6191","NEWT:596153","NEWT:229533","NEWT:1836","NEWT:214053","NEWT:80863","NEWT:105231","NEWT:52638","NEWT:57075","NEWT:4097","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:9785","NEWT:6279","NEWT:1123869","NEWT:9544","NEWT:7370","NEWT:83906","NCBITaxon:780","NCBITaxon:1502","NEWT:6282","NEWT:1134506","NEWT:38783","NEWT:4006","NEWT:6426","NCBITaxon:5476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