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Cameron"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Sars-cov-2","Affinity purification-mass spectrometry","Interactomics","Macrodomain 1","Adp-ribose","Virus-host protein interactions"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069398"],"tissue":["Hepatocyte","Epithelial Cell","Cell Culture"],"sample_protocol":["HEK293T and A549 cells were grown using Dulbeccos’ Modified Eagle’s Medium (high glucose) supplemented with 10% fetal bovine serum, 1% penicillin/streptomycin and 1% glutamine. Cell cultures were maintained at 37°C and 5% CO2.  HEK293T cells were transiently transfected using calcium phosphate method with wildtype Mac 1 (WT), mutant Mac1 (N40A or N40D) or green fluorescent protein (GFP). Media was changed 16 hours post-transfection and the cells were harvested after 24 hours. A549 cells were transiently transfected with using FuGENE 4k (FuGENE, 4K-1000) according to manufacturer’s protocol with GFP, WT Mac1, or Mac1 N40D plasmid in antibiotic-free medium. Media was replaced with antibiotic-supplemented media 16 hours post transfection and the samples were harvested after 24 hours.  Cells were first washed with phosphate buffered saline (PBS) and then scraped and collected in cold 1 mM ethylenediaminetetraacetic acid (EDTA) in PBS. Cells were then pelleted at 200 x g for 5 minutes at 4°C and washed twice with PBS. The remaining PBS was removed by aspiration. Cells were lysed in 200 µL TNI buffer (50 mM Tris pH 7.5, 150 mM NaCl, 0.5% IGEPAL-CA-630) supplemented with Roche cOmplete protease inhibitor on ice for 15 minutes followed by 15 minutes sonication at room temperature. Lysates were cleared by centrifugation at 21.1 x g for 15 minutes at 4°C. Protein concentration was determined using BCA assay (Thermo, 23225) and normalized to the lowest concentration in the sample set.  For crosslinking experiments, cells were washed with PBS, scraped and collected in a tube, and washed with PBS again as described above. DSP (Fisher, PI22585) was dissolved in DMSO for a 50 mM 100x stock immediately before use. DSP was diluted 100x in 1 mL PBS for a working concentration of 0.5 mM, added directly to cells, and incubated rocking for 30 minutes at room temperature. The DSP was then quenched with 100 µL of 1 M Tris pH 7.5 and incubated for 15 minutes at room temperature. Two washes were performed with PBS and lysis procedure was performed as described previously with TNI lysis buffer.  4B Sepharose beads (Sigma-Aldrich, 4B200) and Streptactin beads (IBA, 2-5030-002) were pre-washed 4x with TNI buffer. Lysates were pre-cleared with 20 µL 4B Sepharose beads slurry per sample rotating for 1 hour at 4°C. Beads were cleared at 400 x g for 5 min at 4°C and pre-cleared lysate was added to 20 µL of FLAG bead slurry per sample, rotating overnight at 4°C. Resin was washed 4x with TNI buffer, cleared by centrifugation at 400 x g, and dried with 30G needle after the final wash. Resin-bound proteins were eluted twice in 3x modified Laemelli buffer (6% SDS, 62.5 mM Tris pH 6.8) for 30 minutes at room temperature and 15 minutes at 37°C. Eluted proteins were precipitated via methanol/chloroform water (3:1:3) and washed 3x with methanol. Pellets were air-dried before resuspension with Rapigest SF (Waters) followed by the addition of 10 µL of 0.5 HEPES (pH 8.0). Volume was then adjusted to 47.5 µL with H2O. Proteins were reduced with 5 mM tris(2-carboxyethyl)phosphine (TCEP) (Sigma, 75259) for 30 minutes at room temperature followed by alkylation with 10 mM iodoacetamide (Sigma, I6125). Proteins were digested overnight at 37°C shaking at 750 rpm using 0.5 µg of Trypsin/Lys-C protease mix (Pierce, A40007). TMTpro 16plex reagents (Thermo Fisher, 44520) in 40% v/v acetonitrile were used to label the digested peptides for 1 hour at room temperature and quenched with 0.4% w/v ammonium bicarbonate for 1 hour at room temperature. Samples were pooled acidified using 5% v/v formic acid (Fisher, A117) to reach a pH of 2. The sample was then concentrated to 1/3 of its volume using a speedvac and resuspended in Buffer A (97% water, 2.9% acetonitrile, 0.1% formic acid, v/v/v). Cleaved Rapigest SF was removed by centrifugation for 30 minutes at 21,000 x g."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Peptide identification and TMT-based protein quantification was carried out using Proteome Discoverer 2.4. MS/MS spectra were extracted from Thermo Xcalibur .raw file format and searched using SEQUEST against a Uniprot human proteome database (accessed 03/2014 and containing 28,860 entries) supplemented with the SARS-CoV-2 Macrodomain 1 sequence. The database was curated to remove redundant protein and splice-isoforms. Searches were carried out using following parameters: 20 ppm peptide precursor tolerance, 0.02 Da fragment mass tolerance, minimum peptide length of 6 amino acids, trypsin cleavage with a maximum of two missed cleavages, dynamic methionine modification of +15.995 Da (oxidation), dynamic protein N-terminus +42.011 Da (acetylation), −131.040 (methionine loss), −89.030 (methionine loss + acetylation), static cysteine modification of +57.0215 Da (carbamidomethylation), and static peptide N-terminal and lysine modifications of +304.2071 Da (TMTpro 16plex). Raw TMT abundances from Proteome Discoverer were median normalized and log2 transformed within each 16-plex. The expression changes between Mac1 samples and DMSO samples were calculated for each protein and tested for significance with a paired t-test. Proteins with a log2(fold change) greater than two standard deviations away from 0 and p-value less than 0.05 were considered interactors and were combined from WT Mac1 and Mac1 N40D comparisons."],"omics_type":["Proteomics"],"labhead":["Lars Plate"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Departments of Chemistry, Biological Sciences, Vanderbilt University and Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center"],"species":["Homo Sapiens (human)"],"publication":["10.3390/V18060587"],"submitter_mail":["crissey.d.cameron@vanderbilt.edu"],"submitter_affiliation":["Vanderbilt University"],"submitter_country":["United States"],"doi":["10.6019/PXD069398"],"additional_accession":[]},"is_claimable":false,"name":"Interactomics of SARS-CoV-2 Macrodomain 1 Reveals Putative Clients of ADP-ribosyl Hydrolase Activity","description":"Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has greatly impacted public health due to high rates of transmissibility and mutation during the COVID-19 pandemic. Macrodomain 1 (Mac1) of non-structural protein 3 remained well-conserved across variants and is critical for suppression of host immune response to infection, making Mac1 a promising target for therapeutic development. Mac1 binds and cleaves the post-translational modification ADP-ribose and is hypothesized to have a downstream effect on host interferon response, but the exact cellular targets of Mac1 are still unknown. Characterizing the substrates of Mac1 ADP-ribosyl hydrolase activity using a catalytically inactive mutant N40D can reveal critical virus-host interactions to identify protein targets of Mac1 and reveal mechanisms of host interferon suppression. Here, we co-immunoprecipitated WT Mac1 and Mac1 N40D from HEK293T and A549 cell lines and quantified changes in protein interactions by TMT-multiplexed tandem mass spectrometry.  We identified interactions between Mac1 and ADP-ribosylated substrates involved in DNA damage response, cytoskeletal components, and cell cycle regulation. Additionally, several members of the TRiC complex involved in protein folding were selectively enriched with mutant Mac1 from A549 cells. These findings suggest a novel role of Mac1 in regulating host protein folding.","dates":{"publication":"2026-05-22","submission":"2025-10-13"},"accession":"PXD069398","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NE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