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Arapidi"],"technology_type":["Immunopeptidomics","Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077041"],"tissue":["Cell Culture"],"sample_protocol":["Cell lines.The following cell lines were used in this study: Jurkat (TIB-152, ATC, USA), Raji (CCL-86, ATCC), K562 (CCL-243, ATCC), and MDA-MB-231 (CRM-HTB-26, ATCC). Jurkat, Raji, and K562 suspension cell lines were cultured in RPMI 1640 medium (C330p, PanEco, Russia) containing 10% FBS (26140079, Gibco, USA), 50 U/ml gentamicin (Dalkhimfarm, Russia), and 1.6 mM glutamine GlutaMAX (35050061, Gibco). The adherent cell line MDA-MB 231 was cultured in DMEM (C420p, PanEco), 10% FBS, 50 U/ml gentamicin, and 1.6 mM glutamine. To detach the adhesion cell culture, 0.05% trypsin (15050057, Gibco) in Versene (P080p, PanEco) was used.All cell lines were cultured to the required concentration, then centrifuged for 5 min at 150 g (Eppendorf 5804 R, USA). The cell pellet was washed three times with Dulbecco's phosphate buffered saline, pH 7.4 (PanEco). The supernatant was collected, and the cell pellet was stored at -80°C until further experiments.To obtain antibodies to HLA I, a cell culture of the HB 95 hybridoma (producer of HLA-ABC w6/32 antibodies, ATCC) was cultivated. Primary cultivation was carried out in DMEM F12 Advanced medium (12634010, Gibco) with the addition of 10% FBS (inactivation at 56℃ for 30 minutes), 50 units/ml gentamicin, 1.6 mM glutamine. When the density of 600 thousand cells/ml was reached, the medium was changed to one containing half as much FBS. Thus, the concentration of FBS in the medium was gradually reduced. When the FBS concentration reached 0.5%, the medium was replaced with HyClone ADCF-mab (Cytiva, USA), 50 units/ml gentamicin, 1.6 mM glutamine. Cultivation in this medium until 80-90% of the cells died, then the supernatant containing antibodies was collected. Antibody concentrations in the cell medium were measured using the Easy-Titer mouse IgG Assay (23300, Thermo Scientific, USA) according to the manufacturer's recommendations.All cells were regularly tested for mycoplasma contamination and cultured at 37°C and 5% CO2.Preparation of cell lysates.One of the following lysis buffers was added to the frozen-dried cell pellet on ice:Lys 1 – 1% NP-40, 150 mM NaCl, 50 mM Tris-HCl (pH 7.4) with cOmplet Protease Inhibitor Cocktail (11697498001, Roche, Switzerland).Lys 2 – 10 mM CHAPS/PBS with cOmplet Protease Inhibitor Cocktail. Sonication was also performed (150 W at 50% pulse duration for 3 minutes on ice).Lys 3 – 0.25% sodium deoxycholate, 0.2 mM iodoacetamide, 1 mM EDTA, cOmplet Protease Inhibitor Cocktail, 1 mM PMSF, 1% octyl-D-glucopyranoside in PBS.Lys 4 – 0.2 mM iodoacetamide, 1 mM EDTA, cOmplet Protease Inhibitor Cocktail, 1 mM PMSF, 1% octyl-β-D-glucopyranoside in PBS.The cells were lysed for 1 hour on a rotator at +4 °C, then centrifuged for 15 minutes at 14,000 g and the supernatant was collected for further work.Immunoprecipitation of HLA complexes using magnetic beads.For HLA I immunoprecipitation, 125 μl of Pierce Protein A/G Magnetic Beads (88803, Thermo Scientific) were used per 1 ml of lysate. Immunoprecipitation was performed according to the manufacturer's protocol. For one HLA I extraction, 125 μl of magnetic beads and 50 μg of w6/32 antibodies (MA1-80123, Invitrogen) were used. An aliquot of the magnetic beads was placed in 175 μl of wash buffer (2.7 mM KCl, 0.01 M Na2HPO4, 1.8 mM KH2PO4, 0.15 M NaCl, 0.05% Tween-20), then the magnetic beads were washed twice with 1 ml of wash buffer. w6/32 antibodies were added to the magnetic particle pellet and incubated for 1 hour. Then, 1 ml of clarified cell lysate was incubated with magnetic particles coated with specific antibodies for 1 hour at RT. After incubation, the particles were washed five times with phosphate-buffered saline (PBST), pH 7.4, containing 0.05% Tween-20. Precipitated peptide-HLA I complexes were eluted from the magnetic particles with 250 μl of 10% acetic acid. Peptides were purified by reverse-phase chromatography.Peptide purification.Isolated peptides were separated from HLA and desalted using an Extraction Manifold (Waters, USA) on Discovery DSC-18 columns (1 ml Tubes 100 mg, Supelco). The sorbent was activated with 100% methanol (MeOH), after which the columns were conditioned with a double volume of 1% MeOH in 0.1% trifluoroacetic acid (TFA). The sample was then loaded and washed with 2 ml of 1% MeOH in 0.1% TFA. Elution was carried out with 50% MeOH in 0.1% TFA. Purified peptides were dried in a Concentrator plus centrifugal concentrator (Eppendorf, Germany) and frozen at -80°C until LC-MS/MS analysis. Immediately prior to LC-MS/MS analysis, samples were dissolved in 15 µL of 1% MeOH in 0.1% TFA.Chromatographic mass spectrometric analysis of HLA I ligand peptides.Mass spectrometric analysis was performed on a Q Exactive HF Hybrid Quadrupole-Orbitrap Mass Spectrometer (Thermo Fisher Scientific). The chromatographic system was assembled using a pre-column-column scheme (column: sorbent - Aeris Peptide XB-C18 (Agilent, USA), length - 15 cm, internal diameter - 75 μm, particle size - 3 μm, pore diameter - 120 A, pre-column: sorbent - Aeris Peptide XB-C18, (Agilent, USA), length - 1 cm, internal diameter - 100 μm, particle size - 3 μm, pore diameter - 120 A, solvent A - 98.9% H2O, 1% MeOH, 0.1% formic acid; solvent B - 99.9% ACN, 0.1% formic acid), the chromatographic columns were thermostatted at 50°C. On the pre-column, application and washing were carried out for 10 minutes at a flow rate of 2 μl/min of solvent A. Separation was carried out at 300 nl/min, gradient: 1 min – 95% solvent A, 5% solvent B; The acetonitrile content was then increased linearly over 120 minutes to 60% solvent A and 40% solvent B. The chromatographic system was then washed with 95% solvent B for 10 minutes, followed by a 17-minute wash with 95% solvent A and 5% solvent B. Mass spectral acquisition mode: mass spectral acquisition time – 250 ms, mass/charge ratio range from 300 to 1250 m/z, criteria for preferential selection of ions for isolation and fragmentation – charge 2-5, the number of parent ions sampled in each cycle – no more than 50, minimum intensity – 100 counts/s. After the first analysis, the ion was forcibly excluded from the list of ions for fragmentation for 15 s. Fragmentation parameters: fragmentation spectra accumulation time – 100 ms, mass/charge ratio range from 100 to 2000 Th, voltage in the collision cell varied linearly from 25 V to 55 V, full cycle time – no more than 5.3 s."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw data files acquired on the Q Exactive HF-X were converted to Mascot generic format (mgf) peak lists using MSConvert (ProteoWizard Software Foundation) with the following parameters: “--mgf --filter peakPicking true [1,2]”. The resulting peak lists were searched against the UniProt Knowledgebase (taxon human) concatenated with a reversed decoy set using MASCOT (version 2.5.1, Matrix Science Ltd., UK) and X! Tandem (ALANINE, 2017.02.01, The Global Proteome Machine Organization). The precursor and fragment mass tolerance were set at 20 ppm and 50 ppm, respectively. The database search parameters included no enzyme or possible post-translational modification (PTM). For X! Tandem, additional parameters were selected to check for protein N-terminal residue acetylation, peptide N-terminal glutamine ammonia loss, or peptide N-terminal glutamic acid water loss."],"omics_type":["Proteomics"],"labhead":["Georgij Arapidi"],"instrument_platform":[""],"labhead_affiliation":["Head of System Biology Lab. at Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"submitter_mail":["arapidi@gmail.com"],"publication":["Not available"],"submitter_affiliation":["System Biology Lab. at Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency"],"submitter_country":["Russia"],"doi":["10.6019/PXD077041"],"additional_accession":[]},"is_claimable":false,"name":"Adaptation of immunoaffinity protocol for the isolation of the cell line immunopeptides - immunopeptidomics part","description":"BACKGROUND: The peptide repertoire presented by Human Leukocyte Antigens (HLA) provides a snapshot of intracellular proteins, which is monitored by the immune system. Although mass spectrometry is the gold standard for identification of these peptides, the upstream steps of the immunopeptidomics workflow, including immunoprecipitation and peptides purification, vary and critically impact the peptide yield.AIM: To optimize conditions for the isolation of a larger number of HLA I ligands.METHODS: Immunopeptidomes from cell lines were isolated using immunoaffinity followed by liquid chromatography-mass spectrometry analysis. Cell lines were lysed with various detergents (CHAPS, NP-40, SOD, Triton X-100) and eluted with TFA, urea, or thiocarbamate solutions.RESULTS: We optimized a protocol for immunoprecipitating peptide-HLA complexes and found that the number of identified peptides scales with the number of input cells, while being unaffected by the choice of lysis buffer.CONCLUSION: The optimized protocol allows the isolation of HLA I ligand peptides from suspension cell lines.","dates":{"publication":"2026-04-15","submission":"2026-04-11"},"accession":"PXD077041","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:625351","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","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:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","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:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","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:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","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:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1045775","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:1028307","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NC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