{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD023284/A0201_Uninfected_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD023284/A0201_Uninfected_1.raw"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD023284/A0201_Uninfected.mgf"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["nicola.ternette@ndm.ox.ac.uk"],"submitter":["Nicola Ternette"],"technology_type":["Mass Spectrometry","Top-down proteomics"],"software":["Not available"],"submitter_keywords":["Antigen presetation","Peptides","Lc-ms/ms","Hla"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD023284"],"tissue":["B Cell","Cell Culture"],"sample_protocol":["HLA-I-deficient CD4-expressing 721.221 cells were stably transfected with HLA-A*02:01. Transfectants were expanded by growth in RPMI 1640 medium (Thermo Fisher) containing 10% fetal bovine serum (FBS), 2 mM L-glutamine, 100 U/mL penicillin, and 100 μg/mL streptomycin (R10), and 2 x 108 cells harvested for HLA-I bound peptide profiling. Mass spectrometry-based immunopeptidome profiling of HLA-A*11:01-transfected CD4.221 cells was reported previously (Paes et al PNAS 2019);  the same methodology was employed here for immunopeptidome profiling. Briefly, cells were washed once in PBS, pelleted and 1 ml IGEPAL buffer [0.5% IGEPAL 630, 50 mM Tris pH8.0, 150 mM NaCl and 1 tablet Complete Protease Inhibitor Cocktail EDTA-free (Roche) per 10 ml buffer] was added per 0.5–1 × 108 cells, and cells were lysed by mixing for 45 min at 4°C. Cell lysates were cleared by two centrifugation steps, 2000 × g for 10 min followed by 20,000 × g for 30 min at 4°C. HLA-peptide complexes were immunoprecipitated from the cell lysates on W6/32-coated Protein A‐Sepharose beads overnight at 4°C. W6/32-bound HLA-peptide complexes were sequentially washed with 20 mL of wash buffer 1 (0.005% IGEPAL, 50 mM Tris pH 8.0, 150 mM NaCl, 5 mM EDTA), wash buffer 2 (50 mM Tris pH 8.0, 150 mM NaCl), wash buffer 3 (50 mM Tris pH 8.0, 400 mM NaCl) and finally wash buffer 4 (50 mM Tris pH 8.0). Peptide-HLA complexes were eluted from the beads in 5 mL of 10% acetic acid, and samples were dried down prior to resuspension in 120 μL loading buffer (0.1% TFA, 1% acetonitrile in ultragrade HPLC water). Samples were loaded onto a 4.6 × 50 mm ProSwift RP-1S column (Thermo Fisher Scientific) and eluted using a 500 μL/min flow rate over 10 min from 2 to 34% buffer B (0.1% TFA in acetonitrile) in buffer A (0.1% TFA in water) using an Ultimate 3000 HPLC system (Thermo Scientific). Alternate odd and even HPLC fractions were pooled and dried down prior to resuspension in 20 μL LC-MS/MS loading buffer (0.1% TFA in water)."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["For LC-MS/MS analysis, 9 ul of each sample was injected onto an analytical column on an Ultimate 3000 nUPLC system (Thermo Scientific). Peptides were introduced using an Easy-Spray source at 2000V at 40ºC to a Fusion Lumos mass spectrometer (Thermo Scientific). The ion transfer tube temperature was set to 305ºC. Full MS spectra were recorded from 300-1500 m/z in the Orbitrap at 120,000 resolution with an AGC target of 400,000. Precursor selection was performed using TopSpeed mode at a cycle time of 2 s. Peptide ions were isolated using an isolation width of 1.2 amu and trapped at a maximal injection time of 120 ms with an AGC target of 300,000. Higher-energy collisional dissociation (HCD) fragmentation was induced and fragments were analysed in the Orbitrap. LC-MS/MS data was analysed using PEAKS v8.0 (Bioinformatic Solutions) software."],"omics_type":["Proteomics"],"labhead":["Nicola Ternette"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["University of Oxford"],"species":["Homo Sapiens (human)"],"publication":["33619495 Karnaukhov V, Paes W, Woodhouse IB, Partridge T, Nicastri A, Brackenridge S, Scherbinin D, Chudakov DM, Zvyagin IV, Ternette N, Koohy H, Borrow P, Shugay M. HLA binding of self-peptides is biased towards proteins with specific molecular functions. bioRxiv. 2021:2021.02.16.431395 10.1101/2021.02.16.431395"],"submitter_mail":["nicola.ternette@ndm.ox.ac.uk"],"submitter_affiliation":["University of Oxford"],"submitter_country":["United Kingdom"],"pubmed_abstract":["Human leukocyte antigen (HLA) is highly polymorphic and plays a key role in guiding adaptive immune responses by presenting foreign and self peptides to T cells. Each HLA variant selects a minor fraction of peptides that match a certain motif required for optimal interaction with the peptide-binding groove. These restriction rules define the landscape of peptides presented to T cells. Given these limitations, one might suggest that the choice of peptides presented by HLA is non-random and there is preferential presentation of an array of peptides that is optimal for distinguishing self and foreign proteins. In this study we explore these preferences with a comparative analysis of self peptides enriched and depleted in HLA ligands. We show that HLAs exhibit preferences towards presenting peptides from certain proteins while disfavoring others with specific functions, and highlight differences between various HLA genes and alleles in those preferences. We link those differences to HLA anchor residue propensities and amino acid composition of preferentially presented proteins. The set of proteins that peptides presented by a given HLA are most likely to be derived from can be used to distinguish between class I and class II HLAs and HLA alleles. Our observations can be extrapolated to explain the protective effect of certain HLA alleles in infectious diseases, and we hypothesize that they can also explain susceptibility to certain autoimmune diseases and cancers. We demonstrate that these differences lead to differential presentation of HIV, influenza virus, SARS-CoV-1 and SARS-CoV-2 proteins by various HLA alleles. Finally, we show that the reported self peptidome preferences of distinct HLA variants can be compensated by combinations of HLA-A/HLA-B and HLA-A/HLA-C alleles in frequent haplotypes."],"pubmed_title":["HLA binding of self-peptides is biased towards proteins with specific molecular functions."],"pubmed_authors":["Karnaukhov Vadim V, Paes Wayne W, Woodhouse Isaac B IB, Partridge Thomas T, Nicastri Annalisa A, Brackenridge Simon S, Scherbinin Dmitrii D, Chudakov Dmitry M DM, Zvyagin Ivan V IV, Ternette Nicola N, Koohy Hashem H, Borrow Persephone P, Shugay Mikhail M"],"additional_accession":[]},"is_claimable":false,"name":"HLA binding of self-peptides is biased towards proteins with specific molecular functions","description":"Human leukocyte antigen (HLA) is highly polymorphic and plays a key role in guiding adaptive immune responses by presenting foreign and self peptides to T cells. Each HLA variant selects a minor fraction of peptides that match a certain motif required for optimal interaction with the peptide-binding groove. These restriction rules define the landscape of peptides presented to T cells. Given these limitations, one might suggest that the choice of peptides presented by HLA is non-random and there is preferential presentation of an array of peptides that is optimal for distinguishing self and foreign proteins. In this study we explore these preferences with a comparative analysis of self peptides enriched and depleted in HLA ligands. We show that HLAs exhibit preferences towards presenting peptides from certain proteins while disfavoring others with specific functions, and highlight differences between various HLA genes and alleles in those preferences. We link those differences to HLA anchor residue propensities and amino acid composition of preferentially presented proteins. The set of proteins that peptides presented by a given HLA are most likely to be derived from can be used to distinguish between class I and class II HLAs and HLA alleles.  Our observations can be extrapolated to explain the protective effect of certain HLA alleles in infectious diseases, and we hypothesize that they can also explain  susceptibility to certain autoimmune diseases and cancers. We demonstrate that these differences lead to differential presentation of HIV, influenza virus, SARS-CoV-1 and SARS-CoV-2 proteins by various HLA alleles. Finally, we show that the reported self peptidome preferences of distinct HLA variants can be compensated by combinations of HLA-A/HLA-B and HLA-A/HLA-C alleles in frequent haplotypes.","dates":{"publication":"2026-05-28","submission":"2020-12-23"},"accession":"PXD023284","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:1073882","NEWT:6819","NEWT:112509","NEWT:475174","NEWT:111205","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:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","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:55350","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","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:37919","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","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:2709072","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:294607","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: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: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:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095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