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Briefly, cell pellets consisting of 200*106 cells and secreted melanosomes collected from the media 400*106 cell (50 flasks of 25ml, seeded with 3.5*106 each and collected 4 days post seeding) were homogenized and lysed with lysis buffer (containing 0.25% sodium deoxycholate, 0.2mM iodoacetamide, 1mM EDTA, protease inhibitor cocktail (Sigma-Aldrich), 1mM PMSF and 1% octyl-β-D-glucopyranoside in PBS) and incubated at 4°C for 1 hour. Lysates were cleared by centrifugation at 4°C, 48,000 x g for 45 minutes and passed through a pre-clearing column containing Protein A/ G resin beads (GenScript); Human-derived HLA-peptide complexes were then immunoaffinity purified from the cleared lysate using pan-HLA antibody (W6/32 antibody purified from HB95 hybridoma cells), covalently bound to Protein A Resin (Genescript). For the mouse-derived MHC complexes, two anti-MHC-I antibodies - M28 (HB27) 28-14-8S and M20 (HB11) 20-8-4S (ATCC, HB-27 ™)- were covalently bound to Protein-G sepharose beads (Genscript; the same beads were used for the pre-clear step) at a 1:1 ratio. MHC-peptide complexes were eluted with 1% trifluoracetic acid (TFA), followed by purification of the peptides by Sep-Pak tC18 100mg Sorbent 96-well plate (Waters). Elution of the peptides was done with 28% acetonitrile (ACN) in 0.1% trifluoracetic acid TFA.  In preparation for LC-MS/MS analysis, MHC peptides were dried by vacuum centrifugation and resolubilized with 0.1% formic acid. For Orbitrap MS/MS experiments, peptides were separated using reversed-phase chromatography using the nanoAquity system (Waters), with a Symmetry trap column (180 × 20 mm) and HSS T3 analytical column, 0.75 × 250 mm (Waters), mobile phase A: H2O+0.1% formic acid, B: acetonitrile+0.1% formic acid. The peptides were separated with a linear gradient over 2h from 5 to 28% B, 28 to 35% in 15min, 35% to 95% in 15min, maintained at 95% for 10min and back to initial conditions, at a flow rate of 0.35μl min−1. The LC was connected online via a nano-electrospray ionization source (FlexIon, Thermo Scientific) using an emitter (Fossil) to a Quadrupole Orbitrap MS (Q-Exactive-Plus, Thermo Scientific). Data were acquired using a data-dependent method, fragmenting the peptides by higher-energy collisional dissociation (HCD). On the Q-Exactive-Plus, full-scan MS spectra were acquired at a resolution of 70,000 at 200 m/z with automated gain control (AGC) value of 3 × 106 ions, mass range of 300 to 1800 Th and maximum injection time of 100msec. MS/MS scans were acquired with an AGC target value of 105 with a maximum injection time of 150 msec, isolation of 1.7 Th, normalized collision energy was set to 25%, and MS/MS resolution was 17,500 at 200 m/z. Fragmented m/z values were dynamically excluded from further selection for 20s. For timsTOF (TTU) experiments, the peptides were resolubilized with 0.1% trifluoroacetic acid and 5mM TCEP before LC-MS/MS analysis. 5L of each sample was loaded using the nanoElute2 (Bruker, Germany) liquid chromatography. Mobile phase A was 0.1% formic acid in water. B was 0.1% formic acid in acetonitrile. Peptides were separated using the Aurora Ultimate C18 nano column, 0.075x250mm (IonOptiks, Australia), using a gradient of 2% B to 29% B in 80min, then 0.5min to 95% B, maintained 95%B for 2.9min at flow of 300nL/min. The column was placed in the column toaster and connected to a CaptiveSpray Electrospray ionization source. The column was maintained at 50C. Data was acquired with a timsTOF Ultra (Bruker) in data-dependent-acquisition-parallel-accumulation-serial-fragmentation (DDA-PASEF) mode with the following parameters: capillary voltage of 1600v, temperature of 180C, mass range of 100-1,700 Th, ion mobility 0.6-1.57 1/K0, tims ramp time of 300msec, number of PASEF MS/MS scans 10, target intensity of 20,000 with threshold of 2,500, charge range 0 to 5, collision energy of 20 at 0.6 1/K0 and 59 at 1.6 1/K0."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["RAW files were analyzed using FragPipe v.22 with default parameters for HLA peptides discovery (searched with the human Ensemble v.109) as previously described. NetMHCpan v.4.1 was utilized to predict peptide binding affinity (binder <2% rank). Retention time and Hydrophobicity index Hydrophobicity values for total PSM peptides were predicted with R package protViz version 0.7.7 69 (https://CRAN.R-project.org/package=protViz) were plotted against the experimental retention time.  Tumor-associated antigens identification        A Tumor Associated Antigen (TAA) reference database (TAAs-refDB) was compiled based on melanoma-associated antigens described by Pitcovski et al.  Gene and protein annotations were retrieved using the org.Hs.eg.db and biomaRt packages 1 to map aliases, gene symbols, and descriptions. A custom pipeline was used to merge peptide-related information from human alias databases and FASTA headers extracted from the Ensembl protein database. The presence of peptides in experimental conditions (cells or melanosomes, with and without IFNγ stimulation) was determined by filtering for MS/MS-detected sequences and cross-referencing Protein IDs. Known TAAs were identified by matching against two reference datasets: the Benign HLA Ligand Atlas 113 and the Immune Epitope Database (IEDB). Peptides found in either database were labeled. TAA-to-canonical peptide ratios were calculated per replicate and condition. Whole-exome sequencing and neoantigen identification       Whole Exome Sequencing (WES) was performed on the WM3526 cutaneous melanoma cell line by IDT-V2 enrichment kit at Hadassah Medical Center. Raw sequencing reads in FASTQ format were mapped to the human reference genome (GRCh38) using the BWA aligner. Duplicate reads were removed using Picard tools (https://github.com/broadinstitute/picard). Aligned BAM files were then processed, and variants were called using GATK Mutect2 115, producing a VCF file that was filtered by quality scores. After variant calling, the variants were translated into protein sequences using Annovar 116. For each mutation, 13 amino acids upstream and downstream of the mutation were extracted and stored in a FASTA file for further analysis. Variants were then marked using allele frequencies from the gnomAD database and/or dbSNP (link: https://www.ncbi.nlm.nih.gov/snp/), and variant allele frequency (VAF) was calculated for each variant in the sample data.       Non-synonymous mutations were further analyzed for neoantigen identification by searching the immunopeptidomic data using a proteogenomic approach. We utilized the group-specific false discovery rate (FDR) search feature in FragPipe 108,118 with 1% FDR for both the canonical database (PE=1) and the non-synonymous mutation database (PE=2), followed by a stringent data processing pipeline as previously described108. Identified peptides were further filtered to remove variants with allele frequency > 1% in gnomAD as previously described 119 and to have VAF > 0.1 in the sample data. Neopeptides that passed the variant confidence filtration process were further examined for peptide-spectrum match (PSM) confidence by visualizing mirror plots of the identified spectrum versus the predicted one using the PDV tool and Unweighted Spectral Entropy (USE) scoring."],"omics_type":["Proteomics"],"labhead":["Yardena Samuels"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Molecular Cell Biolody, Weizmann Institute of Science."],"species":["Homo Sapiens (human)","Mus Musculus (mouse)"],"publication":["41401806 Chemla Y, Itzhaki O, Melamed S, Weller C, Sade Y, Manich P, Reshef K, Xenidis N, Maliah A, Levy G, Parikh R, Bartok O, Levy O, Tal I, Aziel G, Nissani A, Yunger S, Likonen D, Kliminsky V, Golan T, Capron C, Ace V, Levy R, Rasoulouniriana D, Eyal Z, Barzilay Y, Balaban R, Khateeb A, Khosravi R, Grau A, Ziv T, Greenberg P, Netanely D, Vaknin H, Wu X, Amitay Y, Brenner R, Martínez Gómez JM, Hershkovitz D, Yardeni T, Zemser-Werner V, Kobiler O, Friedmann Y, Bassan D, Shamir R, Eisenbach L, Santana-Magal N, Milyavsky M, Eisenberg G, Keren L, Cohen M, Gur D, Barak B, Lotem M, Sprinzak D, Greenberger S, Fisher D, Besser MJ, Khaled M, Close P, Shapira R, Apcher S, Madi A, Levesque MP, Rapino F, Carmi Y, Parikh S, Samuels Y, Levy C. HLA export by melanoma cells decoys cytotoxic T cells to promote immune evasion. Cell. 2026 189(1):233-251.e29 10.1016/j.cell.2025.11.020"],"submitter_mail":["chen.weller@weizmann.ac.il"],"submitter_affiliation":["Yardena Samuels lab, Weizmann Institute of Science"],"submitter_country":["Israel"],"pubmed_abstract":["While melanoma cells often express a high burden of mutated proteins, the infiltration of reactive T cells rarely results in tumor-eradicating immunity. We discovered that large extracellular vesicles, known as melanosomes, secreted by melanoma cells are decorated with major histocompatibility complex (MHC) molecules that stimulate CD8<sup>+</sup> T cells through their T cell receptor (TCR), causing T cell dysfunction and apoptosis. Immunopeptidomic and T cell receptor sequencing (TCR-seq) analyses revealed that these melanosomes carry MHC-bound tumor-associated antigens with higher affinity and immunogenicity, which compete with their tumor cell of origin for direct TCR-MHC interactions. Analysis of biopsies from melanoma patients confirmed that melanosomes trap infiltrating lymphocytes, induce partial activation, and decrease CD8<sup>+</sup> T cell cytotoxicity. Inhibition of melanosome secretion in vivo significantly reduced tumor immune evasion. These findings suggest that MHC export protects melanoma from the cytotoxic effects of T cells. Our study highlights a novel immune evasion mechanism and proposes a therapeutic avenue to enhance tumor immunity."],"pubmed_title":["HLA export by melanoma cells decoys cytotoxic T cells to promote immune evasion."],"pubmed_authors":["Chemla Yoav Y, Itzhaki Orit O, Melamed Stav S, Weller Chen C, Sade Yuval Y, Manich Paulee P, Reshef Keren K, Xenidis Nicolas N, Maliah Avishai A, Levy Gilad G, Parikh Roma R, Bartok Osnat O, Levy Opal O, Tal Itay I, Aziel Gal G, Nissani Abraham A, Yunger Sharon S, Likonen Daniela D, Kliminsky Vitaly V, Golan Tamar T, Capron Coralie C, Ace Valentina V, Levy Ronen R, Rasoulouniriana Diana D, Eyal Zohar Z, Barzilay Yuval Y, Balaban Roi R, Khateeb Aseel A, Khosravi Rami R, Grau Amir A, Ziv Tamar T, Greenberg Polina P, Netanely Dvir D, Vaknin Hananya H, Wu Xunwei X, Amitay Yael Y, Brenner Ronen R, Martínez Gómez Julia María JM, Hershkovitz Dov D, Yardeni Tal T, Zemser-Werner Valentina V, Kobiler Oren O, Friedmann Yael Y, Bassan David D, Shamir Ron R, Eisenbach Lea L, Santana-Magal Nadine N, Milyavsky Michael M, Eisenberg Galit G, Keren Leeat L, Cohen Merav M, Gur Dvir D, Barak Boaz B, Lotem Michal M, Sprinzak David D, Greenberger Shoshana S, Fisher David D, Besser Michal J MJ, Khaled Mehdi M, Close Pierre P, Shapira Ronnie R, Apcher Sebastien S, Madi Asaf A, Levesque Mitchell P MP, Rapino Francesca F, Carmi Yaron Y, Parikh Shivang S, Samuels Yardena Y, Levy Carmit C"],"additional_accession":[]},"is_claimable":false,"name":"Immunopeptidomic analyses - HLA Export by Melanoma Cells Decoys Cytotoxic T Cells to Promote Immune Evasion","description":"While melanoma cells often express a high burden of mutated proteins, the infiltration of reactive T cells rarely results in tumor-eradicating immunity. We discovered that large extracellular vesicles, known as melanosomes, secreted by melanoma cells are decorated with MHC molecules that stimulate CD8+ T cells through their T-cell receptor (TCR), causing T cell dysfunction and apoptosis. Immunopeptidomic and TCR-seq analyses revealed that these melanosomes carry MHC-bound-Tumor-Associate- Antigens with higher affinity and immunogenicity, which compete with their tumor cell of origin for direct TCR–MHC interactions. Analysis of biopsies from melanoma patients confirmed that melanosomes trap infiltrating lymphocytes, induce partial activation, and decrease CD8+ T cell cytotoxicity. Inhibition of melanosome secretion in vivo significantly reduced tumor immune evasion. These findings suggest that MHC export protects melanoma from the cytotoxic effects of T cells. Our study highlights a novel immune evasion mechanism and proposes a therapeutic avenue to enhance tumor immunity.","dates":{"publication":"2026-04-19","submission":"2025-10-02"},"accession":"PXD069094","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","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:294671","NEWT:376619","NEWT:1748418","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:2086595","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:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","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:342808","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","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:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","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:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","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:31345","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:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","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:299467","NEWT:9541","NEWT:51350","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:253237","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","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