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Imre"],"technology_type":["Data-dependent acquisition","Glycoproteomics","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Human","Lc-ms","Glycoproteomics","Mouse","Breast cancer"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067987"],"tissue":["Breast Cancer Cell"],"sample_protocol":["Cells were lysed using 8M urea buffer, sonicated and centrifuged to clear the cell lysates. Lysates were quantified using Pierce™ BCA Protein Assay Kit (Thermo Fischer). For each sample, 400 μg of protein were reduced using DTT and subsequently alkylated using IAA. Proteins were digested using Lys C and Trypsin (1 μg enzyme: 50 μg sample) overnight at 32°C. At this point, samples were acidified using TFA to a final concentration of 0.3% before being cleaned using 200 mg (3cc) Sep-Pak cartridges (Waters). The resulting cleaned peptides was dried under vacuum and stored at 20°C before proceeding with the TMT labelling protocol. For the TMT labeling, 120 μg of peptides of each sample were prepared in a final volume of 100 μL of 100 mM HEPES buffer pH 7.6. Samples were labeled using TMTpro 18 plex (Thermo Scientific) reagents, according to manufacturer’s instructions. The labelling efficiency was determined by LC-MS/MS on a small aliquot of each sample. After quenching the labeling reaction, samples were mixed in equimolar amounts, evaluated by LC-MS/MS. The mixed sample was acidified to a pH below 2 with 10% TFA and desalted using C18 cartridges (Sep-Pak Vac 1cc (200mg), Waters). Peptides were eluted with 2 x 600 μl 80% Acetonitrile (ACN) and 0.1% Formic Acid (FA), followed by freeze-drying. Glycopeptides were enriched from the resulting TMTpro mixes by performing off-line ion pairing (IP) HILIC chromatography. Briefly, the dried samples were taken up in 100 μL 75% acetonitrile containing 0.1 % TFA, and subjected to chromatographic separation on a TSKgel Amide-80 column (4.6 x 250 mm, particle size 5μ) using a linear gradient from 0.1% TFA in 80% acetonitrile to 0.1% TFA in 40% acetonitrile over 35 min (Dionex Ultimate 3000, Thermo). The 25 collected fractions were vacuum dried. Samples were resuspended using 0.1% trifluoroacetic acid (TFA, Thermo Scientific, Cat#28903). The IP-HILIC fractions were individually analysed by LC–MS/MS. The nano HPLC system used was an UltiMate 3000 HPLC RSLC nano system (Thermo Scientific) coupled to a Exploris 480 mass spectrometer (Thermo Scientific), equipped with a Proxeon nanospray source (Thermo Scientific). Peptides were loaded onto a trap column (Thermo Scientific, PepMap C18, 5 mm × 300 μm ID, 5 μm particles, 100 Å pore size) at a flow rate of 25 μL/min using 0.1% TFA as mobile phase. After 10 min, the trap column was switched in line with an analytical column (Thermo Scientific, PepMap C18, 500 mm × 75 μm ID, 2 μm, 100 Å). Peptides were eluted using a flow rate of 230 nl/min and a binary 180 min gradient. The two steps gradient started with the mobile phases: 98% A solution (water/formic acid, 99.9/0.1, v/v) and 2% B solution (water/acetonitrile/formic acid, 19.92/80/0.08, v/v/v), which was then increased to 35% B over the next 180 min, followed by a gradient of 90% B for 5 min, which was finally, in a 2 min period, decreased to the gradient 95% A and 2% B for equilibration at 30°C. The following parameters were used for MS acquisition using an Exploris 480 instrument, operated in data-dependent mode: the instrument was operated in a positive mode; compensation voltages (CVs) used = CV-40, CV-50, CV-60; cycle time (per CV) = 1 sec. The monoisotopic precursor selection (MIPS) mode was set to Peptide. Precursor isotopes and single charge state precursors were excluded. MS1 resolution=60,000; MS1 Normalised AGC target=300%; MS1 maximum inject time=50msec. MS1 restrictions were relaxed when few precursors were present. MS1 scan range= 400–1,600m/z; MS2 resolution=45,000; MS2 Normalised AGC target=200%. Maximum inject time=250msec. Precursor ions charge states allowed = 2-7; isolation window=1.4m/z; fixed first mass=110m/z; HCD collision energies=30,33,36; exclude isotopes=True; dynamic exclusion=45s."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["All MS/MS data were processed and analysed using Xcalibur v3.1 (Thermo), and Byonic (Protein Metrics) included in Proteome Discoverer v3.0. Two default glycan databases (Mammalian O-glycans and Human N- glycans) were used together with the latest human or mouse UniProt database, to generate the glycopeptide search space. Carbamidomethylation (C) and TMTpro (pept N-term and K) were defined as static modifications. Oxidation (M), phosphorylation (S,T,Y), deamidation (N), and pyroGlu (pept-N-term Q) were considered as dynamic modifications. We used an in-house developed R script to concatenate the glyco-PSMs into glycopeptide groups, after filtering out poorly matching spectra (considering isolation interference lower than 50% and a Byonic score higher than 200) and summing the glyco-PSMs TMT intensities."],"omics_type":["Proteomics"],"labhead":["Tiago Oliveira"],"instrument_platform":[""],"labhead_affiliation":["IMBA and Medical University of Vienna"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["richard.imre@imba.oeaw.ac.at"],"submitter_affiliation":["IMBA Vienna"],"submitter_country":["Austria"],"additional_accession":[]},"is_claimable":false,"name":"Glycoproteomics of breast cancer cell lines","description":"Breast cancer is the most common cancer among women. However, the use of immune checkpoint inhibitors, that have revolutionized treatment of multiple cancers, unfortunately remain largely ineffective in most breast cancer patients. Here, we report the most comprehensive glycoproteome map in breast tumor cells, pointing to a key role of sialic acid modifications in mammary cancer. Genetic and pharmacologic inhibition of sialylation repolarizes the tumor microenvironment, leading to a reduction in myeloid-derived suppressor cells and a significant increase in Tcf7+ memory and CD8+  effector T cells. Mechanistically, sialylation controls cell surface expression of MHC class I and PD-1-ligand on the tumor cells. Functionally, in vivo interference with sialylation on breast cancer cells licenses CD8+ T cells to effectively kill the tumors. In multiple immunotherapy-resistant breast tumor models, we also show that the abrogation of sialylation sensitizes to anti-PD-1 immune checkpoint therapy. We further demonstrate that hyper-sialylation occurs in over half of human breast cancers tested and correlates with poor T cell infiltration. Our results establish sialylation as a central immunoregulator in breast cancer, orchestrating multiple pathways of immune evasion. Targeting tumor sialylation licenses immunologically inert mammary tumors to be efficiently eliminated by anti-cancer immunity and sensitizes to immune checkpoint therapy.","dates":{"publication":"2026-05-05","submission":"2025-09-02"},"accession":"PXD067987","cross_references":{"TAXONOMY":["NEWT:3555","NEWT:71647","NEWT:330879","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:43186","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:641809","NEWT:27933","NEWT:556484","NEWT:317447","NEWT:4688","NEWT:7955","NEWT:7959","NEWT:2261","NEWT:31156","NEWT:3112","NEWT:79329","NEWT:4442","NEWT:192875","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:108061","NEWT:60711","NEWT:1316931","NEWT:224308","NEWT:3347","NEWT:511145","NEWT:160621","NEWT:212790","NEWT:931281","NEWT:4432","NEWT:5762","NEWT:658457","NEWT:1310161","NEWT:77133","NEWT:295358","NEWT:145481","NCBITaxon:79824","NEWT:2246","NEWT:2652724","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:4897","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:5507","NEWT:410661","NEWT:55571","NEWT:35500","NEWT:1235816","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:4896","NEWT:1287689","NEWT:1390","NEWT:11557","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:294","NEWT:1773","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:3711","NEWT:935293","NEWT:375146","NEWT:2065263","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:1246791","NEWT:7067","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:33548","NEWT:274","NEWT:7070","NEWT:408172","NEWT:408170","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","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:2853422","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:109760","NEWT:943274","NEWT:644223","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:272623","NEWT:272624","NEWT:320637","NEWT:983964","NEWT:118499","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:55529","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:3988","NEWT:1116234","NEWT:1255228","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:3983","NEWT:352472","NEWT:1071661","NEWT:1202532","NEWT:360094","NEWT:470","NEWT:41364","NEWT:1313","NEWT:39491","NCBITaxon:5811","NEWT:29491","NEWT:2014887","NEWT:33952","NEWT:153009","NEWT:261756","NEWT:571256","NEWT:40483","NEWT:63366","NEWT:63367","NEWT:215402","NCBITaxon:548681","NEWT:272634","NEWT:9031","NEWT:1872122","NEWT:7091","NEWT:1034015","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:2903","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:98351","NEWT:1263854","NEWT:118503","NEWT:2059687","NEWT:160488","NEWT:28104","NEWT:207559","NEWT:407821","NCBITaxon:2","NEWT:85057","NEWT:985076","NEWT:568708","NEWT:1215323","NEWT:986","NEWT:52641","NEWT:7159","NEWT:267671","NEWT:28532","NEWT:353152","NEWT:8496","NEWT:7165","NEWT:27448","NEWT:40674","NEWT:1194669","NEWT:243230","NEWT:1080772","NEWT:519","NEWT:8479","NEWT:8485","NEWT:6063","NEWT:49240","NEWT:1328388","NEWT:104395","NEWT:9557","NEWT:62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