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Levi"],"software":[""],"tissue":["Blood Cell"],"sample_protocol":["Cells are incubated with 2 mM Sulfo-NHS-SS-biotin (21331; Pierce) plus 2 mM EZ link NHS-PEG4 biotin (21330 ; Pierce) or with vehicle (PBS) alone. For carboxyl labelling, cells were washed with PBS+ pH 5.7 and then preincubated with 2 mM EDC and 5 mM NHS-Sulfo in PBS pH 5.7 for 15 min at 4°C. After preincubation, cells were washed with PBS+ pH 8.0 and subsequently incubated with 2 mM carboxyl reactive biotin (EX-Link-Amine_PEG2 Biotin (21346;Thermo) in PBS pH 8.0 for 40 min at 4°C. Residual biotin was quenched with 100 mM glycine in PBS pH 8.0 and then washed twice with PBS pH 7.4. Cells were lysed in modified RIPA buffer (50 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, 10 mM iodoacetamide, 0.2% SDS (v/w), 0.5% sodium deoxycholate, 1% Triton X-100, pH 8.0) containing protease inhibitors. Cell lysates were centrifuged at 15,000 x g for 5 min at 4 °C, the nuclear pellet was discarded, and supernatants were incubated with preconditioned Streptavidin Magnetic Beads (8817; Pierce) for 3 hr to overnight at 4 °C. Unbound samples were collected, and beads were washed as follows; x 3 RIPA lysis buffer, x3 in Urea buffer (8 M urea in 0.1 M Tris/HCl pH 8.5), x 2 in 2M NaCl, x 3 with 50 mM Ammonium bicarbonate (AMBIC), x 1 with 25 mM AMBIC. Finally, the biotinylated proteins were digested on-beads at 37°C with 1 µg sequencing grade trypsin (Pierce) overnight in 25 mM ammonium bicarbonate. The digested peptides were eluted, the beads rinsed with 50 ul of 25 mM ammonium bicarbonate, and this second tryptic fraction was pooled with the first one.The samples were acidified to 1% TFA and peptide desalting was performed by reverse-phase liquid chromatography on an Agilent Bravo Automated Liquid Handling Platform, using the peptide clean-up v3.0 protocol. Briefly, reverse phase S cartridges 12 (Agilent, 5 μL bed volume) were primed with 250 μL 99.9% acetonitrile (ACN) with 0.1%TFA 13 and equilibrated with 250 μL of 0.1% TFA at a flow rate of 10 μL/min. The samples were loaded (770 μL) at 20 μL/min, followed by an internal cartridge wash with 250 μL of 0.1% 15 TFA at a flow rate of 10 μL/min. Peptides were then eluted with 105 μL of 1M glycolic acid with 50% ACN, 5% TFA. After desalting, 150μl of the elute is transferred to Lo-bind tubes and subjected to SpeedVac used to concentrate the samples overnight and then stored at -80°C. Peptides were re-suspended in 20 µL of reconstitution (97% H2O, 3% ACN, 0.1% TFA, 8 50fmol/µl-1 enolase peptide digest) and sonicated for 5 minutes at RT. Following a brief centrifugation, 4μl was loaded onto a LC-MS/MS system. The LC-MS/MS platform consisted of a Dionex UltiMate 3000 RSLC coupled to Q Exactive™ Plus Orbitrap Mass Spectrometer (Thermo Fisher Scientific) through an EASY-Spray source."],"repository":["Pride"],"labhead":["Pedro R.Cutillas"],"instrument_platform":[""],"labhead_affiliation":["Instituto de Parasitología y Biomedicina López-Neyra Consejo Superior de Investigaciones Científicas, CSIC Avda. del Conocimiento, 17 18016 Granada. SPAIN"],"submission_type":["COMPLETE"],"publication":["10.1016/J.MCPRO.2026.101572"],"submitter_affiliation":["Barts Cancer Institute, Queen Mary University of London"],"labhead_mail":["prcutillas@ipb.csic.es"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Acute Leukemia"],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD068779"],"quantification_method":[""],"modification":[""],"data_protocol":["For protein identification the MS data were searched using Mascot Server via Mascot Daemon (v2.8.0.1, in-house server) which matched the MS/MS data to the Swissprot Database for Homo sapiens 2021¬_02.fasta (17080 sequences, 181677051 residues). The FDR was set to ~1 % (peptide matches above homology or identity threshold). Searches had the following parameters: 2 trypsin missed cleavages, mass tolerance of ±10 ppm for the MS scans and ±25 mmu for the MS/MS scans, carbamidomethyl Cys as a fixed modification and oxidation of Met, PyroGlu on N-terminal Gln and deamidated (NQ) as variable modifications.  Pescal (Peak Statistic Calculator) was used to calculate m/z and retention time (tR) values for each identified peptide ion to generate extracted ion chromatograms (XICs). The software constructed XICs for all the peptides identified in at least one of the LC-MS/MS runs across all samples. XIC mass and retention time windows were ±7 ppm and ± 1.5 min, respectively. Algorithms in Pescal then calculate area under the peak of the XICs in the generated arrays and return these values to Excel file for further analysis. The relative quantity of a peptide was calculated relative to the mean of peptide normalized ion intensities of this peptide across the samples to be compared. For the reported differentially expressed proteins at least one unique peptide assigned to them was also required. We accepted the returned protein identifications when Mascot scores were above the statistically significant threshold (expectancy < 0.05 for individual peptides) and at least two peptides matched the identified protein.  A bioinformatics pipeline that incorporates R algorithms for pathway analysis and interactive visualisations (https://github.com/CutillasLab/protools2/) was used for the quantitative processing and GO enrichment analysis of the proteomic data against the location subset of ontologies or the in silico surfaceome obtained from Bausch-Fluck et al. Peak area normalisations were performed and then log2 scaled and cantered. Statistical differences between comparisons were calculated using the LIMMA function, and then adjusted for FDR using the Benjamini-Hochberg method. Proteins were considered significant if present in labelled samples with Log2fold difference > 0.5 and p-value < 0.05 compared to the mock labelled control."],"omics_type":["Proteomics"],"species":["Homo Sapiens (human)"],"submitter_mail":["a.levi@qmul.ac.uk"],"submitter_country":["United Kingdom"],"doi":["10.6019/PXD068779"],"additional_accession":[]},"is_claimable":false,"name":"Surfaceome Capture by Multiplex biotinylation (SUCAM) allows enhanced identification of cell surface proteins by mass spectrometry","description":"Comprehensive interrogation of the cell surface proteome is critical for identifying targets for immunotherapy. Although surfaceomic technologies have advanced, current approaches remain limited by sensitivity and functional group specificity, restricting analyses to samples with large cell numbers and potentially overlooking subsets of surface proteins. To overcome these limitations, we developed Surfaceome Capture by Multiplex (SUCAM) biotinylation, a combinatorial strategy that employs multiplexed biotin reagents to derivatize multiple functional groups on cell surface proteins. Following enrichment with streptavidin magnetic beads, proteins were identified and quantified by LC–MS/MS. SUCAM enabled enhanced detection of plasma membrane and cell surface proteins compared with single-reagent methods, achieving robust identification from as few as 1.2 million cells. Replicate analyses demonstrated high reproducibility (mean coefficient of variation, 17%). Application of SUCAM to a panel of leukaemia cell lines recovered canonical leukaemic surface antigens as well as proteins with previously uncharacterised roles in this malignancy. These findings establish SUCAM as a complementary surfaceomic strategy that broadens proteome coverage and facilitates the discovery of therapeutic targets in both haematological and solid tumours.","dates":{"publication":"2026-05-01","submission":"2025-09-24"},"accession":"PXD068779","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:2902907","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:123606","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:518","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","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