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Finn"],"technology_type":["Data-dependent acquisition","Glycoproteomics","Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Human","Lc-ms","Glycoproteomics","Seminal fluid","O-glycoproteomics","Serum","Method"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD061804"],"tissue":["Cell Suspension Culture","Semen","Blood Serum"],"sample_protocol":["Sample Loading. Ultracentrifugal molecular weight cut-off (MWCO) filters were first rinsed 3x with 500 µL of 20 mmol L-1 tris pH 7.4 by centrifuging the filters at 6,000 rcf for 5 min. Approximately 1 mg of biological samples, as determined by nanodrop, was loaded onto the filter. In cases where the sample was less than 400 µL in volume, the sample was brought up to 500 µL on the filter using 20 mmol L-1 Tris prior to centrifugation. Following sample loading, it was centrifuged until approximately 100 µL or less remained atop the filter. Each sample was concentrated to 100 µL 3x to ensure adequate depletion of contaminants. All additions of buffer or sample were mixed on the filter by pipetting up and down 3x. Glycoprotease Digestion. Once the sample was rinsed at least three times, the volume was brought to approximately 250 µL with 20 mmol L-1Tris.  A single unit of OgpA or 0.2 µg of BT4244 was added onto the filter to rinsed HEK293-6e ΔC1GALT1 cell growth media. For all other samples, 1 unit of IMPa was added. The filter was then closed, secured with parafilm, and incubated at 37 °C for 3 hrs to overnight. After incubation, the parafilm was removed, and the sample was centrifuged into a new collection tube. After centrifugation, the flow through was collected and another 150 µL of Tris was added to the sample. This was repeated 2-3 times until 450-600 µL of filtrate had been collected. This filtrate contained the glycopeptides that were analyzed. If using a 30 kDa or higher MWCO filter, the filtrate was then reduced with 25 mmol L-1 DTT at 65 °C for 1 hr, followed by alkylation with 35 mmol L-1 IAA in the dark at room temperature for 15 min. Then 0.2 µg of trypsin was added to the sample, and it was incubated at 37 °C for 3 hrs to overnight. After incubation, the sample was desalted. If a 10 kDa filter was used, reduction, alkylation, and tryptic digestion were omitted, and the sample was desalted after collecting glycopeptides. Sample desalting. Samples were acidified with formic acid to a final concentration of 0.5% (v/v) prior to desalting. Desalting was performed using 10 mg Strata-X 33 µm polymeric reversed phase SPE columns. Each column was activated using 1 mL of ACN, followed by 1 mL of 0.1% formic acid in LC-MS grade water (buffer A), 1 mL of 0.1% formic acid in 40% ACN (buffer B), and equilibrated with an additional 1 mL of buffer A. Samples were then loaded onto to the column and rinsed twice with 200 µL of buffer A. The columns were transferred to a 1.5 mL Eppendorf tube for elution using 150 µL 0.1% formic acid in 40% ACN twice. Finally, the eluents were dried using a vacuum concentrator and resuspended in 0.1% formic acid prior to MS analysis  Mass spectrometry data acquisition. Samples were analyzed by online nanoflow liquid chromatography-tandem mass spectrometry using an Orbitrap Eclipse Tribrid mass spectrometer coupled to a Dionex UltiMate 3000 HPLC instrument. Samples were resuspended in 10 µL of buffer A, and 6 µL were injected onto an Acclaim PepMap 100 column packed with 2 cm of 5 μm C18 material. Peptides were then separated on a 15 cm PepMap RSLC EASY-Spray C18 column packed with 2 μm C18 material using a gradient from 0 to 35% solvent B (0.1% formic acid with 80% ACN) in 60 min with a constant flow rate of 300 nL min-1. Full scan MS1 spectra were acquired at a resolution of 60,000 full width at half maximum (FWHM) at 400 m/z, an automatic gain control (AGC) target of 3e5, and a mass range from 300 to 1,500 m/z. Dynamic exclusion settings allowed 2 repeats in 7 s before exclusion for 7 s. Only charge states 2 to 6 were selected for fragmentation. MS2s were generated at top speed for 3 s.  Fragmentation scans were collected in the Orbitrap at 15,000 resolution. Higher-energy collisional dissociation (HCD) was performed on all selected precursor masses with the following parameters: isolation window of 2 m/z, stepped collision energy 25–30–40% normalized collision energy (nCE), Orbitrap detection (resolution of 7,500), maximum inject time of 50 ms, and a standard AGC target. An additional electron transfer dissociation (ETD) fragmentation of the same precursor was triggered if 1) 3 of 8 HexNAc or NeuAc fingerprint ions (126.055, 138.055, 144.07, 168.065, 186.076, 204.086, 274.092, and 292.103) were present at ± 0.1 m/z and greater than 5% relative intensity, 2) the precursors were present at a sufficient abundance for localization using ETD. If the precursor was between 300–850 m/z and over 3e4 intensity, an ETD scan was triggered and read out using the ion trap at a normal scan rate. For precursors between 850–1500 m/z with an intensity greater than 1e5, supplemental activation was used (EThcD) was also applied at 15% nCE and read out in the Orbitrap at 7500 resolution. Both used charge-calibrated ETD reaction times, 150 ms maximum injection time, and 200% standard injection targets."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["RAW files were searched using Byonic v4.0.12.66 (ProteinMetrics), against the human proteome. Using this search, databases were created for each RAW file that contained all proteins that were found to have at least one peptide with a score >150 and logP >1.5. RAW files were subsequently searched against their focused databases. Data from previously published reports were used to benchmark GlycoFASP against WGA, Jacalin, and StcEE447D enrichment8, 18. RAW data from publications was downloaded from the PRIDE repository with the data set identifier PXD053713 for WGA and Jacalin enrichments and data set identifier PXD046534 for StcEE447D enrichment. Mass tolerance was set at 10 ppm for MS1s and 20 ppm for MS2s. Files were searched with various cleavage specificities. In tryptic digests, C-terminal Arg/Lys; in IMPa, SmE, BT4244, and OgpA digests, N-terminal Ser/Thr was selected. Carbamidomethyl Cys was set as a fixed modification. For samples treated with PNGaseF, Asn deamidation was added as a variable modification. For samples that underwent guanidation, Lys and N-term guanidyl was added as a variable modification. The fragmentation type was set to read directly from the scan headers. N- and O-glycopeptide searches were performed simultaneously, with the 9 most common O-glycans designated as common modifications with a maximum of two per peptide and 132 N-glycans designated as rare modifications with a maximum of one per peptide. Other variable modifications were set as common for these searches, with a maximum of two common and one rare modification per peptide. Peptide hits were filtered using a 1% false discovery rate (FDR) for each program. Missed cleavages were set to 7 for all digests. For glycoproteomic analysis, glycopeptides were filtered for score >150 and logP >1.5 to ensure accurate peptide sequence. Peptides not flagged as containing a glycan were grouped as unmodified peptides. Peptides that contained any glycan on an Asn residue were grouped as N-glycopeptides, and all other glycopeptides were grouped as O-glycopeptides. Unique peptide identifications were found by removing duplicate glycopeptides, defined as peptides with the same calculated (M+H)+ mass, protein of origin, and sequence position. O-glycoproteins were defined as any protein with an O-glycopeptide with score >150 and logP >1.5. Unmodified proteins were defined as any protein with at least one peptide with score >150 and logP >1.5 and no N- or O-glycopeptides above the same score cutoff. Glycoprotein intensity percentages were calculated by summating the total intensity of glycoproteins as reported by Byonic and dividing by the total intensity of all modified and unmodified proteins."],"omics_type":["Proteomics"],"labhead":["Stacy Malaker"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Yale University"],"species":["Homo Sapiens (human)"],"publication":["41124113 Finn SM, Mahoney KE, Lucas TM, Rangel-Angarita V, Chen RJ, Malaker SA. GlycoFASP: A Universal Method to Prepare Complex Mixtures for O-Glycoproteomic Analysis. Anal Chem. 2025 97(43):23751-23756 10.1021/acs.analchem.5c02666"],"submitter_mail":["shane.finn@yale.edu"],"submitter_affiliation":["Yale University"],"submitter_country":["United States"],"pubmed_abstract":["Glycoproteomic analyses remain a significant challenge due to the considerable heterogeneity in the composition, linkage, and localization of glycosylation. These issues are further complicated in the study of <i>O</i>-glycosylation, which primarily occurs on serine or threonine residues, given the lack of a consensus peptide motif and the proximity of <i>O</i>-glycosites. Mass spectrometry (MS)-based analysis is the premier technique for analyzing <i>O</i>-glycoproteins,but often equires prior separation or enrichment. Variability in the properties of O-glycosylation has thus far prevented the development of universal glycoconjugate enrichments. In response to this problem, we developed GlycoFASP, a one-pot preparation method for <i>O</i>-glycoproteins requiring only 1 mg of sample and limited protein purification. Our method isolates <i>O</i>-glycopeptides through selective proteolysis of glycoproteins using proteases with dual peptide-glycan cleavage motifs, called <i>O</i>-glycoproteases, on a molecular-weight cutoff (MWCO) filter. It can be processed in a single day and provides enrichment as broad as all <i>O</i>-glycoproteins in a sample or as narrow as peptides bearing specific <i>O</i>-glycan structures. GlycoFASP regularly achieves depletion of nearly all non-<i>O</i>-glycosylated proteins, with ≥70% of the protein signal originating from <i>O</i>-glycoproteins in analyses of human serum, seminal fluid, and cell growth media. Our method was compared to other common enrichments, such as glycan-binding proteins (GBP), strong anion exchange (SAX-ERLIC), and another digestion-based strategy in analyses of human serum. GlycoFASP identified over twice as many <i>O</i>-glycopeptides as all other methods. Given its ease of use, reagent accessibility, and low cost, we expect this method to greatly accelerate glycoscience research by enabling nonglycoproteomic experts to perform these analyses."],"pubmed_title":["GlycoFASP: A Universal Method to Prepare Complex Mixtures for O-Glycoproteomic Analysis."],"pubmed_authors":["Finn Shane M SM, Mahoney Keira E KE, Lucas Taryn M TM, Rangel-Angarita Valentina V, Chen Ryan J RJ, Malaker Stacy A SA"],"additional_accession":[]},"is_claimable":false,"name":"GlycoFASP: A Universal Method to Prepare Complex Mixtures for O-Glycoproteomic Analysis","description":"Here we describe a method titled filter-aided preparation of O-glycoproteomic samples (GlycoFASP) which takes advantage of molecular-weight cut-off filters and O-glycoprotease digestion specificity. Using GlycoFASP, preparation for MS analysis of biological samples is completed within one day and only requires one milligram of sample. It is both low-cost and amenable to non-specialists. GlycoFASP regularly achieves depletion of nearly all non-O-glycosylated proteins, with ≥70% of the protein signal originating from O-glycoproteins.","dates":{"publication":"2026-07-08","submission":"2025-03-13"},"accession":"PXD061804","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:193528","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:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","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:2767842","NEWT:314345","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:1310161","NEWT:1230383","NEWT:77133","NCBITaxon:5207","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:32201","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:2709072","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:1195466","NEWT:2483192","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:427924","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:29471","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:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:480020","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:4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