{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-N-HCD220TparvaPostBasicSearch_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-N-HCD220TparvaBovineAPandPellet_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/AGAINST-TAURUS_O-GLYCAN-HCD_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-O-HCD220TparvaBovine_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/BasicSearch-Default_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-N-HCD220Tparva-re_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-O-HCD220TparvaPostBasicSearch_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-N-HCD220TparvaBovineDPonly_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/AGAINST-THEILERIA_N-GLYYCAN-HCD_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/AGAINST-THEILERIA_O-GLYCAN-OPEN-HCD_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-O-open-HCD220Tparva_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Theileria_search_result_comparison.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/AGAINST-THEILERIA_O-GLYCAN-HCD_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/AGAINST-TAURUS_N-GLYCAN-HCD_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-N-HCD220Bos_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-O-HCD220Bos_psm.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/Glyco-O-HCD220Tparva_psm.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/2303047_Tparva_AP.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/20240131_JST_Shi_WGA_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/20231107_JST_AP.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/20231107_JST_DP.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/20240131_JST_Shi_WGA_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/2303046_Tparva_DP_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/2303046_Tparva_DP.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/20240131_JST_Shi_WGA_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/20240131_JST_Shi_WGA_3.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/UP_Theileria_parva_tx5875_2790_231027.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD070746/UP_Bos_taurus_tx9913_37504_231027.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["shi.yan@vetmeduni.ac.at"],"submitter":["Shi Yan"],"technology_type":["Glycoproteomics","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070746"],"sample_protocol":["To determine potential parasite glycans, proteins from AP and DP fractions of TpM schizonts were subjected to glycoproteomic analyses using mass spectrometry (MS). Briefly, protein samples were denatured in reducing buffer (8 M urea, 50 mM ammonium bicarbonate, 5 mM DTT, pH 7.8) and treated with trypsin (Promega) overnight at 37°C. The resulting peptides were purified using hand-packed C18 cartridges (50% acetonitrile with 0.1% trifluoroacetic acid as eluent) and evaporated to dryness using a speed-vac concentrator. Dried peptides were resuspended in HPLC-grade water and analysed on an Autoflex Speed MALDI-TOF MS (Bruker Daltonics) using α-cyano-4-hydroxycinnamic acid or 6-aza-2-thiothymine as matrix. The instrument was calibrated with the Bruker Peptide Calibration Standard II.   Additionally, AP and DP samples were analysed by nanoLC-ESI-MS(/MS), using a Q Exactive HF Orbitrap mass spectrometer (Thermo Fisher Scientific) coupled to a nano-HPLC Ultimate 3000 RSLC system (Dionex) for peptide separation. MS full scans were performed in the ultrahigh-field Orbitrap mass analyser in ranges m/z 350−2,000 with a resolution of 60,000, the maximum injection time (MIT) was 50 ms and the automatic gain control (AGC) was set to 3e^6. The top ten intense ions of each MS scan were selected for gas-phase fragmentation using high energy collision dissociation (HCD). For each MS/MS scan, the AGC was set at 5e^4 and the MIT was 50 ms. Dynamic exclusion of precursor ion masses over a time window of 30s was used to reduce MS/MS data redundancy.  Overall glycopeptide populations of AP and DP samples were enriched using hydrophilic interaction liquid chromatography (HILIC), as described recently. In brief, dried (glyco)peptides were re-suspended in 50 µL of 80% acetonitrile containing 1% trifluoroacetic acid (TFA) and fractionated using a TSK-Amide 80 column (4.6 x 250 mm, 5 µm, Tosoh). A linear gradient was developed from 80% acetonitrile with 0.1% TFA to 50% acetonitrile with 0.1% TFA over 30 minutes, at a flow rate of 1 mL/min. Fractions of 1 mL were collected using a fraction collector (Shimadzu). Late-eluting HILIC fractions (minutes 20–39) were pooled and lyophilised prior to LC-MS/MS analysis.  Enriched (glyco)peptides were resuspended in 20 µL of 0.1% formic acid and separated by reversed-phase nano-LC using a nanoEase M/Z HSS T3 column (100 Å, 1.8 µm, 300 µm × 150 mm; Waters). MS/MS analysis was performed on an Orbitrap Exploris 480 mass spectrometer (Thermo Fisher Scientific) equipped with a standard H-ESI source, operated in positive ion mode. MS spectra were acquired in the m/z range of 350–1500 at a resolution of 60,000. Data-dependent MS/MS acquisition was triggered for precursor ions with charge states 2–6 and intensities above 800,000, using an isolation window of 1.4 m/z (offset 0.5 m/z), with a normalised AGC target of 200%. Fragmentation was performed using stepped HCD. MS/MS scans were acquired at a resolution of 30,000 with the first fixed mass set at m/z 120."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data of C18-purified AP and DP samples were searched against proteomes of T. parva (Taxon ID: 5875; 2790 entries) and B. taurus (Taxon ID: 9913; 37504 entries) using Proteome Discoverer (version 2.4.1.15; Thermo Fisher Scientific). Furthermore, all LC-ESI-MS/MS data were also analysed using the FragPipe Software version 220 with the MSFragger search engine (Nesvilab) for glycopeptide identification. Prediction of signal peptides and transmembrane domains as well as N-glycosylation sites for identified proteins was performed with the SignalP-6.0, Deep TMHMM-1.0 algorithms and NetNGlyc - 1.0, respectively, developed by DTU Health Tech."],"omics_type":["Proteomics"],"labhead":["Shi Yan"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["University of Veterinary Medicine Vienna"],"species":["Bos Taurus (bovine)","Theileria Parva"],"submitter_mail":["shi.yan@vetmeduni.ac.at"],"publication":["42339100 Kolakowski J, Yan S, Stadlmann J, Lepenies B, Ngugi D, Harris H, Werling D. Investigation of carbohydrate-based molecules of &lt;i&gt;Theileria parva&lt;/i&gt; parasites. Front Vet Sci. 2026 13:1816563 10.3389/fvets.2026.1816563"],"submitter_affiliation":["University of Veterinary Medicine Vienna"],"submitter_country":["Austria"],"pubmed_abstract":["<i>Theileria parva</i> (Tp), the causative agent of East Coast Fever, poses a major threat to <i>Bos taurus</i> cattle in sub-Saharan Africa. Progress towards a stable, affordable, cross-protective subunit vaccine covering more than one major histocompatibility complex (MHC)-presented Tp antigen has been hindered by the limited knowledge of antigens. Given the importance of glycoconjugates in protozoan pathogen biology, especially during the invasion process, we investigated the glycosylation potential of Tp. Screening of Tp Muguga (TpM) schizonts with C-type lectin (-like) receptors showed that ruminant, but not murine, Macrophage C-type Lectin (MCL) recognises the parasite. Binding of ruminant MCL to TpM schizonts suggested the presence of carbohydrate-associated parasite surface molecules. Lectin staining further suggested the presence of terminal GlcNAc residues on the parasite surface which is in alignment with the identification of a minimal N-glycosylation machinery in TpM schizonts. LC-MS/MS analysis of HILIC HPLC and lectin-enriched peptides from parasite protein fractions yielded eight predicted N-glycopeptides and two predicted O-glycopeptides. Putative parasite O-glycans were assigned with high confidence, yet assignments of putative N-glycans to parasite proteins were less confident. Our data provide first insights into potential TpM glycoconjugates while confirmation of glycan composition and assignment requires additional analyses."],"pubmed_title":["Investigation of carbohydrate-based molecules of &lt;i&gt;Theileria parva&lt;/i&gt; parasites."],"pubmed_authors":["Kolakowski Jeannine J, Yan Shi S, Stadlmann Johannes J, Lepenies Bernd B, Ngugi Daniel D, Harris Heather H, Werling Dirk D"],"additional_accession":[]},"is_claimable":false,"name":"Theileria parva Muguga (TpM) schizonts LC-MS/MS","description":"The apicomplexan parasite Theileria parva (Tp) causes East Coast Fever (ECF), an often fatal tick-borne disease especially for Bos taurus cattle breeds that causes substantial economic losses for cattle farmers in sub-Saharan Africa. Replacement of the currently employed live vaccine with a more standardised, stable, affordable, and cross-protective subunit vaccine has not yet been successful and requires the identification of additional suitable parasite antigens. Carbohydrate-based molecules play an important role in the survival and establishment of pathogens including protozoan parasites and can represent strong virulence factors. The current knowledge of the glycobiology of Tp, however, is very limited which led us to investigate the glycosylation potential of Tp in this study. Screening of isolated Tp Muguga (TpM) schizonts with C-type lectin (-like) receptors identified recognition of the parasites by ruminant but not murine Macrophage C-type lectin (MCL). This suggested the presence of carbohydrate-associated schizont surface molecules. Specific binding of isolated schizonts by WGA but not ConA further suggested the presence of terminal GlcNAc residues on the surface of the parasites which is in alignment with the identification of a minimal N-glycosylation machinery in TpM schizonts. LC-MS/MS analyses of either HILIC-HPLC or WGA enriched peptides from parasite protein fractions identified eight predicted N-glycopeptides and two predicted O-glycopeptides. While putative parasite O-glycans were assigned with high confidence, assignments of putative N-glycans to parasite proteins were less confident. Confirmation of both the assignment and the composition of predicted parasite glycans requires further analyses.","dates":{"publication":"2026-06-29","submission":"2025-11-14"},"accession":"PXD070746","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","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:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","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:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","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:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:48106","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:19662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