{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD079660/proteomic.xlsx"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD079660/proteomic.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD079660/phosphoproteomic.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD079660/phosphoproteomic_Results.zip"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["cryptosporida@gmail.com"],"submitter":["Dongqiang Wang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Phosphorylation","Cryptosporidium parvum","Phosphoproteomics","Dia-pasef","Proteomics","Sporozoite","Glycolysis","Lc-ms/ms","Carbohydrate metabolism","Dia"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079660"],"sample_protocol":["Cryptosporidium parvum JLU01 oocysts were purified from calf feces and stored in PBS containing antibiotics at 4°C. Free sporozoites were obtained by in vitro excystation in RPMI-1640 medium supplemented with 0.5% sodium taurocholate at 37°C for 45 min. Excysted sporozoites were washed with prewarmed RPMI-1640 medium and lysed in RIPA buffer containing protease inhibitors by repeated freeze–thaw cycles. For proteomic analysis, protein extracts were evaluated by Bradford assay and SDS-PAGE, digested with trypsin, desalted, and fractionated by high-pH reversed-phase HPLC. Peptide fractions were analyzed by nano-LC-MS/MS using DDA and DIA acquisition. For phosphoproteomic analysis, independently prepared sporozoite samples were pooled, proteins were acetone-precipitated, reduced, alkylated, digested with trypsin, and phosphopeptides were enriched using immobilized metal affinity chromatography. Enriched phosphopeptides were analyzed by LC-MS/MS on a Bruker timsTOF Pro 2 instrument operated in dia-PASEF mode."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For proteomic data, DDA raw files were processed with MaxQuant using the Andromeda search engine, and the resulting identifications were used to construct a project-specific spectral library for DIA analysis. MS/MS spectra were searched against the Cryptosporidium parvum RefSeq protein database concatenated with a reverse decoy database. Trypsin/P was specified as the digestion enzyme, allowing up to two missed cleavages. Carbamidomethylation of cysteine was set as a fixed modification, and oxidation of methionine and protein N-terminal acetylation were included as variable modifications. Peptide-spectrum matches, peptides, and proteins were filtered at a 1% false discovery rate. DIA data were analyzed using a spectral library-based workflow with iRT calibration, targeted data extraction, mProphet-based scoring, FDR control, and protein-level quantification. For phosphoproteomic data, dia-PASEF raw files were processed using Spectronaut version 18. Spectra were searched against the C. parvum RefSeq-based FASTA database with a reverse decoy database. Phosphorylation of serine, threonine, and tyrosine residues was included as a variable modification, and peptide- and protein-level FDRs were controlled at less than 1%."],"omics_type":["Proteomics"],"labhead":["Guan Zhu"],"instrument_platform":[""],"labhead_affiliation":["State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Institute of Zoonosis, and College of Veterinary Medicine, Jilin University, Changchun, China"],"submission_type":["PARTIAL"],"species":["Cryptosporidium Parvum X Cryptosporidium Tyzzeri"],"publication":["42393791 Wang D, Li M, Wang C, Li H, Yin J, Zhu G. A comprehensive proteome and the first phosphoproteome reveal extensive phosphorylation of carbohydrate metabolism in Cryptosporidium parvum sporozoites. Parasit Vectors. 2026 19(1):408 10.1186/s13071-026-07538-3"],"submitter_mail":["wangdq909@163.com"],"submitter_affiliation":["jilin university"],"submitter_country":["China"],"pubmed_abstract":["<h4>Background</h4>Cryptosporidium parvum is an obligate apicomplexan parasite and a major cause of diarrheal disease in humans and animals worldwide. Despite its public health importance, the molecular regulation of parasite metabolism, particularly at the post-translational level, remains poorly understood. This study aims to understand major pathways regulated by protein phosphorylation in sporozoites, the parasite invasive stage, by comparative analysis of the proteomic and phosphoproteomic profiles.<h4>Methods</h4>The proteome and phosphoproteome of excysted sporozoites of C. parvum were determined by data-independent acquisition-based mass spectrometry. Highly abundant pathways at proteomic and phosphoproteomic levels were identified by functional enrichment. A relative phosphorylation index (RPI) was developed for comparative assessment of phosphorylation propensity across proteins.<h4>Results</h4>Proteomics identified 2,272 proteins in the sporozoites, representing 58% of the predicted parasite proteome. Phosphoproteomics identified 8,994 phosphorylation sites across 2,141 proteins; after intensity filtering, 833 phosphoproteins were retained for downstream analysis, representing 36.7% of the detected proteome. The correlations between transcript and protein abundances are weak. Proteins involved in carbohydrate metabolism, particularly glycolysis, are highly abundant in the proteome and phosphoproteome. Proteins in carbohydrate metabolism, signaling, cytoskeletal organization, and host-parasite interaction are selectively phosphorylated. In carbohydrate metabolism, starch degradative enzymes exhibit greater phosphorylation propensity than glycolytic and fermentative enzymes.<h4>Conclusions</h4>The C. parvum sporozoites translate more than half of the protein-coding genes, in which one-third of the proteome is phosphorylated in varied degrees. In the highly active energy metabolism, starch degradation enzymes show greater phosphorylation propensity than core glycolytic and fermentative enzymes. This study reveals the first phosphoproteome and the largest proteome for C. parvum, providing a resource for further investigations of the functional regulation by protein phosphorylation."],"pubmed_title":["A comprehensive proteome and the first phosphoproteome reveal extensive phosphorylation of carbohydrate metabolism in Cryptosporidium parvum sporozoites."],"pubmed_authors":["Wang Dongqiang D, Li Meng M, Wang Chenchen C, Li Haitao H, Yin Jigang J, Zhu Guan G"],"additional_accession":[]},"is_claimable":false,"name":"A comprehensive proteome and the first phosphoproteome reveal extensive phosphorylation of carbohydrate metabolism in Cryptosporidium parvum sporozoites","description":"Cryptosporidium parvum is an obligate intracellular apicomplexan parasite and a major cause of diarrheal disease in humans and animals. This dataset provides a comprehensive proteomic and phosphoproteomic resource for excysted C. parvum sporozoites, the invasive stage responsible for host cell entry. Data-independent acquisition-based proteomic analysis identified 2,272 proteins, representing approximately 58% of the predicted parasite proteome. In parallel, phosphoproteomic profiling identified 8,994 phosphorylation sites across 833 phosphoproteins. Integrated analysis of protein abundance and phosphorylation revealed extensive post-transcriptional and post-translational regulation in sporozoites, with prominent representation of carbohydrate metabolism and selective phosphorylation of enzymes associated with glycolysis and connected metabolic pathways. This dataset provides a molecular resource for studying protein expression, phosphorylation, metabolism, and host invasion in C. parvum.","dates":{"publication":"2026-09-28","submission":"2026-06-13"},"accession":"PXD079660","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:625351","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:57577","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","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:67352","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","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:29064","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:273791","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:33554","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:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","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:980415","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:66440","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:34878","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:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","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:237610","NEWT:95486","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","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:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","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:3728","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:207340","NEWT:172271","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","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:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","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:7375","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:2925","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NE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