{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/mqpar_phos.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/mqpar_TPNg.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/4TPNg.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/TPPY-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/3TPNg.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/2TPNg.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/TPPY-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/TPPY-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/TPPY-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/1TPNg.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/TPPY-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/TPPY-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/71054TPNg_Search.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD014116/7421TP_search.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mlzzcld@aliyun.com"],"submitter":["Qingguo Meng"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":[""],"submitter_keywords":["Eriocheir sinensis","Phosphoproteome","N-glycoproteome","Spiroplasma eriocheiris","Hemocytes"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD014116"],"tissue":["Hemolymph"],"sample_protocol":["2.1.Experimental bacterial infection and hemocytes collection S. eriocheirisused in this study was isolated from the diseasedE. sinensisusing themethods described byWang et al.11and were cultured in R2 medium at 30 ℃. E. sinensis (50±5 g) were purchased from anaquaculture farminBaoying, Jiangsu Province, China and cultivated inan ultraviolet radiation sterilization circulating water temperature controlledaquaculture system. HealthyE. sinensis(verified by S. eriocheiris negative results using PCR of 16s rRNA sequenceanalyses) weremaintained for 1 week before tests. The crabsin the experimentalgroup (30 individuals) received an injection of 100 μL of S. eriocheiris (107 cells/ml). Thirty crabs in the controlgroup received an injection of 100 μL of R2 medium. Ten crabs from the control group or the experimental group,at 24 h post-injection were randomly collected to prepare hemocyte samples, the samples from ten crabs were mixed together to analysis.For phosphoproteome,experimental group (IS-P) and control group (IR-P). For N-glycoproteome, experimental group (IS-G) and control group (IR-G). Previous studies have indicated that theS. eriocheiris start to enter the hemocyteat 24 h. The hemolymph was drawn from crabsusing a 1-mL syringe, and quickly added into anticoagulant solutionat a ratio of 1:1. Sterile anticoagulant citrate dextrose solution B(ACD-B, glucose, 1.47 g; citrate, 0.48 g; sodium citrate, 1.32 g;pH = 4.0; prepared in double distilledwater at 100 mL final volume,and filtered with 0.22μM filter) was employed. Samples wereimmediately centrifuged at 4000 rpm, 4 ℃ for 5 min to collect thehemocytes. 2.2 Protein Extraction, Trypsin Digestion andTMT Labeling Carb hemocytes was sonicated three times on ice using a high intensity ultrasonic processor (40% power with 15’’ pulse and 45’’ interval,Scientz) in lysis buffer (8 M urea, 1% Protease Inhibitor Cocktail). The remaining debris was removed by centrifugation at 12,000 g at 4 ℃ for 10 min. Finally, the supernatant was collected and the protein concentration was determined with BCA kit according to the manufacturer’s instructions. For digestion, the protein solution was reduced with 5 mM dithiothreitol for 30 min at 56 ℃and alkylated with 11 mM iodoacetamide for 15 min at room temperature in darkness. The protein sample was then diluted by adding 100 mM TEAB to urea concentration less than 2M. Finally, trypsin was added at 1:50 trypsin-to-protein mass ratio for the first digestion overnight and 1:100 trypsin-to-protein mass ratio for a second 4 h-digestion. After trypsin digestion, peptide was desalted by Strata X C18 SPE column (Phenomenex) and vacuum-dried. Peptide was reconstituted in 0.5 M TEAB and processed according to the manufacturer’s protocol for TMT kit. Briefly, one unit of TMT reagent were thawed and reconstituted in acetonitrile. The peptide mixtures were then incubated for 2 h at room temperature and pooled, desalted and dried by vacuum centrifugation.The samples from ten crabs (experimental group and control group) were mixed together for phosphoproteome (IS-P and IR-P) and N-glycoproteome (IS-G and IR-G) analysis. SamplesIS-P and IR-P were labeled by 126 and 131, samplesIS-G and IR-G were labeled by 129 and 130, respectively.TMT labeling efficiency was evaluated for all sample, the labeling efficiency for phosphoproteome is 100%, for N-glycoproteome is 98%. 2.3Affinity Enrichment For phosphoproteome, the quantity of peptides used for phosphorylation enrichment is 1.9 mgof each fraction,peptide mixtures were first incubated with immobilized metal ion affinity chromatography (IMAC) microspheres suspension with vibration in loading buffer (50% acetonitrile/6% trifluoroacetic acid). Ti4+-IMAC microsphere was used here to enrich phosphopeptide and it was purchased from Dalian Institute of Chemical Physics.12The IMAC microspheres with enriched phosphopeptides were collected by centrifugation, and the supernatant was removed. To remove nonspecifically adsorbed peptides, the IMACmicrospheres were washed with 50% acetonitrile/6% trifluoroacetic acid and 30% acetonitrile/0.1% trifluoroacetic acid, sequentially. To elute the enriched phosphopeptides from the IMAC microspheres, elution buffer containing 10% NH4OH was added and the enriched phosphopeptides were eluted with vibration. The supernatant containing phosphopeptides was collected and lyophilized for LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For TMT quantification, the ratios of the TMT reporter ion intensities in MS/MS spectra (m/z 126–131) from raw data sets were used to calculate fold changes among samples.The resulting MS/MS data were processed using Maxquant search engine (v.1.5.2.8). Tandem mass spectra were searched against transcriptome of E. sinensis hemocytes database concatenated with reverse decoy database. Trypsin/P was specified as cleavage enzyme allowing up to 4 missing cleavages. The mass tolerance for precursor ions was set as 20 ppm in First search and 5 ppm in Main search, and the mass tolerance for fragment ions was set as 0.02 Da. Carbamidomethyl on Cys was specified as fixed modification and phosphorylation on Ser, Thr, Tyr and glycosylation on Asp were specified as variable modifications. False discovery rate (FDR) thresholds for protein, peptide and modification site were specified at 1%. Minimum peptide length was set at 7. All the other parameters in MaxQuant were set to default values. The site localization probability was set as > 0.5.Two-sample, two-sided T-tests were used to compare expression of proteins. In general, a significance level of 0.05 was used for statistical testing, and we reported the P value or significance level any time a statistical test was performed."],"omics_type":["Proteomics"],"labhead":["Qingguo Meng"],"instrument_platform":[""],"labhead_affiliation":["Jiangsu Key Laboratory for Aquatic Crustacean Diseases, College of Life Sciences&College of Marine Science and Engineering, Nanjing Normal University, 1 Wenyuan Road, Nanjing 210046, China"],"submission_type":["PARTIAL"],"species":["Eriocheir Sinensis (chinese Mitten Crab)"],"submitter_mail":["mlzzcld@aliyun.com"],"publication":["41814390 Yao Y, Ma Y, Yin X, Yu Z, Yan J, Hou L, Xu X, Gu W, Meng Q. Eriocheir sinensis PI3K-mediated 14-3-3ζ phosphorylation at a conserved tyrosine residue enhances ROS production to defend against Spiroplasma eriocheiris infection. Cell Commun Signal. 2026 24(1):237 10.1186/s12964-026-02781-8"],"submitter_affiliation":["Nanjing Normal University"],"submitter_country":["China"],"pubmed_title":["Eriocheir sinensis PI3K-mediated 14-3-3ζ phosphorylation at a conserved tyrosine residue enhances ROS production to defend against Spiroplasma eriocheiris infection."],"pubmed_authors":["Yao Yu Y, Ma Yubo Y, Yin Xin X, Yu Zhenyu Z, Yan Jing J, Hou Libo L, Xu Xuechuan X, Gu Wei W, Meng Qingguo Q"],"additional_accession":[]},"is_claimable":false,"name":"Protein phosphorylation and N-glycosylation in the early stage of Spiroplasma eriocheiris infect Eriocheir sinensis","description":"As a novel lethal pathogen of Eriocheirsinensistremor disease,Spiroplasma eriocheiris, has led into catastrophic economic losses in aquaculture.The hemocytes of E. sinensis is the first target cells of S. eriocheiris. Our study is the first time designed to understanding of the phosphoproteome and N-glycoproteome dynamics of E. sinensis hemocytesunderS. eriocheiris infected at the early phage. In the current study, the phosphoproteome and N-glycoproteome changes of E. sinensishemocytesafter S. eriocheiris infection were obtained usingtandem mass tags(TMT) labeling and affinity enrichment followed by high-resolution Liquid chromatography coupled tandem mass spectrometry (LC-MS/MS) analysis. Using a 1.2-fold change in expression as a physiologically significant benchmark.In total, 549 differentially expressed phosphoproteins were reliably quantified, including 278 up-regulated phosphoproteinsand 271 down-regulated phosphoproteins; 167 differentially expressed N-glycosylated proteins were reliably quantified, including 79 up-regulated glycosylated proteins and 88 down-regulated glycosylated proteins subsequented to S. eriocheiris infection.Gene ontology (GO) annotation, protein domain annotation, Kyoto Encyclopedia of Genes and Genomes (KEGG) annotation, subcellular localization annotation and protein-protein interaction network were used to analysis those significantly differentlyexpression proteins shown that many biological process and pathway are participate inS. eriocheiris infected host cell, such as phagocytosis, ECM-receptor interaction, lysosome, prophenoloxidase system, and so on. Our study could serve as a basis to understand the relationship between E. sinensisand the pathogen S. eriocheiris, and alsoprovide reference to study protein phosphorylation and N-glycosylationin other crustaceans.","dates":{"publication":"2026-04-27","submission":"2019-06-04"},"accession":"PXD014116","cross_references":{"TAXONOMY":["NEWT:3555","NEWT:71647","NEWT:330879","NEWT:35554","NCBITaxon:12939","NEWT:32046","NEWT:544496","NEWT:59529","NEWT:2042546","NEWT:32049","NEWT:1392696","NEWT:259447","NEWT:295546","NEWT:45351","NEWT:445974","NEWT:43179","NEWT:180454","NEWT:5722","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:10245","NEWT:55153","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:351581","NEWT:43186","NEWT:428146","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:1147161","NEWT:661410","NEWT:638632","NEWT:263737","NEWT:224326","NEWT:1333499","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:5702","NEWT:95648","NEWT:1589","NEWT:135622","NEWT:1349","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:1401257","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:44491","NEWT:641809","NEWT:27933","NEWT:556484","NEWT:317447","NEWT:4688","NEWT:7955","NEWT:7719","NEWT:7959","NEWT:2261","NEWT:868565","NEWT:31156","NEWT:3112","NEWT:79329","NEWT:4442","NEWT:192875","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:284218","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:1316931","NEWT:224308","NEWT:3347","NEWT:511145","NEWT:160621","NEWT:212790","NEWT:931281","NEWT:4432","NEWT:5762","NEWT:5763","NEWT:658457","NEWT:1310161","NEWT:77133","NEWT:295358","NEWT:145481","NEWT:29058","NCBITaxon:79824","NEWT:2246","NEWT:2652724","NEWT:5757","NEWT:68415","NCBITaxon:4563","NEWT:5755","NEWT:44688","NEWT:44689","NEWT:44447","NEWT:752555","NEWT:498211","NEWT:5759","NEWT:347256","NEWT:1736231","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:1392","NEWT:498217","NEWT:498216","NEWT:2242","NEWT:11320","NEWT:286","NEWT:391619","NEWT:246196","NEWT:287","NEWT:246197","NEWT:145458","NEWT:633149","NEWT:1149786","NEWT:10239","NEWT:68895","NEWT:44685","NEWT:161934","NEWT:4897","NEWT:1148","NEWT:5744","NEWT:72901","NEWT:213863","NEWT:5508","NEWT:3329","NEWT:5507","NEWT:410661","NEWT:55571","NEWT:35500","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:177437","NEWT:1772","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:263","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:11988","NEWT:284812","NEWT:8175","NEWT:400667","NEWT:43330","NEWT:1603293","NEWT:408169","NEWT:44664","NEWT:47946","NEWT:3702","NEWT:1245466","NEWT:243277","NEWT:1246791","NEWT:7067","NEWT:118694","NEWT:586722","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:274","NEWT:7070","NCBITaxon:287","NEWT:408172","NEWT:408170","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1436733","NEWT:460519","NEWT:1247411","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:333760","NEWT:34607","NEWT:56636","NEWT:1513458","NEWT:1233681","NCBITaxon:40559","NEWT:506599","NEWT:2853422","NEWT:81077","NEWT:84588","NEWT:1679718","NEWT:480","NEWT:65349","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:300852","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:508771","NEWT:1883446","NEWT:253","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:93062","NEWT:34613","NCBITaxon:4932","NEWT:109760","NEWT:29031","NEWT:943274","NEWT:644223","NEWT:235443","NEWT:108458","NEWT:5936","NEWT:272623","NEWT:272624","NEWT:320637","NEWT:886559","NEWT:3750","NEWT:55521","NEWT:983964","NEWT:118499","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:1130798","NEWT:55529","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:3988","NEWT:1116234","NEWT:561007","NEWT:1255228","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:3983","NEWT:203696","NEWT:352472","NEWT:97441","NEWT:1071661","NEWT:1202532","NEWT:360094","NEWT:1408223","NEWT:470","NEWT:1408224","NEWT:41364","NEWT:5911","NEWT:1313","NEWT:1218097","NEWT:1080348","NCBITaxon:50557","NEWT:1314","NEWT:39251","NEWT:39491","NEWT:212142","NCBITaxon:5811","NEWT:29491","NEWT:101841","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:571256","NEWT:40483","NEWT:63366","NEWT:63367","NEWT:688333","NEWT:215402","NCBITaxon:548681","NEWT:318586","NCBITaxon:5820","NEWT:1547","NEWT:272634","NEWT:198107","NEWT:9031","NEWT:27292","NEWT:1872122","NEWT:1308","NEWT:7091","NEWT:1034015","NEWT:760568","NEWT:141262","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:4087","NEWT:9778","NEWT:306","NEWT:150475","NEWT:303","NEWT:267872","NEWT:97477","NEWT:7111","NEWT:347515","NEWT:172269","NEWT:9534","NEWT:6269","NEWT:5180","NEWT:256737","NEWT:4090","NEWT:4092","NEWT:9541","NEWT:869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