PXD014116 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | 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. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-04-27 |
| AnnouncementXML | Submission_2026-04-26_16:38:17.965.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Qingguo Meng |
| SpeciesList | scientific name: Eriocheir sinensis (Chinese mitten crab); NCBI TaxID: NEWT:95602; |
| ModificationList | N-glycosylated residue; phosphorylated residue |
| Instrument | Q Exactive Plus |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2019-06-04 03:50:56 | ID requested | |
| ⏵ 1 | 2026-04-26 16:38:18 | announced | |
Publication List
| Yao Y, Ma Y, Yin X, Yu Z, Yan J, Hou L, Xu X, Gu W, Meng Q, phosphorylation at a conserved tyrosine residue enhances ROS production to defend against Spiroplasma eriocheiris infection. Cell Commun Signal, 24(1):(2026) [pubmed] |
| 10.1186/s12964-026-02781-8; |
Keyword List
| submitter keyword: phosphoproteome,Eriocheir sinensis,N-glycoproteome, Spiroplasma eriocheiris,hemocytes |
Contact List
| Qingguo Meng |
| contact 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 |
| contact email | mlzzcld@aliyun.com |
| lab head | |
| Qingguo Meng |
| contact affiliation | Nanjing Normal University |
| contact email | mlzzcld@aliyun.com |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
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| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD014116
- Label: PRIDE project
- Name: Protein phosphorylation and N-glycosylation in the early stage of Spiroplasma eriocheiris infect Eriocheir sinensis