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PXD043166-3

PXD043166 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleGlobal profiling of the proteome, phosphoproteome, and N-glycoproteome of protoscolex and adult worms of Echinococcus granulosus
DescriptionCystic echinococcosis (CE) is a chronic zoonosis caused by infection with the larval stage(protoscoleces, PSCs) of the cestode Echinococcus granulosus. A unique characteristic of the PSC is an ability to develop bidirectionally into an adult worm in the definitive host or into a secondary hydatid cyst in the intermediate host. Furmore, the cestode has a complex life-cycle involving different development stages but the mechanisms underpinning this development. Many studies have demonstrated that some matrix proteins undergo posttranslational modifications, including phosphorylation and glycosylation, which have important regulatory effects on the functional properties of the proteins. Systematic analysis of the proteome, the phosphorylated modified proteome and the glycosylated modified proteome of the PSCs and adult worms was performed using a proteomics strategy. A total of 6407 phosphorylation sites and 1757 proteins were quantifiable. Of those, 2032 phosphorylation sites and 770 proteins were up-regulated, and 2993 phosphorylation sites and 1217 proteins were down-regulated in the PSCs compared with the adult worms. A total of 612 N-glycosylation sites within 392 N-glycoproteins were identified. Of which, 355 N-glycosylation sites and 212 N-glycoproteins were quantifiable. Of those, 90 N-glycosylation sites and 64 N-glycoproteins were up-regulated, and 171 N-glycosylation sites and 126 N-glycoproteins were down-regulated 6407 in the PSCs compared with the adult worms. GO enrichment analysis indicated that the differently expressed phosphoproteins were mainly enriched in regulation of oxidoreduction coenzyme metabolic process, myelin sheath and RNA helicase activity, while the differently expressed N-glycoproteins were enriched in the cellular response to unfolded protein, endoplasmic reticulum lumen and nucleic acid binding. KEGG enrichment analysis indicated that the differently expressed phosphoproteins were mainly enriched in RNA transport, Hypertrophic cardiomyopathy (HCM), Glycolysis/Gluconeogenesis, HIF-1 signaling pathway and Pyruvate metabolism. while the differently expressed N-glycoproteins were enriched in PI3K-Akt signaling pathway, ECM-receptor interaction and Protein processing in endoplasmic reticulum.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_06:13:39.800.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterZhengrong Wang
SpeciesList scientific name: Echinococcus granulosus; NCBI TaxID: 6210;
ModificationListN-glycosylated residue; phosphorylated residue
InstrumenttimsTOF Pro
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-06-21 05:35:28ID requested
12023-10-31 19:48:17announced
22023-11-14 09:06:10announced2023-11-14: Updated project metadata.
32024-10-22 06:13:40announced2024-10-22: Updated project metadata.
Publication List
10.3389/FVETS.2023.1275486;
Keyword List
submitter keyword: Echinococcus granulosus
phosphoproteome
N-glycoproteome
Global profiling
Contact List
Zhengrong Wang
contact affiliationInstitute of Animal Husbandry and Veterinary Medicine, Xinjiang Academy of Agricultural and Reclamation Sciences
contact emailwzrtiger@sina.com
lab head
Zhengrong Wang
contact affiliationXinjiang Academy of Agricultural Sciences
contact emailwzrtiger@sina.com
dataset submitter
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Dataset FTP location
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