PXD043166-2

PXD043166 is an original dataset announced via ProteomeXchange.

Title	Global profiling of the proteome, phosphoproteome, and N-glycoproteome of protoscolex and adult worms of Echinococcus granulosus
Description	Cystic 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.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_09:06:10.358.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Zhengrong Wang
SpeciesList	scientific name: Echinococcus granulosus; NCBI TaxID: 6210;
ModificationList	N-glycosylated residue; phosphorylated residue
Instrument	timsTOF Pro

Revision	Datetime	Status	ChangeLog Entry
0	2023-06-21 05:35:28	ID requested
1	2023-10-31 19:48:17	announced
⏵ 2	2023-11-14 09:06:10	announced	2023-11-14: Updated project metadata.
3	2024-10-22 06:13:40	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: Echinococcus granulosus

phosphoproteome

N-glycoproteome

Global profiling

Zhengrong Wang
contact affiliation	Institute of Animal Husbandry and Veterinary Medicine, Xinjiang Academy of Agricultural and Reclamation Sciences
contact email	wzrtiger@sina.com
lab head
Zhengrong Wang
contact affiliation	Xinjiang Academy of Agricultural Sciences
contact email	wzrtiger@sina.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD043166
     1. Label: PRIDE project
     2. Name: Global profiling of the proteome, phosphoproteome, and N-glycoproteome of protoscolex and adult worms of Echinococcus granulosus