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Global profiling of the proteome, phosphoproteome, and N-glycoproteome of protoscolex and adult worms of Echinococcus granulosus

ABSTRACT: 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.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Echinococcus Granulosus

TISSUE(S): Protoscolex, Adult

SUBMITTER: Zhengrong Wang

LAB HEAD: Zhengrong Wang

PROVIDER: PXD043166 | Pride | 2023-11-01

REPOSITORIES: Pride

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Project description:N-glycosylation is an important posttranslational modification in all eukaryotes, but little is known about the N-glycoproteomes in microalgal systems. Here, N-glycoproteome of the model diatom Phaeodactylum tricornutum was unveiled. Totally, 893 different N-glycosylated sites from 649 proteins were identified from P. tricornutum. The new synthesized N-glycans were principally transferred to asparagine residues within the conserved N-X-S/T (where X is a residue other than proline) sequence of nascent polypeptide chains. Functional annotation of N-glycosylated proteins showed that 70% N-glycoproteins were involved in vesicular transport and posttranslational modification, protein turnover, chaperones, indicating the N-glycosylation was important for these functions. Of the all identified N-glycoproteins 45.3% were predicted to localize on chloroplast, which implied the widespread regulatory role of N-glycosylation in chloroplast. Furthermore, the enrichment results of N-glycoproteins indicated that compared to ‘Cellular component’ and ‘Biological process’ categories proteins related with the ‘Molecular function’ category were more prone to be N-glycosylated. And it was speculated that N-glycosylation played a vital regulatory role in catalytic activity of enzymes and metabolism processes of many small molecules. 47% of all enriched proteins were related with metabolic pathways. The functional annotation and enrichment of N-glycoproteins suggested that N-glycoproteins participated in a variety of important metabolic pathways and perform different functions in P. tricornutum. 12 proteins involved in the ER quality control mechanism and ER- associated degradation pathway were identified as N-glycosylated proteins, indicating that the N-glycosylated modification was important for their functions in the protein N-glycosylation pathway. Additionally, some interacted glycoproteins were classified from this study, which provided valuable information for studying the functions of these glycoproteins. In the study, the identification of N-glycosylation on nascent proteins expands our understanding of this PTM at a proteomics scale and may facilitate the elucidation of the precise function of proteins in this model diatom.

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Global profiling of the proteome, phosphoproteome, and N-glycoproteome of protoscolex and adult worms of Echinococcus granulosus

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