PXD066529

PXD066529 is an original dataset announced via ProteomeXchange.

Title	Protein phosphorylation networks in Baylisascaris procyonis revealed by phosphoproteomic analysis
Description	Background: Baylisascaris procyonis is an intestinal ascarid worm that parasitizes in raccoons and causes fatal neural, visceral, and ocular larva migrans in humans. Phosphorylated proteins and protein kinases have been studied as vaccine and drug target candidates against parasitic infections. However, no data are available on protein phosphorylation in the raccoon roundworm. Methods: In this study, the entire proteome of adult B. procyonis was enzymatically digested. Then, phosphopeptides were enriched using immobilized metal affinity chromatography (IMAC) and analyzed by liquid chromatography-mass spectrometry (LC-MS/MS). Results: Our phosphoproteome analysis displayed 854 unique phosphorylation sites mapped to 450 proteins in B. procyonis (3,308 phosphopeptides total). The annotated phosphoproteins were associated with various biological processes, including cytoskeletal remodeling, supramolecular complex assembly, and developmental regulation. The phosphopeptide functional enrichment revealed that B. procyonis phosphoproteins were mostly involved in the cytoskeleton cellular compartment, protein binding molecular function, and multiple biological processes, including regulating supramolecular fiber and cytoskeleton organization, and assembling cellular protein-containing complexes and organelles. The significantly enriched pathways of phosphoproteins included the insulin signaling pathway, tight junction, endocytosis, longevity-regulating, glycolysis/gluconeogenesis, and apelin signaling pathways. Domain analysis revealed that the Src homology 3 domain was significantly enriched. Conclusions: This study presents the first phosphoproteomic landscape of B. procyonis, elucidating phosphorylation-mediated regulation of cytoskeletal dynamics, host interaction pathways, and metabolic adaptations. The identified 450 phosphoproteins and enriched functional domains establish a foundation for targeting conserved mechanisms critical to B. procyonis survival.
HostingRepository	PRIDE
AnnounceDate	2025-08-04
AnnouncementXML	Submission_2025-08-03_16:08:36.054.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	QIN MENG
SpeciesList	scientific name: Baylisascaris procyonis; NCBI TaxID: 6259;
ModificationList	phosphorylated residue
Instrument	timsTOF Pro

Revision	Datetime	Status	ChangeLog Entry
0	2025-07-24 05:37:58	ID requested
⏵ 1	2025-08-03 16:08:36	announced

Meng Q, Li Z, Qiu Q, Chen S, Gong H, Tan X, Liu X, Chen Z, Liu W, Protein phosphorylation networks in Baylisascaris procyonis revealed by phosphoproteomic analysis. Parasit Vectors, 18(1):307(2025) [pubmed]

10.1186/s13071-025-06949-y;

submitter keyword: Raccoon, Liquid chromatography-mass spectrometry, signaling pathway,Baylisascaris procyonis, Phosphoproteome, Function

Wei Liu
contact affiliation	Research Center for Parasites & Vectors, College of Veterinary Medicine, Hunan Agricultural University, Changsha 410128, PR China
contact email	weiliupro@hunau.edu.cn
lab head
QIN MENG
contact affiliation	Hunan Agricultural University
contact email	1412296095@qq.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD066529
     1. Label: PRIDE project
     2. Name: Protein phosphorylation networks in Baylisascaris procyonis revealed by phosphoproteomic analysis