Dataset Information

Protein phosphorylation networks in Baylisascaris procyonis revealed by phosphoproteomic analysis

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Baylisascaris Procyonis

TISSUE(S): Whole Body

SUBMITTER: QIN MENG

LAB HEAD: Wei Liu

PROVIDER: PXD066529 | Pride | 2025-08-04

REPOSITORIES: Pride

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			Action	DRS
	AE022PIST_BP_1_Slot2-29_1_10660.d.zip	Other
	AE022PIST_BP_2_Slot2-29_1_10662.d.zip	Other
	AE022PIST_BP_3_Slot2-29_1_10664.d.zip	Other
	checksum.txt	Txt
	txt1.zip	Other

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Protein phosphorylation networks in Baylisascaris procyonis revealed by phosphoproteomic analysis.

Meng Qin Q Li Zhikang Z Qiu Qiguan Q Chen Shuyu S Gong Haiyan H Tan Xiaoruo X Liu Xiaoheng X Chen Zhaoguo Z Liu Wei W

Parasites & vectors 20250728 1

<h4>Background</h4>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.<h4>Methods</h4>In this study, the entire proteome of adult B. procyonis was enzymatically digested. Then, phospho ...[more]

PMID: 40722118

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