# Protein phosphorylation networks in Baylisascaris procyonis revealed by phosphoproteomic analysis

## TL;DR

This study identifies 450 phosphorylated proteins in the raccoon roundworm, revealing key processes like cytoskeleton control and host interaction that could help develop new treatments.

## Contribution

First phosphoproteomic analysis of B. procyonis, revealing phosphorylation sites and their roles in critical biological processes.

## Key findings

- 854 unique phosphorylation sites were identified across 450 proteins in B. procyonis.
- Phosphoproteins were linked to cytoskeletal remodeling, developmental regulation, and host interaction pathways.
- Enriched pathways included insulin signaling, endocytosis, and glycolysis, with the Src homology 3 domain being significantly enriched.

## Abstract

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.

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).

Our phosphoproteome analysis displayed 854 unique phosphorylation sites mapped to 450 proteins in B. procyonis (3308 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.

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.

The online version contains supplementary material available at 10.1186/s13071-025-06949-y.