Authors
Xianmei Wang, Na Yang, Shui Yu, Kun Guo, Shiman Yang, Lifang Wang, Qun Liu, Yong Fu, Jing Liu
Published in
International journal for parasitology. Pages 104924. Jul 09, 2026. Epub Jul 09, 2026.
Abstract
Neospora caninum is a major apicomplexan pathogen causing bovine abortion, resulting in major economic losses to the global livestock industry. Since its initial identification in 1988, N. caninum has emerged as one of the leading infectious causes of bovine abortion worldwide. Protein kinase G (PKG) acts as a central regulator of parasite motility, invasion, and egress; however, the downstream effectors that mediate these processes remain poorly defined. To systematically define the PKG-associated signaling network, we employed TurboID-mediated proximity labeling combined with subcellular localization profiling and phosphoproteomic analysis, identifying 37 high-confidence candidate proteins associated with PKG. These proteins are involved in vesicular trafficking, ion transport and metabolism, transcriptional regulation, and phosphoinositide/cyclic nucleotide signaling. We further identified a previously uncharacterized microneme-localized protein containing ion-transport domains, ITP1, that shows proximity to PKG and exhibits PKG-dependent phosphorylation. Genetic ablation of ITP1 significantly impaired parasite invasion and egress and reduced microneme protein secretion. These findings support a functional link between PKG signaling and ion transport-associated processes in the regulation of microneme exocytosis and host cell invasion in apicomplexan parasites.
PMID:
42425259
Bibliographic data and abstract were imported from PubMed on 10 Jul 2026.
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