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Fasciclin-calcareous corpuscle binary complex mediated protein-protein interactions in Taenia solium metacestode
Chun-Seob Ahn1, Jeong-Geun Kim1, Young-An Bae2
1Department of Molecular Parasitology, Samsung Medical Center, Sungkyunkwan University School of Medicine, Suwon, 16419, South Korea.
Background:
Neurocysticercosis (NC) caused by Taenia solium metacestode (TsM) is a serious neurological disease of global concern. Diverse bioactive molecules involved in the long-term survival of TsM might contribute to disease progression. Fasciclin (Fas) is an extracellular protein that mediates adhesion, migration and differentiation of cells by interacting with other molecules. We hypothesized that TsMFas might bind to calcareous corpuscle (CC) through its adhesive property and participate in crucial protein-protein interactions, thus contributing to the creation of a symbiotic interactome network.
Methods:
Two paralogous TsMFas (TsMFas1 and TsMFas2) were isolated, and their molecular properties were characterized. The co-localization pattern of TsMFas1 and TsMFas2 with CC was determined. CC-TsMFas binary complex was generated by incubating CC with recombinant proteins (rTsMFas1 and 2). In vitro binding assay of CC-rTsMFas1 or CC-rTsMFas2 binary complex with TsM cellular proteins extracted from scolex and neck was conducted. Their binding partners were identified through proteomic analysis. Integrated protein-protein interaction networks were established.
Results:
TsMFas1 (6072 bp long) was composed of 15 exons (841 amino acid polypeptide) interrupted by 14 introns. TsMFas2 (5201 bp long) comprised of 11 exons (597 amino acids) and 10 intervening introns. These proteins displayed 22% amino acid sequence identity to each other, but tightly conserved Fas-related domains. Several isoforms of Fas1 and Fas2 proteins might have been expressed through post-translational modifications. They showed adhesion activity with other cells. TsMFas proteins were largely distributed in parenchymal regions of the scolex and bladder wall. These molecules were co-localized with CC, a unique organelle found in platyhelminths. Subsequent proteome analysis of CC-Fas binary complex mediated protein-protein interactions revealed seven protein ligands in the TsM cellular proteins. Their functions were mainly segregated into carbohydrate metabolism (enolase, phosphoenolpyruvate carboxykinase, phosphoglycerate kinase and glyceraldehyde 3-phosphate dehydrogenase) and cytoskeleton/cellular motility (actin, paramyosin and innexin nuc-9). Those proteins had direct (physical) and/or indirect (functional) relationships along with their biochemical properties and biological roles.
Conclusion:
Protein repertoires strongly suggest that TsMFas and CC may symbiotically mediate protein-protein interactions during biological processes to maintain efficacious homeostatic functions and ensure the prolonged survival of TsM in the host.
Insights
Taenia solium metacestode Fasciclin (TsMFas) proteins bind to calcareous corpuscles (CC), forming complexes. This interaction involves key metabolic and motility proteins, aiding parasite survival.
Area of Science:
- Parasitology
- Molecular Biology
- Biochemistry
Background:
- Neurocysticercosis (NC), caused by Taenia solium metacestode (TsM), is a significant global health issue.
- TsM survival involves diverse bioactive molecules, including Fasciclin (Fas) proteins, which mediate cell adhesion and migration.
Purpose of the Study:
- To investigate the hypothesis that TsMFas binds to calcareous corpuscles (CC) via adhesive properties.
- To explore the role of TsMFas-CC interactions in protein-protein interactions and the formation of a symbiotic network for TsM survival.
Main Methods:
- Isolation and characterization of two paralogous TsMFas proteins (TsMFas1 and TsMFas2).
- Determination of co-localization patterns of TsMFas with CC.
- In vitro binding assays and proteomic analysis to identify binding partners and establish protein-protein interaction networks.
Main Results:
- Two TsMFas proteins (TsMFas1 and TsMFas2) were identified, showing conserved Fas domains and adhesion activity.
- TsMFas proteins co-localized with CC in TsM tissues.
- Proteomic analysis revealed seven protein ligands involved in carbohydrate metabolism and cytoskeleton/cellular motility, forming a complex network.
Conclusions:
- TsMFas and CC likely form a symbiotic interaction.
- This interaction mediates protein-protein interactions crucial for maintaining homeostasis and prolonged TsM survival within the host.