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Updated: May 6, 2026
Expression and Purification of Mammalian Bestrophin Ion Channels
Published on: August 2, 2018
Molecular characterization of voltage-gated calcium channel β-subunits of Clonorchis sinensis
Pyo Yun Cho1, Won Gi Yoo, Tae Im Kim
1Department of Parasitology and Inha Research Institute for Medical Sciences, Inha University School of Medicine, Incheon, 400-712, Republic of Korea.
Abstract:
The voltage-gated Ca(2+) channel β-subunit is a member of the membrane-associated guanylate kinase family and modulates kinetic properties of the Ca(2+) channels, such as their voltage-dependent activation and inactivation rates. Two cDNA clones were identified to encode each β-subunit isotype of the voltage-gated Ca(2+) channel of Clonorchis sinensis, CsCavβ1 and CsCavβ2, which consist of 606 and 887 amino acids, respectively. CsCavβ1 was found to be similar to the β-subunit containing two conserved serine residues that constitute the consensus protein kinase C phosphorylation site in the β-interaction domain (BID). CsCavβ2 had cysteine and alanine residues instead of the two serine residues conserved in BID and was homologous to variant β-subunit of Schistosoma mansoni and Schistosoma japonicum. CsCavβ1 and CsCavβ2 were almost equally expressed in the adults and metacercariae, but were more expressed in adult C. sinensis than in metacercariae. Collectively, our findings suggest that substitution of the two serine residues in BID of CsCavβ2 may render C. sinensis sensitive to praziquantel.
Insights
Researchers identified two voltage-gated calcium channel beta-subunits (CsCavβ1 and CsCavβ2) in Clonorchis sinensis. Variations in CsCavβ2 may increase susceptibility to praziquantel, a key anti-parasitic drug.
Area of Science:
- Molecular Biology
- Parasitology
- Biochemistry
Background:
- Voltage-gated calcium channels are crucial for cellular functions, modulated by beta-subunits.
- The beta-subunit interacts with the guanylate kinase domain, influencing channel kinetics.
- Clonorchis sinensis is a parasitic flatworm causing clonorchiasis.
Purpose of the Study:
- To identify and characterize beta-subunit isotypes of voltage-gated calcium channels in Clonorchis sinensis.
- To investigate the structural differences between identified beta-subunits.
- To explore the potential implications of these differences for drug sensitivity.
Main Methods:
- cDNA cloning and sequencing to identify beta-subunit isotypes.
- Amino acid sequence analysis to identify conserved domains and variations.
- Gene expression analysis using quantitative methods (e.g., RT-PCR) in different life stages.
Main Results:
- Two distinct beta-subunit isotypes, CsCavβ1 and CsCavβ2, were identified in C. sinensis.
- CsCavβ1 possesses conserved serine residues in the beta-interaction domain (BID), typical for protein kinase C phosphorylation.
- CsCavβ2 exhibits cysteine and alanine substitutions in the BID, differing from CsCavβ1 and showing homology to schistosome variants.
- Both isotypes were expressed in adult worms and metacercariae, with higher expression in adults.
Conclusions:
- The identified beta-subunit isotypes, CsCavβ1 and CsCavβ2, play roles in C. sinensis biology.
- Structural variations in the BID of CsCavβ2, specifically the serine-to-cysteine/alanine substitution, may alter its function.
- These alterations in CsCavβ2 could potentially confer sensitivity to praziquantel, a critical drug for treating parasitic infections.
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