Comparative Characterization of Four Calcium-Binding EF Hand Proteins from Opisthorchis viverrini
- Author:
Palida EMMANOCH
1
;
Nanthawat KOSA
;
Suksiri VICHASRI-GRAMS
;
Smarn TESANA
;
Rudi GRAMS
;
Amornrat GEADKAEW-KRENC
Author Information
- Publication Type:Brief Communication
- Keywords: Opisthorchis viverrini; Platyhelminthes; EF hand motif; calcium-binding; dynein light chain; tegument
- MeSH: Antibodies; Blotting, Western; Calcium-Binding Proteins; Cations, Divalent; Dyneins; EF Hand Motifs; Electrophoretic Mobility Shift Assay; Fasciola hepatica; Humans; Molecular Weight; Opisthorchiasis; Opisthorchis; Parasites; Protein Isoforms
- From:The Korean Journal of Parasitology 2018;56(1):81-86
- CountryRepublic of Korea
- Language:English
- Abstract: Four isoforms of calcium binding proteins containing 2 EF hand motifs and a dynein light chain-like domain in the human liver fluke Opisthorchis viverrini, namely OvCaBP1, 2, 3, and 4, were characterized. They had molecular weights of 22.7, 21.6, 23.7, and 22.5 kDa, respectively and showed 37.2–42.1% sequence identity to CaBP22.8 of O. viverrini. All were detected in 2- and 4-week-old immature and mature parasites. Additionally, OvCaBP4 was found in newly excysted juveniles. Polyclonal antibodies against each isoform were generated to detect the native proteins in parasite extracts by Western blot analysis. All OvCaBPs were detected in soluble and insoluble crude worm extracts and in the excretory-secretory product, at approximate sizes of 21–23 kDa. The ion-binding properties of the proteins were analyzed by mobility shift assays with the divalent cations Ca²⁺, Mg²⁺, Zn²⁺, and Cu²+. All OvCaBPs showed mobility shifts with Ca²⁺ and Zn²⁺. OvCaBP1 showed also positive results with Mg²⁺ and Cu²⁺. As tegumental proteins, OvCaBP1, 2, and 3 are interesting drug targets for the treatment of opisthorchiasis.
