Comparative Characterization of Four Calcium-Binding EF Hand Proteins from Opisthorchis viverrini.
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.
['Emmanoch|Palida|P|', 'Kosa|Nanthawat|N|', 'Vichasri-Grams|Suksiri|S|', 'Tesana|Smarn|S|', 'Grams|Rudi|R|', 'Geadkaew-Krenc|Amornrat|A|']
D000818:Animals D000909:Antibodies, Helminth D002118:Calcium D002135:Calcium-Binding Proteins D020832:EF Hand Motifs D015801:Helminth Proteins D008970:Molecular Weight D009889:Opisthorchiasis D009891:Opisthorchis D020033:Protein Isoforms
calcium-binding Opisthorchis viverrini EF hand motif tegument Platyhelminthes dynein light chain