Comparative Characterization of Four Calcium-Binding EF Hand Proteins from Opisthorchis viverrini

Palida Emmanoch; Nanthawat Kosa; Suksiri Vichasri-Grams; Smarn Tesana; Rudi Grams; Amornrat Geadkaew-Krenc

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자료유형: 학술저널

저자정보: Palida Emmanoch (Thammasat University) Nanthawat Kosa (Thammasat University) Suksiri Vichasri-Grams (Mahidol University) Smarn Tesana (Faculty of Medicine) Rudi Grams (Thammasat University) Amornrat Geadkaew-Krenc (Thammasat University)

저널정보: 대한기생충학열대의학회 Parasites, Hosts and Diseases The Korean Journal of Parasitology Vol.56 No.1

발행연도: 2018.2

수록면: 81 - 86 (15page)

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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.

#Opisthorchis viverrini #Platyhelminthes #EF hand motif #calcium-binding #dynein light chain #tegument

참고문헌 (30)

참고문헌 신청

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