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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/46049
Title: Comparative characterization of four calcium-binding EF hand proteins from opisthorchis viverrini
Authors: Palida Emmanoch
Nanthawat Kosa
Suksiri Vichasri-Grams
Smarn Tesana
Rudi Grams
Amornrat Geadkaew-Krenc
Faculty of Medicine, Khon Kaen University
Mahidol University
Thammasat University
Keywords: Immunology and Microbiology;Medicine
Issue Date: 1-Feb-2018
Citation: Korean Journal of Parasitology. Vol.56, No.1 (2018), 81-86
Abstract: © 2018, Korean Society for Parasitology and Tropical Medicine. 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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85044380818&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/46049
ISSN: 17380006
00234001
Appears in Collections:Scopus 2018

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