Publication: Molecular and biochemical characterization of opisthorchis Viverrini calreticulin
Issued Date
2017-12-01
Resource Type
ISSN
17380006
00234001
00234001
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2-s2.0-85040533197
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Mahidol University
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SCOPUS
Bibliographic Citation
Korean Journal of Parasitology. Vol.55, No.6 (2017), 643-652
Suggested Citation
Wanlapa Chaibangyang, Amornrat Geadkaew-Krenc, Suksiri Vichasri-Grams, Smarn Tesana, Rudi Grams Molecular and biochemical characterization of opisthorchis Viverrini calreticulin. Korean Journal of Parasitology. Vol.55, No.6 (2017), 643-652. doi:10.3347/kjp.2017.55.6.643 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/42732
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Title
Molecular and biochemical characterization of opisthorchis Viverrini calreticulin
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Abstract
© 2017, Korean Society for Parasitology and Tropical Medicine. Calreticulin (CALR), a multifunctional protein thoroughly researched in mammals, comprises N-, P-, and C-domain and has roles in calcium homeostasis, chaperoning, clearance of apoptotic cells, cell adhesion, and also angiogenesis. In this study, the spatial and temporal expression patterns of the Opisthorchis viverrini CALR gene were analyzed, and calcium-binding and chaperoning properties of recombinant O. viverrini CALR (OvCALR) investigated. OvCALR mRNA was detected from the newly excysted juvenile to the mature parasite by RT-PCR while specific antibodies showed a wide distribution of the protein. OvCALR was localized in tegumental cell bodies, testes, ovary, eggs, Mehlis’ gland, prostate gland, and vitelline cells of the mature parasite. Recombinant OvCALR showed an in vitro suppressive effect on the thermal aggregation of citrate synthase. The recombinant OvCALR C-domain showed a mobility shift in native gel electrophoresis in the presence of calcium. The results imply that OvCALR has comparable function to the mammalian homolog as a calcium-binding molecular chaperone. Inferred from the observed strong immunostaining of the reproductive tissues, OvCALR should be important for reproduction and might be an interesting target to disrupt parasite fecundity. Transacetylase activity of OvCALR as reported for calreticulin of Haemonchus contortus could not be observed.