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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/42732
Title: Molecular and biochemical characterization of opisthorchis Viverrini calreticulin
Authors: Wanlapa Chaibangyang
Amornrat Geadkaew-Krenc
Suksiri Vichasri-Grams
Smarn Tesana
Rudi Grams
Thammasat University
Mahidol University
Khon Kaen University
Keywords: Immunology and Microbiology
Issue Date: 1-Dec-2017
Citation: Korean Journal of Parasitology. Vol.55, No.6 (2017), 643-652
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85040533197&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/42732
ISSN: 17380006
00234001
Appears in Collections:Scopus 2016-2017

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