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An EF-handed Ca2+-binding protein of Chinese liver fluke Clonorchis sinensis

Authors
Chung, Eun JooKim, Tae YunHong, Sung-JongYong, Tai-Soon
Issue Date
Dec-2013
Publisher
SPRINGER
Citation
PARASITOLOGY RESEARCH, v.112, no.12, pp 4121 - 4128
Pages
8
Journal Title
PARASITOLOGY RESEARCH
Volume
112
Number
12
Start Page
4121
End Page
4128
URI
https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/14057
DOI
10.1007/s00436-013-3603-0
ISSN
0932-0113
1432-1955
Abstract
A cDNA clone encoding 8 kDa protein was retrieved from an EST pool of Chinese liver fluke Clonorchis sinensis. A deduced polypeptide of the cDNA clone was similar to 8 kDa Ca2+-binding proteins from other parasitic trematodes, and, thus, named as CsCa8, containing two EF-hand Ca2+-binding sites. Homology models predicted CsCa8 to be a single globular structure having four helices and molecular folds similar to Ca2+-binding state of other small Ca2+-binding proteins. Recombinant CsCa8 protein showed specific Ca2+-binding affinity and shifting in native gel mobility assay. Mouse immune sera raised against recombinant CsCa8 protein recognized native CsCa8 from adult C. sinensis worm extract. CsCa8 was localized in oral and ventral suckers, vitelline follicles and subtegumental tissues. These findings suggest that CsCa8 might be involved in cellular Ca2+ signal transduction for muscle contraction and egg production.
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