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Updated: Jul 16, 2026

Functional Cloning Using a Xenopus Oocyte Expression System
Published on: January 30, 2016
Clonorchis sinensis: molecular cloning, enzymatic activity, and localization of yolk ferritin
Yi Tang1, Pyo Yun Cho, Tae Im Kim
1Department of Parasitology, Chung-Ang University College of Medicine, Tongjak-gu, Seoul 156-756, Republic of Korea.
Abstract:
Ferritin is an intracellular protein that is involved in iron metabolism. A cDNA clone of Clonorchis sinensis (CsFtn), 565 bp long, encoded a putative polypeptide of 166 amino acids. CsFtn cDNA revealed a putative loop-stem structure similar to iron-responsive element (IRE). CsFtn polypeptide appeared homologous to the ferritin of trematodes with high sequential identity. Phylogenetic tree analysis showed that CsFtn clustered with the ferritins of other flukes. Recombinant CsFtn protein was produced and purified from an Escherichia coli system, and immune mouse serum was raised against CsFtn. Recombinant CsFtn showed iron-uptake ability. In adult C. sinensis, CsFtn protein was found to localize in vitelline follicles and eggs. Based on these results, CsFtn cDNA is considered to encode a C. sinensis yolk ferritin.
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