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.
In trematodes, vitelline precursor proteins are required for eggshell formation. A cDNA clone of Clonorchis sinensis (CsVpB1) was selected from an EST pool, encoding a polypeptide of 245 amino acids. The CsVpB1 polypeptide demonstrated homology with vitelline precursor proteins from trematodes with high sequential identities. In a phylogenic tree, CsVpB1 clustered with trematode VpB proteins. The CsVpB1 polypeptide was found to be rich in tyrosine residues, including putative pre-dihydroxyphenyl alanine (DOPA) residues, involved in cross-linking of the precursor proteins. Mouse immune sera were raised against a recombinant CsVpB1 protein. In adult C. sinensis , CsVpB1 protein was exclusively localized in vitelline follicles. Based on these results, the CsVpB1 cDNA is believed to encode a VpB of C. sinensis .