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Background   Giardia duodenalis  causes giardiasis, with diarrhea as the primary symptom. The trophozoite proliferation of this zoonotic parasite is mainly affected by telomerase, although the mechanism of telomerase regulation has not been thoroughly analyzed.    Methods  This study was performed to identify the telomerase RNA-binding domain (TRBD)-interacting protein in  G. duodenalis  and its regulation of telomerase. Interaction between TRBD and interacting proteins was verified  via  pulldown assays and co-immunoprecipitation (co-IP) techniques, and the subcellular localization of the protein interactions was determined  in vivo via  split SNAP-tag labeling. The hammerhead ribozyme was designed to deplete the mRNA of TRBD-interacting proteins.    Results  Using TRBD as bait, we identified zinc-finger domain (ZFD)-containing proteins and verified it  via  pulldown and co-IP experiments. Protein-protein interaction occurred in the nuclei of 293T cells and both nuclei of  G. duodenalis . The hammerhead ribozyme depleted ZFD mRNA levels, which reduced the reproduction rate of  G. duodenalis , telomerase activity and telomere length.    Conclusions  Our findings suggest that ZFD may regulate telomere function in  G. duodenalis  nuclei.

Identification of a TRBD zinc finger-interacting protein in Giardia duodenalis and its regulation of telomerase