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Updated: Feb 23, 2026

Overexpressing and Purifying a Toxic Nuclease from Escherichia coli
Published on: August 29, 2025
Characterization of Echinostoma cinetorchis endoribonuclease, RNase H
Sung-Bin Lim1,2, Seok Ho Cha1, Seung Jegal1,3
1Department of Tropical Medicine and Parasitology, Inha University School of Medicine, Incheon 22212, Korea.
Abstract:
Echinostoma cinetorchis is an oriental intestinal fluke causing significant pathological damage to the small intestine. The aim of this study was to determine a full-length cDNA sequence of E. cinetorchis endoribonuclease (RNase H; EcRNH) and to elucidate its molecular biological characters. EcRNH consisted of 308 amino acids and showed low similarity to endoribonucleases of other parasites (<40%). EcRNH had an active site centered on a putative DDEED motif instead of DEDD conserved in other species. A recombinant EcRNH produced as a soluble form in Escherichia coli showed enzymatic activity to cleave the 3'-O-P bond of RNA in a DNA-RNA duplex, producing 3'-hydroxyl and 5'-phosphate. These findings may contribute to develop antisense oligonucleotides which could damage echinostomes and other flukes.
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