Korean J Parasitol.
2017 Aug;55(4):451-455. 10.3347/kjp.2017.55.4.451.
Characterization of Echinostoma cinetorchis endoribonuclease, RNase H
- Affiliations
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- 1Department of Tropical Medicine and Parasitology, Inha University School of Medicine, Incheon 22212, Korea. tongsookim@inha.ac.kr
- 2Department of Bioscience, Dongkuk University, Seoul 04620, Korea.
- 3Department of Infectious Diseases Diagnosis, Incheon Institute of Public Health and Environment, Incheon 22320, Korea.
- 4Department of Biomedical Laboratory Science, College of Health Sciences, Yonsei University, School of Public Health, Wonju 26493, Korea.
- 5Department of Convergence Medicine, University of Ulsan, College of Medicine, Asan Institute for Life Sciences, Asan Medical Center, Seoul 05505, Korea.
- 6Department of Biotechnology, Konkuk University, Chungju 27478, Korea.
- 7Institute of Research and Development, Scorpiogen Co., Anseong 17579, Korea. rainlee67@naver.com
- KMID: 2389984
- DOI: http://doi.org/10.3347/kjp.2017.55.4.451
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"²-O-P bond of RNA in a DNA-RNA duplex, producing 3"²-hydroxyl and 5"²-phosphate. These findings may contribute to develop antisense oligonucleotides which could damage echinostomes and other flukes.
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