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Characterization of Echinostoma cinetorchis endoribonuclease, RNase H

  • Lim, Sung-Bin (Department of Tropical Medicine and Parasitology, Inha University School of Medicine) ;
  • Cha, Seok Ho (Department of Tropical Medicine and Parasitology, Inha University School of Medicine) ;
  • Jegal, Seung (Department of Tropical Medicine and Parasitology, Inha University School of Medicine) ;
  • Jun, Hojong (Department of Tropical Medicine and Parasitology, Inha University School of Medicine) ;
  • Park, Seo Hye (Department of Tropical Medicine and Parasitology, Inha University School of Medicine) ;
  • Jeon, Bo-Young (Department of Biomedical Laboratory Science, College of Health Sciences, Yonsei University, School of Public Health) ;
  • Pak, Jhang Ho (Department of Convergence Medicine, University of Ulsan, College of Medicine, Asan Institute for Life Sciences, Asan Medical Center) ;
  • Bakh, Young Yil (Department of Biotechnology, Konkuk University) ;
  • Kim, Tong-Soo (Department of Tropical Medicine and Parasitology, Inha University School of Medicine) ;
  • Lee, Hyeong-Woo (Institute of Research and Development, Scorpiogen Co.)
  • 투고 : 2016.09.16
  • 심사 : 2017.08.02
  • 발행 : 2017.08.31

초록

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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