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생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
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A Novel Mannose-binding Tuber Lectin from Typhonium divaricatum (L.) Decne (family Araceae) with Antiviral Activity Against HSV-II and Anti-proliferative Effect on Human Cancer Cell Lines

  • Luo, Yongting (College of Life Sciences, Sichuan University) ;
  • Xu, Xiaochao (College of Life Sciences, Sichuan University) ;
  • Liu, Jiwei (College of Life Sciences, Sichuan University) ;
  • Li, Jian (College of Life Sciences, Sichuan University) ;
  • Sun, Yisheng (College of Life Sciences, Sichuan University) ;
  • Liu, Zhen (College of Life Sciences, Sichuan University) ;
  • Liu, Jinzhi (College of Life Sciences, Sichuan University) ;
  • Damme, Els Van (Department of Molecular Biotechnology, Ghent University) ;
  • Balzarini, Jan (Rega Institute for Medical Research, Katholieke University Leuven) ;
  • Bao, Jinku (College of Life Sciences, Sichuan University)
  • 발행 : 2007.05.31
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초록

A novel mannose-binding tuber lectin with in vitro antiproliferative activity towards human cancer cell lines and antiviral activity against HSV-II was isolated from fresh tubers of a traditional Chinese medicinal herb, Typhonium divaricatum (L.) Decne by a combined procedure involving extraction, ammonium sulfate precipitation, ion exchange chromatography on DEAE-SEPHAROSE, CM-SEPHAROSE and gel-filtration on sephacryl S-200. The apparent molecular mass of the purified Typhonium divaricatum lectin (TDL) was 48 kDa. TDL exhibits hemagglutinating activity toward rabbit erythrocytes at 0.95 $\mu$g/ml, and its activity could be strongly inhibited by mannan, ovomucoid, asialofetuin and thyroglobulin. TDL showed antiproliferative activity towards some well established human cancer cell lines, e.g. Pro-01 (56.7 $\pm$ 6.8), Bre-04 (41.5 $\pm$ 4.8), and Lu-04 (11.4 $\pm$ 0.3). The anti-HSV-II activity of TDL was elucidated by testing its HSV-II infection inhibitory activity in Vero cells with $TC_50$ and $EC_50$ of 5.176 mg/ml and 3.054 $\mu$g/ml respectively. The full-length cDNA sequence of TDL was 1145 bp and contained an 813-bp open reading frame (ORF) encoding a 271 amino acid precursor of 29-kDa. Homology analysis showed that TDL had high homology with many other mannose-binding lectins. Secondary and three-dimensional structures analyses showed that TDL is heterotetramer and similar with lectins from mannose-binding lectin superfamily, especially those from family Araceae.

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