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Volume 19 Issue 3
June 2004
    Citation: LIANG Wen-xing, SONG Li-min, HUANG Jin-guang, TIAN Guo-zhong, LI Huai-fang, FAN Zai-feng. Expression of the cp gene and Antiserum Preparation of Wisteria Vein Mosaic Virus .VIROLOGICA SINICA, 2004, 19(3) : 281-284.
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    Expression of the cp gene and Antiserum Preparation of Wisteria Vein Mosaic Virus

    • 1.

      1.Department of Plant Pathology, China Agricultural University, Beijing 100094, China

    • 2.

      Research Institute of Forest Ecology, Environment and Protection, China Academy of Forestry, Beijing 100091, China

    • Corresponding author: FAN Zai-feng, 
    • Available online: 20 June 2004
    • The coat protein (CP) gene of the Beijing isolate of Wisteria vein mosaic virus (WVMV-BJ) was amplified by RT-PCR, and ligated to the expression vector pET22b(+). The recombinant plasmid pET-WVMVCP was transformed into E. coli BL21(DE3) and then induced by IPTG. It was shon that the CP gene was highly expressed by SDS-PAGE and Western blot analysis. The molecular weight of the recombinant protein was about 34.4kDa. Antiserum with high specificity was produced after the rabbit was immunized with purified recombinant protein, and the titer was determined to be 1/1024 by micro-precipitation, or 1/8192 by antigen coating plate- ELISA(ACP-ELISA).
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      Expression of the cp gene and Antiserum Preparation of Wisteria Vein Mosaic Virus

        Corresponding author: FAN Zai-feng,
      • 1. 1.Department of Plant Pathology, China Agricultural University, Beijing 100094, China
      • 2. Research Institute of Forest Ecology, Environment and Protection, China Academy of Forestry, Beijing 100091, China

      Abstract: The coat protein (CP) gene of the Beijing isolate of Wisteria vein mosaic virus (WVMV-BJ) was amplified by RT-PCR, and ligated to the expression vector pET22b(+). The recombinant plasmid pET-WVMVCP was transformed into E. coli BL21(DE3) and then induced by IPTG. It was shon that the CP gene was highly expressed by SDS-PAGE and Western blot analysis. The molecular weight of the recombinant protein was about 34.4kDa. Antiserum with high specificity was produced after the rabbit was immunized with purified recombinant protein, and the titer was determined to be 1/1024 by micro-precipitation, or 1/8192 by antigen coating plate- ELISA(ACP-ELISA).

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