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Volume 22 Issue 1
February 2007

    Yi ZHANG, Wei WANG, Jin-rong GAO, Li YE, Xiao-nan FANG, Ying-chun ZENG, Zheng-hui WU, Ying-long SHE and Lin-bai YE. The Functional Motif of SARS-CoV S Protein Involved in the Interaction with ACE2[J]. Virologica Sinica, 2007, 22(1): 1-7.
    Citation: Yi ZHANG, Wei WANG, Jin-rong GAO, Li YE, Xiao-nan FANG, Ying-chun ZENG, Zheng-hui WU, Ying-long SHE, Lin-bai YE. The Functional Motif of SARS-CoV S Protein Involved in the Interaction with ACE2 .VIROLOGICA SINICA, 2007, 22(1) : 1-7.
    shu

    SARS-CoV S蛋白与受体ACE2结合的功能区域研究

    • 武汉大学病毒学国家重点实验室，湖北省 430072

    • 收稿日期： 2006-07-17
      录用日期： 2006-07-31
    • 摘要：SARS冠状病毒是一种新发传染病严重急性呼吸系统综合征的病原体。病毒的S蛋白通过与靶细胞表面的特异受体血管紧张素转换酶2（ACE2）结合，在病毒的吸附和侵入过程中起到了重要的作用。为了确定S蛋白与ACE2结合的功能区域，我们在大肠杆菌中表达了7个从N端截短或从C端截短的S蛋白，并用Ni柱纯化。将各个截短的蛋白包被在96孔ELISA板上，与ACE2作用，再用ACE2蛋白的兔抗血清作为一抗检测截短的S蛋白与ACE2的结合情况。ELISA结果显示，S蛋白中编码氨基酸388～496的序列是受体结合的功能区域；用这段截短的S蛋白免疫家兔得到的抗血清能够有效地阻断S蛋白与ACE2的结合。该结果为S蛋白发展为SARS疫苗提供了实验依据。

    The Functional Motif of SARS-CoV S Protein Involved in the Interaction with ACE2

    • State Key Laboratory of Virology,College of Life Science,Wuhan University,Wuhan 430072,China

    • Corresponding author: Lin-bai YE, linbaiye@whu.edu.cn
    • Received Date: 17 July 2006
      Accepted Date: 31 July 2006
    • SARS-CoV is a newly discovery pathogen causing severe acute respiratory syndrome, S protein play an important rule in the adsorption and penetration of SARS-CoV into the cell by interaction with ACE2 receptor. To determinant the functional motif of S protein involved in the interaction with ACE2, seven truncated S proteins deleted from N or C terminal were obtained by E.Coli expression system and purified by column chromatography to homogeneity. Each truncated S protein was fixed on to the well of ELISA plate and interacted with ACE2 protein. The adsorption were quantified by ELISA, the results demonstrated that the amino acid from 388 to 496 of S protein was responsible for interaction with ACE2 receptor, and the interaction can be disrupted completely by the antibody specific against amino acid 388 to 496 of S protein. The deletion besides this domain did not show significant effects on the interaction with ACE2, suggested that S protein of SARS-CoV could be developed as vaccines to prevent the spread of SARS-CoV.
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      The Functional Motif of SARS-CoV S Protein Involved in the Interaction with ACE2

        Corresponding author: Lin-bai YE, linbaiye@whu.edu.cn
      • State Key Laboratory of Virology,College of Life Science,Wuhan University,Wuhan 430072,China
      • Received Date: 17 July 2006
      • Accepted Date: 31 July 2006

      Abstract: SARS-CoV is a newly discovery pathogen causing severe acute respiratory syndrome, S protein play an important rule in the adsorption and penetration of SARS-CoV into the cell by interaction with ACE2 receptor. To determinant the functional motif of S protein involved in the interaction with ACE2, seven truncated S proteins deleted from N or C terminal were obtained by E.Coli expression system and purified by column chromatography to homogeneity. Each truncated S protein was fixed on to the well of ELISA plate and interacted with ACE2 protein. The adsorption were quantified by ELISA, the results demonstrated that the amino acid from 388 to 496 of S protein was responsible for interaction with ACE2 receptor, and the interaction can be disrupted completely by the antibody specific against amino acid 388 to 496 of S protein. The deletion besides this domain did not show significant effects on the interaction with ACE2, suggested that S protein of SARS-CoV could be developed as vaccines to prevent the spread of SARS-CoV.

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