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

SARS-CoV 是一最新引起严重尖锐呼吸问题的发现病原体。在这病原体的 S 蛋白质由和 ACE2 受体的相互作用在 SARS-CoV 的吸附和穿入玩一条重要规则进宿主细胞，这被建立了。到 S 蛋白质的功能的主题涉及和 ACE2 的相互作用的决定因素，从 N 或 C 终端删除的七截断的 S 蛋白质被一个 E.coli 表达式系统获得并且由列层析净化了到同质。每截断的 S 蛋白质被修理在上到 ELISA 的井，板和一个相互作用与 ACE2 蛋白质被开始。吸附被 ELISA 确定，并且结果显示从 388 ～ 496 S 蛋白质的氨基酸为和 ACE2 受体的相互作用负责，并且相互作用能被对这些氨基酸特定的抗体完全破坏。邻近这个领域的删除不看起来在和 ACE2 的相互作用上有重要影响，建议 SARS-CoV 的 S 蛋白质能作为阻止 SARS-CoV 的传播的一支疫苗被开发。关键词 SARS-CoV - S 蛋白质 - ACE2 - 相互作用 CLC 数字

SARS-CoV is a newly discovery pathogen causing severe acute respiratory problems. It has been established that the S protein in this pathogen plays an important rule in the adsorption and penetration of SARS-CoV into the host cell by interaction with the ACE2 receptor. To determinant which functional motif of the S protein was involved in the interaction with ACE2, seven truncated S proteins deleted from the N or C terminal were obtained by an E.coli expression system and purified by column chromatography to homogeneity. Each trtmcated S protein was fixed on to the well of an ELISA plate and an interaction was initiated with the ACE2 protein. The adsorption were quantified by ELISA, and the results indicated that amino acids from 388 to 496 of the S protein was responsible for the interaction with the ACE2 receptor, and the interaction could be completely disrupted by an antibody specific to these amino acids. Deletions adjacent to this domain did not appear to have a significant impact on the interaction with ACE2, suggesting that the S protein of SARS-CoV could be developed as a vaccine to prevent the spread of SARS-CoV.