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Virologica Sinica

, Volume 22, Issue 1, pp 1–7 | Cite as

The functional motif of SARS-CoV S protein involved in the interaction with ACE2

  • Yi Zhang
  • Wei Wang
  • Jin-rong Gao
  • Li Ye
  • Xiao-nan Fang
  • Ying-chun Zeng
  • Zheng-hui Wu
  • Ying-long She
  • Lin-bai YeEmail author
Article

Abstract

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 truncated 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.

Key words

SARS-CoV S protein ACE2 Interaction 

CLC number

R373 

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Copyright information

© Wuhan Institute of Virology, CAS and Springer Berlin Heidelberg 2007

Authors and Affiliations

  • Yi Zhang
    • 1
  • Wei Wang
    • 1
  • Jin-rong Gao
    • 1
  • Li Ye
    • 1
  • Xiao-nan Fang
    • 1
  • Ying-chun Zeng
    • 1
  • Zheng-hui Wu
    • 1
  • Ying-long She
    • 1
  • Lin-bai Ye
    • 1
    Email author
  1. 1.State Key Laboratory of Virology, College of Life ScienceWuhan UniversityWuhanChina

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