State Key Laboratory of Virology, College of Life Science, Wuhan University, Wuhan, Hubei Province 430072, PR China
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.