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.
SARS-CoV S protein ACE2 Interaction
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He Y, Zhou Y, Siddiqui P,et al. 2004. Inactivated SARS-CoV vaccine elicits high titers of spike protein specific antibodies that block receptor binding and virus entry[J]. Biochem Biophys Res Commun, 325(2): 445–452.PubMedCrossRefGoogle Scholar
Ho T Y, Wu S L, Cheng S E,et al. 2004. Antigenicity and receptor-binding ability of recombinant SARS coronavirus spike protein[J]. Biochem Biophys Res Commun, 313(4): 938–947.PubMedCrossRefGoogle Scholar
Hua R, Zhou Y, Wang Y,et al. 2004. Identification of two antigenic epitopes on SARS-CoV spike protein[J]. Biochem Biophys Res Commun, 319(3): 929–935.PubMedCrossRefGoogle Scholar
Li W, Moore M J, Vasilieva N,et al. 2003. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus[J]. Nature, 426(6965): 450–454.PubMedCrossRefGoogle Scholar
Li W, Greenough T C, Moore M J,et al. 2004. Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2[J]. J Virol, 78(20): 11429–11433.PubMedCrossRefGoogle Scholar
Li W, Zhang C, Sui J,et al. 2005. Receptor and viral determinants of SARS coronavirus adaptation to human ACE2[J]. Embo J, 24(8): 1634–1643.PubMedCrossRefGoogle Scholar
Marra M A, Jones S J, Astell C R,et al. 2003. The Genome sequence of the SARS-associated coronavirus[J]. Science, 300(5624): 1399–1404.PubMedCrossRefGoogle Scholar
Peiris J S, Yuen K Y, Osterhaus A D,et al. 2003. The severe acute respiratory syndrome [J]. N Engl J Med, 349(25): 2431–2441.PubMedCrossRefGoogle Scholar
Prabakaran P, Xiao X, Dimitrov D S,et al. 2004. A model Pf the ACE2 structure and function as a SARS-CoV-receptor[J]. Biochem Biophys Res Commun, 314(1): 235–241.PubMedCrossRefGoogle Scholar
Rota P A, Oberste M S, Monroe S S,et al. 2003. Characteri-zation of a novel coronavirus associated with severe acute respiratory syndrome[J]. Science, 300(5624): 1394–1399.PubMedCrossRefGoogle Scholar
Siddell S G. 1995. The coronaviridae[M]. New York: Plenum Press.Google Scholar
Wang P, Chen J, Zheng A,et al. 2004. Expression cloning of functional receptor used by SARS coronavirus[J]. Biochem Biophys Res Commun, 315(2): 439–444.PubMedCrossRefGoogle Scholar