๐ A 193-Amino Acid Fragment of the SARS Coronavirus S Protein Efficiently Binds Angiotensin-converting Enzyme 2
The coronavirus spike (S) protein mediates infection of receptor-expressing host cells and is a critical target for antiviral neutralizing antibodies. Angiotensin-converting enzyme 2 (ACE2) is a functional receptor for the coronavirus (severe acute respiratory syndrome (SARS)-CoV) that causes SARS. Here we demonstrate that a 193-amino acid fragment of the S protein (residues 318-510) bound ACE2 more efficiently than did the full S1 domain (residues 12-672). Smaller S protein fragments, expressing residues 327-510 or 318-490, did not detectably bind ACE2. A point mutation at aspartic acid 454 abolished association of the full S1 domain and of the 193-residue fragment with ACE2. The 193-residue fragment blocked S protein-mediated infection with an IC50 of less than 10 nM, whereas the IC 50 of the S1 domain was โผ50 ฮผM. These data identify an independently folded receptor-binding domain of the SARS-CoV S protein.
keywords
๐ severe acute (1373)
๐ neutralizing antibodies (122)
๐ receptor-binding domain (99)
๐ host cell (262)
๐ amino acid (454)
๐ converting enzyme (162)
๐ respiratory syndrome (2004)
๐ acute respiratory (1734)
author
๐ค Wong, Swee Kee
๐ค Li, Wenhui
๐ค Moore, Michael J.
๐ค Choe, Hyeryun
๐ค Farzan, Michael
year
โฐ 2004
issn
๐ 00219258
volume
279
number
5
page
3197-3201
citedbycount
303
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