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The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

A 193-Amino Acid Fragment of the SARS Coronavirus S Protein Efficiently Binds Angiotensin-converting Enzyme 2

Open access
Wong, Swee Kee, Li, Wenhui, Moore, Michael J., Choe, Hyeryun, Farzan, Michael·2004·Journal of Biological Chemistry

Abstract

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 IC(50) of less than 10 nm, whereas the IC(50) of the S1 domain was approximately 50 nm. These data identify an independently folded receptor-binding domain of the SARS-CoV S protein.

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Crossref · 10.1074/jbc.c300520200

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Metadata

Authors
Wong, S. K., Li, W., Moore, M. J., Choe, H., & Farzan, M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2004-01
Volume
279
Issue
5
Pages
3197-3201
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2146476111
Cited by
694
References
4
FWCI
38.97
Type
journal article
Language
en
Open access
hybrid

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