articleJournal of Biological ChemistryJan 1, 2004HYBRID OA

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

Harvard University · Brigham and Women's Hospital · +1 more institution

PubMed
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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…

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727
total citations
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30.93
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100%
References
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Authors

5

Topics & keywords

Keywords
  • Angiotensin-converting enzyme 2
  • Fragment (logic)
  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
  • Coronavirus
  • Enzyme
  • Virology
  • Chemistry
  • Coronavirus disease 2019 (COVID-19)
UN Sustainable Development Goals
  • Good health and well-being
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