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
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…
Citation impact
- FWCI
- 30.93
- Percentile
- 100%
- References
- 18
Authors
5- SKSwee Kee Wong
Harvard University, Brigham and Women's Hospital
- WLWenhui Li
Brigham and Women's Hospital, Harvard University
- MJMichael J. Moore
Harvard University, Brigham and Women's Hospital
- HCHyeryun Choe
Harvard University, Boston Children's Hospital
- MFMichael FarzanCorresponding
Brigham and Women's Hospital, Harvard University
Topics & 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)
- Good health and well-being