An engineered decoy receptor for SARS-CoV-2 broadly binds protein S sequence variants
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Abstract
An engineered decoy receptor tightly binds S from diverse SARS-related coronaviruses with limited potential for viral escape.
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The B.1.1.7, B.1.351, and P.1 lineages all harbor a N501Y mutation in the RBD, which increases the affinity for the ACE2 receptor, and a D614G mutation, which increases virion spike density, infectivity, and transmissibility.
“The B.1.1.7, B.1.351, and P.1 lineages all harbor a N501Y mutation in the RBD, which increases the affinity for the ACE2 receptor (57, 58), and a D614G mutation, which increases virion spike density, infectivity, and transmissibility (59, 60).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [57]
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- Authors
- Chan, K. K., Tan, T. J. C., Narayanan, K. K., & Procko, E.
- Affiliations
- Orthogonal Biologics, Champaign, IL 61821, USA.
- University of Illinois Urbana-Champaign (US)
- Corresponding author
- Procko, Erik
- Venue
- Science Advances
- Published
- 2021-02-19
- Volume
- 7
- Issue
- 8
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC7888922
- OpenAlex
- W3132966328
- Cited by
- 152
- References
- 51
- Citations by year
- 2026: 12 · 2025: 11 · 2024: 16 · 2023: 23 · 2022: 43 · 2021: 46 · 2020: 1
- FWCI
- 10.14
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Science Advances (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI129719)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 detection and testing
- Keywords
- SARS-CoV-2, ACE2, receptor binding domain, saturation mutagenesis, in vitro selection
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