AI Article Synopsis
- The spike glycoprotein of SARS-CoV-2 binds to human ACE 2, enabling infection, and a camelid-derived antibody fragment called saRBD-1 blocks this interaction.
- Researchers developed multivalent nanobody constructs that can inhibit the virus at very low concentrations and remain effective against various COVID-19 variants.
- saRBD-1 is stable under different conditions, suggesting it could be a promising therapeutic option for treating COVID-19.
Article Abstract
The spike glycoprotein of SARS-CoV-2 engages with human ACE 2 to facilitate infection. Here, we describe an alpaca-derived heavy chain antibody fragment (VHH), saRBD-1, that disrupts this interaction by competitively binding to the spike protein receptor-binding domain. We further generated an engineered bivalent nanobody construct engineered by a flexible linker and a dimeric Fc conjugated nanobody construct. Both multivalent nanobodies blocked infection at picomolar concentrations and demonstrated no loss of potency against emerging variants of concern including Alpha (B.1.1.7), Beta (B.1.351), Gamma (P.1), Epsilon (B.1.427/429), and Delta (B.1.617.2). saRBD-1 tolerates elevated temperature, freeze-drying, and nebulization, making it an excellent candidate for further development into a therapeutic approach for COVID-19.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8863326 | PMC |
| http://dx.doi.org/10.1016/j.isci.2022.103960 | DOI Listing |
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