| Products/Services Used | Details | Operation |
|---|---|---|
| Recombinant Proteins | The protein was cleaved using bovine enterokinase (GenScript) leaving a FLAG-tag at the C-terminus of the RBD. Enzyme and FC-portion was removed on HIS-Pur Ni-NTA resin (Thermo Fisher Scientific) and Protein G sepharose (GE Healthcare) respectively, and the RBD was purified by size-exclusion chromatography on a Superdex 200 in 50 mM Tris pH 8, 200 mM NaCl. | Get A Quote |
We report the isolation and characterization of an alpaca-derived, single domain antibody fragment (nanobody) that specifically targets the receptor binding domain (RBD) of the SARS-CoV-2 spike glycoprotein (spike) and potently neutralizes the virus. A cryo-electron microscopy structure of the bound complex at 2.9 Å resolution reveals that the nanobody (Ty1) binds to an epitope on the RBD accessible in both the ‘up’ and ‘down’ conformations and that Ty1 sterically hinders RBD-ACE2 binding. Mechanistic characterization confirms that Ty1 directly interferes with host cell receptor binding. This 12.8 kDa nanobody binds the SARS-CoV-2 spike with high specificity and affinity, and can be produced in high qu... More
