Potent Antibody Against SARS-CoV-2
10/27/2020
A potent neutralizing antibody blocks the SARS-CoV-2 spike protein. X-ray macromolecular crystallography reveals how the CV30 antibody (blue and aqua) overlaps the binding domain of the SARS-CoV-2 spike protein (pink) on the ACE2 receptor (gold) on the surface of human cells, thereby preventing infection. [Reprinted under a Creative Commons CC BY license (https://creativecommons.org/licenses/), from Hurlburt, N.K., Seydoux, E., Wan, YH. et al. "Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation." Nat Commun 11, 5413 (2020). DOI: 10.1038/s41467-020-19231-9]
Researchers employed high-brightness X-rays from the U.S. Department of Energy’s Advanced Photon Source (APS) to show how a monoclonal antibody from a COVID-19 survivor acts as a potent neutralizer of SARS-CoV-2.
The antibody, CV30, binds to the receptor binding domain on the SARS-CoV-2 spike protein and induces it to shed its S1 subunit. Without the S1 subunit, which normally facilitates binding of the spike protein to the ACE2 receptor on human cells, the virus can no longer infect cells. CV30 also binds to a region of the ACE2 receptor that overlaps with the binding region of the spike protein, thereby blocking its access to the cell.
CV30 may prove useful in the prevention or treatment of COVID-19. To find out, the antibody, along with other candidate proteins, needs to be tested pre-clinically and then in human trials.
Related Links
- BER Resource: Structural Biology Center
- Feature Story: Mapping the Structure of a Potent Antibody against the Coronavirus
References
Hurlburt, N.K., Seydoux, E., Wan, YH. et al. “Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation.” Nat Commun 11, 5413 (2020). [DOI: 10.1038/s41467-020-19231-9]