Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 143, Issue 33, Pages 13205-13211Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.1c05435
Keywords
-
Categories
Funding
- National Science Foundation (U.S.) RAPID award [2030473]
- NIH [S10RR022341]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [2030473] Funding Source: National Science Foundation
Ask authors/readers for more resources
The fusion peptide of SARS-CoV-2 plays a crucial role in the fusion of viral and cell membranes, with its structure changes affecting the fusion process between the virus and the cell.
The receptor binding and proteolysis of Spike of SARS-CoV-2 release its S-2 subunit to rearrange and catalyze viral-cell fusion. This deploys the fusion peptide for insertion into the cell membranes targeted. We show that this fusion peptide transforms from intrinsic disorder in solution into a wedge-shaped structure inserted in bilayered micelles, according to chemical shifts, N-15 NMR relaxation, and NOEs. The globular fold of three helices contrasts the open, extended forms of this region observed in the electron density of compact prefusion states. In the hydrophobic, narrow end of the wedge, helices 1 and 2 contact the fatty acyl chains of phospholipids, according to NOEs and proximity to a nitroxide spin label deep in the membrane mimic. The polar end of the wedge may engage and displace lipid head groups and bind Ca2+ ions for membrane fusion. Polar helix 3 protrudes from the bilayer where it might be accessible to antibodies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available