Journal
NATURE COMMUNICATIONS
Volume 12, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-021-27325-1
Keywords
-
Categories
Funding
- Universite catholique de Louvain
- Foundation Louvain
- Fonds National de la Recherche Scientifique (FRS-FNRS)
- European Research Council under the European Union's Horizon 2020 research and innovation program [758224]
- FNRS-Welbio [CR-2019S-01]
- National Science Center, Poland [2017/26/D/NZ1/00466]
- Foundation for Polish Science [MAB PLUS/2019/11]
- PL-GRID infrastructure
Ask authors/readers for more resources
The study utilized atomic force microscopy and molecular dynamics to investigate the impact of SARS-CoV-2 variants on the kinetic, thermodynamic, and structural properties of RBD-ACE2 complex formation. The research found a significant increase in complex stability for several variants of concern.
Despite an unprecedented global gain in knowledge since the emergence of SARS-CoV-2, almost all mechanistic knowledge related to the molecular and cellular details of viral replication, pathology and virulence has been generated using early prototypic isolates of SARS-CoV-2. Here, using atomic force microscopy and molecular dynamics, we investigated how these mutations quantitatively affected the kinetic, thermodynamic and structural properties of RBD-ACE2 complex formation. We observed for several variants of concern a significant increase in the RBD-ACE2 complex stability. While the N501Y and E484Q mutations are particularly important for the greater stability, the N501Y mutation is unlikely to significantly affect antibody neutralization. This work provides unprecedented atomistic detail on the binding of SARS-CoV-2 variants and provides insight into the impact of viral mutations on infection-induced immunity. Here, the authors combine single-molecule atomic force spectroscopy measurements and molecular dynamics simulations to investigate the binding of spike proteins from four SARS-CoV-2 variants of concern (VoC) to the human ACE2 receptor. They observe an increase in the RBD-ACE2 complex stability for several of the VoCs and derive how the mutations affect the kinetic, thermodynamic and structural properties of complex formation.
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