Unknown

Dataset Information

0

Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor.


ABSTRACT: Study of the interactions established between the viral glycoproteins and their host receptors is of critical importance for a better understanding of virus entry into cells. The novel coronavirus SARS-CoV-2 entry into host cells is mediated by its spike glycoprotein (S-glycoprotein), and the angiotensin-converting enzyme 2 (ACE2) has been identified as a cellular receptor. Here, we use atomic force microscopy to investigate the mechanisms by which the S-glycoprotein binds to the ACE2 receptor. We demonstrate, both on model surfaces and on living cells, that the receptor binding domain (RBD) serves as the binding interface within the S-glycoprotein with the ACE2 receptor and extract the kinetic and thermodynamic properties of this binding pocket. Altogether, these results provide a picture of the established interaction on living cells. Finally, we test several binding inhibitor peptides targeting the virus early attachment stages, offering new perspectives in the treatment of the SARS-CoV-2 infection.

SUBMITTER: Yang J 

PROVIDER: S-EPMC7486399 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC8239528 | biostudies-literature
| EMPIAR-11181 | biostudies-other
| S-BSST649 | biostudies-other
| S-EPMC8562373 | biostudies-literature
| EMPIAR-11180 | biostudies-other
| EMPIAR-11179 | biostudies-other
| S-EPMC8263772 | biostudies-literature
| EMPIAR-11176 | biostudies-other
| EMPIAR-11177 | biostudies-other
| S-EPMC7544872 | biostudies-literature