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Molecular insights into receptor binding energetics and neutralization of SARS-CoV-2 variants

Medicine and Health

Molecular insights into receptor binding energetics and neutralization of SARS-CoV-2 variants

M. Koehler, A. Ray, et al.

This cutting-edge study reveals how SARS-CoV-2 mutations, particularly N501Y and E484Q, modify receptor binding and antibody neutralization. By employing atomic force microscopy and molecular dynamics, the authors delve into the stability of the RBD-ACE2 complex, offering crucial insights into the variant's implications on immunity. This research was conducted by Melanie Koehler, Ankita Ray, Rodrigo A. Moreira, Blinera Juniku, Adolfo B. Poma, and David Alsteens.

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Abstract
This study investigates the impact of SARS-CoV-2 mutations on receptor binding and antibody neutralization. Using atomic force microscopy and molecular dynamics, the researchers found increased stability in the RBD-ACE2 complex for several variants of concern, particularly due to N501Y and E484Q mutations. While N501Y increased stability, it is unlikely to significantly affect antibody neutralization. The work provides detailed insights into the binding of SARS-CoV-2 variants and their impact on immunity.
Publisher
Nature Communications
Published On
Nov 30, 2021
Authors
Melanie Koehler, Ankita Ray, Rodrigo A. Moreira, Blinera Juniku, Adolfo B. Poma, David Alsteens
Tags
SARS-CoV-2
mutations
receptor binding
antibody neutralization
RBD-ACE2 complex
N501Y
E484Q

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