» Articles » PMID: 36416453

Thermodynamic Analysis of the Interactions Between Human ACE2 and Spike RBD of Betacoronaviruses (SARS-CoV-1 and SARS-CoV-2)

Overview
Journal FEBS Open Bio
Specialty Biology
Date 2022 Nov 23
PMID 36416453
Authors
Affiliations
Soon will be listed here.
Abstract

There are many scientific reports on the interaction of the SARS-CoV-2 virus S protein (and its RBD) with the human ACE2 receptor protein. However, there are no reliable data on how this interaction differs from the interaction of the receptor binding domain of SARS-CoV-1 with ACE2, in terms of binding strength and changes in reaction enthalpy and entropy. Our studies have revealed these differences and the impact of zinc ions on this interaction. Intriguingly, the binding affinity of both RBDs (of SARS-CoV-1 and of SARS-CoV-2) to the ACE2 receptor protein is almost identical; however, there are some differences in the entropic and enthalpic contributions to these interactions.

Citing Articles

Cognitive dysfunctions in the course of SARS‑CoV‑2 virus infection, including NeuroCOVID, frontal syndrome and cytokine storm (Review).

Sadowski J, Klaudel T, Rombel-Bryzek A, Buldak R Biomed Rep. 2024; 21(1):103.

PMID: 38800038 PMC: 11117100. DOI: 10.3892/br.2024.1791.


Ghosts of the past: Elemental composition, biosynthesis reactions and thermodynamic properties of Zeta P.2, Eta B.1.525, Theta P.3, Kappa B.1.617.1, Iota B.1.526, Lambda C.37 and Mu B.1.621 variants of SARS-CoV-2.

Popovic M, Pantovic Pavlovic M, Pavlovic M Microb Risk Anal. 2023; 24:100263.

PMID: 37234934 PMC: 10199755. DOI: 10.1016/j.mran.2023.100263.


Never ending story? Evolution of SARS-CoV-2 monitored through Gibbs energies of biosynthesis and antigen-receptor binding of Omicron BQ.1, BQ.1.1, XBB and XBB.1 variants.

Popovic M Microb Risk Anal. 2023; 23:100250.

PMID: 36777740 PMC: 9896887. DOI: 10.1016/j.mran.2023.100250.

References
1.
Lan J, He X, Ren Y, Wang Z, Zhou H, Fan S . Structural insights into the SARS-CoV-2 Omicron RBD-ACE2 interaction. Cell Res. 2022; 32(6):593-595. PMC: 9007263. DOI: 10.1038/s41422-022-00644-8. View

2.
Grossoehme N, Spuches A, Wilcox D . Application of isothermal titration calorimetry in bioinorganic chemistry. J Biol Inorg Chem. 2010; 15(8):1183-91. DOI: 10.1007/s00775-010-0693-3. View

3.
Upadhyay V, Lucas A, Panja S, Miyauchi R, Mallela K . Receptor binding, immune escape, and protein stability direct the natural selection of SARS-CoV-2 variants. J Biol Chem. 2021; 297(4):101208. PMC: 8445900. DOI: 10.1016/j.jbc.2021.101208. View

4.
Laffeber C, de Koning K, Kanaar R, Lebbink J . Experimental Evidence for Enhanced Receptor Binding by Rapidly Spreading SARS-CoV-2 Variants. J Mol Biol. 2021; 433(15):167058. PMC: 8139174. DOI: 10.1016/j.jmb.2021.167058. View

5.
Shang J, Ye G, Shi K, Wan Y, Luo C, Aihara H . Structural basis of receptor recognition by SARS-CoV-2. Nature. 2020; 581(7807):221-224. PMC: 7328981. DOI: 10.1038/s41586-020-2179-y. View