The Molecular Basis of the Effect of Temperature on the Structure and Function of SARS-CoV-2 Spike Protein

Faez Iqbal Khan; Kevin A Lobb; Dakun Lai

doi:10.3389/fmolb.2022.794960

The Molecular Basis of the Effect of Temperature on the Structure and Function of SARS-CoV-2 Spike Protein

Front Mol Biosci. 2022 Mar 25:9:794960. doi: 10.3389/fmolb.2022.794960. eCollection 2022.

Authors

Faez Iqbal Khan^{1

2}, Kevin A Lobb³, Dakun Lai²

Affiliations

¹ Department of Biological Sciences, School of Science, Xi'an Jiaotong-Liverpool University, Suzhou, Jiangsu, China.
² School of Electronic Science and Engineering, University of Electronic Science and Technology of China, Chengdu, China.
³ Department of Chemistry, Rhodes University, Grahamstown, South Africa.

Abstract

The remarkable rise of the current COVID-19 pandemic to every part of the globe has raised key concerns for the current public healthcare system. The spike (S) protein of SARS-CoV-2 shows an important part in the cell membrane fusion and receptor recognition. It is a key target for vaccine production. Several researchers studied the nature of this protein under various environmental conditions. In this work, we applied molecular modeling and extensive molecular dynamics simulation approaches at 0°C (273.15 K), 20°C (293.15 K), 40°C (313.15 K), and 60°C (333.15 K) to study the detailed conformational alterations in the SARS-CoV-2 S protein. Our aim is to understand the influence of temperatures on the structure, function, and dynamics of the S protein of SARS-CoV-2. The structural deviations, and atomic and residual fluctuations were least at low (0°C) and high (60°C) temperature. Even the internal residues of the SARS-CoV-2 S protein are not accessible to solvent at high temperature. Furthermore, there was no unfolding of SARS-CoV-2 spike S reported at higher temperature. The most stable conformations of the SARS-CoV-2 S protein were reported at 20°C, but the free energy minimum region of the SARS-CoV-2 S protein was sharper at 40°C than other temperatures. Our findings revealed that higher temperatures have little or no influence on the stability and folding of the SARS-CoV-2 S protein.

Keywords: COVID-19; Gibbs free energy; MD simulations; SARS-CoV-2; spike protein.