ABSTRACT
The Covid19 pandemic caused by SARS-CoV-2 has created panic around most of the nations. Statistical and epidemiological data from its predecessor SARS-CoV-1 imply temperature sensitivity of the virus. However, we still lack molecular level understanding of the same. Spike protein is the outermost structural protein of the virus which interacts with the human receptor ACE2 and enters the respiratory system. It is also one of largest proteins which have primary exposure to external environmental conditions. In this study, we performed an all atom molecular dynamics simulation to study the effect of temperature on the structure of the Spike protein. After 200ns of simulation at different temperatures, we came across some interesting phenomena exhibited by the protein. We found that the receptor binding motif of the virus is sensitive to the surrounding temperature and behaves differently at altered temperatures. Bioinformatics and structural studies hinted that the N-terminal Domain of the Spike protein is capable of binding to receptors and should not be overlooked. We also observed that at higher temperatures, the structure of the Spike protein is in a more confined conformation. The study would not only prove very beneficial for understanding the fundamental nature of the virus, but will also support in the development of vaccines and therapeutics.
Competing Interest Statement
The authors have declared no competing interest.
Abbreviations
- RBD
- Receptor Binding Domain;
- NTD
- N-Terminal Domain,
- RBM
- Receptor Binding Motif