Molecular dynamics simulations show structural insights into the N-terminal domain mutations of the spike protein in the Omicron (B.۱.۱.۵۲۹) variant of SARS-CoV-۲.

Since the outbreak of SARS-CoV-۲, many variants with different mutations in the structure of the virus havespread rapidly global. One of the new Variant of Concern (VOC) with high infectivity is Omicron(B.۱.۱.۵۲۹), which was first reported in November ۲۰۲۱ from South Africa. Since Spike glycoprotein is amajor driving force in virus infectivity, it is important to study the effects of mutations in understanding thestructural changes of the new variants. Careful evaluation of the spike glycoprotein sequence in omicronreveals numerous point and deletion mutations as well as an additional insertion. The N-terminal domain(NTD) of spike glycoprotein is an effective factor in cell surface adhesion and plays an important role in thevirus escaping the immune system. Therefore, the study of the effect of mutations through moleculardynamics simulations shows changes in the structure of NTD and its stability. these analyzes, helpsresearchers to achieve a relative understanding of the high infectivity and antigenicity of the new variant inthe compared to the Wuhan-Hu-۱ type.

کلیدواژه ها:

SARS-CoV-۲ ، Omicron (B.۱.۱.۵۲۹) ، Spike glycoprotein ، N-terminal domain (NTD) ، Molecular dynamics simulations