1st International and 10th National Iranian Conference on Bioinformatics
Home Accepted Papers
Molecular dynamics simulations show structural insights into the N-terminal domain mutations of the spike protein in the Omicron (B.1.1.529) variant of SARS-CoV-2.
Paper ID : 1178-ICB10
Authors:
Fatemeh Bayani, Negin Safaei Hashkavaei, Yahya Sefidbakht *
مرکز تحقیقات پروتئین، دانشگاه شهید بهشتی، تهران، ایران.
Abstract:
Since the outbreak of SARS-CoV-2, many variants with different mutations in the structure of the virus have spread rapidly global. One of the new Variant of Concern (VOC) with high infectivity is Omicron (B.1.1.529), which was first reported in November 2021 from South Africa. Since Spike glycoprotein is a major driving force in virus infectivity, it is important to study the effects of mutations in understanding the structural changes of the new variants. Careful evaluation of the spike glycoprotein sequence in omicron reveals 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 the virus escaping the immune system [1]. Therefore, the study of the effect of mutations through molecular dynamics simulations shows changes in the structure of NTD and its stability. these analyzes, helps researchers to achieve a relative understanding of the high infectivity and antigenicity of the new variant in the compared to the Wuhan-Hu-1 type.
Keywords:
SARS-CoV-2; Omicron (B.1.1.529); Spike glycoprotein; N-terminal domain (NTD); Molecular dynamics simulations.
Status : Paper Accepted (Oral Presentation)