Omicron,另一种SARS-CoV-2变种,已被记录并报告为VoC。它已经在30多个国家/地区传播,并且是一种高度突变的变体。我们试图通过与先前表征的VoC进行比较来理解突变在所研究的变体中的作用。我们使用生物信息学工具和统计软件绘制了OmicronS-糖蛋白二级和三级结构的突变图,并开发了不同的模型。此外,我们分析了S-糖蛋白抗体结合区的不同突变对所研究抗体结合亲和力的影响.本研究选择了Omicron(D614G,E484A,N501Y,Q493K,K417N,S477N,Y505HG496S),其中七个位于RBD地区。我们还对这些突变的ΔΔG评分进行了比较分析,以了解所研究突变的稳定或不稳定特性。分析结果表明,D614G,Q493K,和S477N突变是稳定的突变,ΔΔG评分为0.351kcal/mol,0.470kcal/mol,和0.628千卡/摩尔,分别,根据DynaMut的估计。而其他突变(E484A,N501Y,K417N,Y505H,G496S)显示不稳定结果。D614G,E484A,N501Y,K417N,Y505H,G496S突变增加了S-糖蛋白与ACE2受体相互作用的分子灵活性,增加变种的传染性。我们的研究将有助于SARS-CoV-2变种的研究,Omicron,通过提供有关这八个重要突变的突变模式和令人兴奋的特性的信息,例如抗体逃逸和感染性商数(稳定或去稳定;S-糖蛋白与人ACE2受体相互作用的分子灵活性增加或降低)。
Omicron, another SARS-CoV-2 variant, has been recorded and reported as a VoC. It has already spread across >30 countries and is a highly mutated variant. We tried to understand the role of mutations in the investigated variants by comparison with previous characterized VoC. We have mapped the mutations in Omicron S-glycoprotein\'s secondary and tertiary structure landscape using bioinformatics tools and statistical software and developed different models. In addition, we analyzed the effect of diverse mutations in antibody binding regions of the S-glycoprotein on the binding affinity of the investigated antibodies. This study has chosen eight significant mutations in Omicron (D614G, E484A, N501Y, Q493K, K417N, S477N, Y505H G496S), and seven of them are located in the RBD region. We also performed a comparative analysis of the ΔΔG score of these mutations to understand the stabilizing or destabilizing properties of the investigated mutations. The analysis outcome shows that D614G, Q493K, and S477N mutations are stable mutations with ΔΔG scores of 0.351 kcal/mol, 0.470 kcal/mol, and 0.628 kcal/mol, respectively, according to DynaMut estimations. While other mutations (E484A, N501Y, K417N, Y505H, G496S) showed destabilizing results. The D614G, E484A, N501Y, K417N, Y505H, and G496S mutations increased the molecular flexibility of S-glycoprotein to interact with the ACE2 receptor, increasing the variant\'s infectivity. Our study will contribute to research on the SARS-CoV-2 variant, Omicron, by providing information on the mutational pattern and exciting properties of these eight significant mutations, such as antibody escape and infectivity quotient (stabilizing or destabilizing; increased or decreased molecular flexibility of S-glycoprotein to interact with the human ACE2 receptor).