Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.
Delhi Pharmaceutical Sciences and Research University, New Delhi, India.
J Autoimmun. 2022 Jan;126:102779. doi: 10.1016/j.jaut.2021.102779. Epub 2021 Dec 13.
Severe Acute Respiratory Coronavirus (SARS-CoV-2) has been emerging in the form of different variants since its first emergence in early December 2019. A new Variant of Concern (VOC) named the Omicron variant (B.1.1.529) was reported recently. This variant has a large number of mutations in the S protein. To date, there exists a limited information on the Omicron variant. Here we present the analyses of mutation distribution, the evolutionary relationship of Omicron with previous variants, and probable structural impact of mutations on antibody binding. Our analyses show the presence of 46 high prevalence mutations specific to Omicron. Twenty-three of these are localized within the spike (S) protein and the rest localized to the other 3 structural proteins of the virus, the envelope (E), membrane (M), and nucleocapsid (N). Phylogenetic analysis showed that the Omicron is closely related to the Gamma (P.1) variant. The structural analyses showed that several mutations are localized to the region of the S protein that is the major target of antibodies, suggesting that the mutations in the Omicron variant may affect the binding affinities of antibodies to the S protein.
自 2019 年 12 月初首次出现以来，严重急性呼吸系统冠状病毒（SARS-CoV-2）已经以不同变体的形式出现。最近报告了一种名为奥密克戎变体（B.1.1.529）的新关注变体（VOC）。该变体在 S 蛋白中有大量突变。迄今为止，关于奥密克戎变体的信息有限。在这里，我们展示了突变分布的分析、奥密克戎与以前变体的进化关系，以及突变对抗体结合的可能结构影响。我们的分析表明，奥密克戎存在 46 种特异性高的高频突变。其中 23 种位于刺突（S）蛋白内，其余分布在病毒的其他 3 种结构蛋白，包膜（E）、膜（M）和核衣壳（N）。系统发育分析表明，奥密克戎与伽马（P.1）变体密切相关。结构分析表明，几个突变位于 S 蛋白的抗体主要靶标区域，这表明奥密克戎变体中的突变可能影响抗体与 S 蛋白的结合亲和力。
