Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Biochemistry, Durham, NC 27710, USA.
Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Biochemistry, Durham, NC 27710, USA; Duke University, Department of Surgery, Durham, NC 27710, USA.
Cell Rep. 2023 Dec 26;42(12):113444. doi: 10.1016/j.celrep.2023.113444. Epub 2023 Nov 18.
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern, first identified in November 2021, rapidly spread worldwide and diversified into several subvariants. The Omicron spike (S) protein accumulated an unprecedented number of sequence changes relative to previous variants. In this review, we discuss how Omicron S protein structural features modulate host cell receptor binding, virus entry, and immune evasion and highlight how these structural features differentiate Omicron from previous variants. We also examine how key structural properties track across the still-evolving Omicron subvariants and the importance of continuing surveillance of the S protein sequence evolution over time.
严重急性呼吸综合征冠状病毒 2（SARS-CoV-2）奥密克戎变体于 2021 年 11 月首次被发现，迅速在全球范围内传播，并分化为几个亚变体。奥密克戎刺突（S）蛋白相对于以前的变体积累了前所未有的大量序列变化。在这篇综述中，我们讨论了奥密克戎 S 蛋白结构特征如何调节宿主细胞受体结合、病毒进入和免疫逃逸，并强调了这些结构特征如何将奥密克戎与以前的变体区分开来。我们还研究了关键结构特性如何在不断演变的奥密克戎亚变体中跟踪，并强调了随着时间的推移继续监测 S 蛋白序列进化的重要性。
