Unité de Virologie Structurale, CNRS UMR 3569, Institut Pasteur, 28 rue du Dr Roux, 75015 Paris, France.
C R Biol. 2021 Jun 21;344(1):77-110. doi: 10.5802/crbiol.53.
This review covers the main features of the severe acquired respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein, its interaction with the main entry receptor, the human angiotensin converting enzyme 2 (ACE2), and the subsequent membrane fusion step. The focus is on the structural organization of these proteins and mechanistic aspects of their interactions that lead to cytoplasmic release of the viral genome. The most potently neutralizing antibodies against SARS-CoV-2 were shown to interfere with the spike/ACE2 interaction. I thus also review the location and the potential impact of mutations in the spike protein observed in the variants of concern that emerged concomitantly with acquired immunity in the population after one year of virus circulation. Understanding how these interactions affect the spike/ACE2 interactions and the subsequent spike-protein-induced membrane fusion reaction is important to stay one step ahead of the virus evolution and develop efficient countermeasures.
本篇综述涵盖了严重急性呼吸综合征冠状病毒 2（SARS-CoV-2）刺突蛋白的主要特征，及其与主要进入受体人血管紧张素转换酶 2（ACE2）的相互作用，以及随后的膜融合步骤。重点介绍了这些蛋白的结构组织，以及导致病毒基因组细胞质释放的相互作用的机制方面。已证明针对 SARS-CoV-2 的最有效中和抗体可干扰刺突/ACE2 相互作用。因此，我还综述了在病毒传播一年后，人群获得性免疫的同时出现的关注变种中观察到的刺突蛋白的位置和突变的潜在影响。了解这些相互作用如何影响刺突/ACE2 相互作用以及随后的刺突蛋白诱导的膜融合反应，对于紧跟病毒进化并开发有效的对策非常重要。
