中国食品药品检定研究院Youchun Wang、Weijin Huang等研究人员，合作揭示了新冠病毒（SARS-CoV-2）突刺蛋白突变对病毒感染性和抗原性的影响。这一研究成果于2020年7月17日在线发表在《细胞》上。

据研究人员介绍，SARS-CoV-2的突刺蛋白已经发生突变，并高度糖基化。研究这些突变的生物学意义至关重要。

研究人员检测了80个变体和26个糖基化位点的修饰，从而对康复期患者中和的中和抗体和血清的感染性和反应性进行评估。D614G以及同时包含D614G和另一个氨基酸变化的几个变体更具感染性。大多数在受体结合结构域具有氨基酸变化的变体感染力较小，但包括A475V、L452R、V483A和F490L的变体对某些中和抗体产生抗性。此外，大多数糖基化缺失的感染性较小，而同时缺失N331和N343糖基化则大大降低了感染力，这表明了糖基化对于病毒感染性的重要性。值得注意的是，N234Q对中和抗体具有明显的抗性，而N165Q变得更加敏感。这些发现可能对疫苗和治疗性抗体的开发有价值。

附：英文原文

Title: The impact of mutations in SARS-CoV-2 spike on viral infectivity and antigenicity

Author: Qianqian Li, Jiajing Wu, Jianhui Nie, Li Zhang, Huan Hao, Shuo Liu, Chenyan Zhao, Qi Zhang, Huan Liu, Lingling Nie, Haiyang Qin, Meng Wang, Qiong Lu, Xiaoyu Li, Qiyu Sun, Junkai Liu, Linqi Zhang, Xuguang Li, Weijin Huang, Youchun Wang

Issue&Volume: 2020-07-17

Abstract: The spike protein of SARS-CoV-2 has been undergoing mutations and is highly glycosylated. It is critically important to investigate the biological significance of these mutations. Here we investigated 80 variants and 26 glycosylation site modifications for the infectivity and reactivity to a panel of neutralizing antibodies and sera from convalescent patients. D614G, along with several variants containing both D614G and another amino acid change, were significantly more infectious. Most variants with amino acid change at receptor binding domain were less infectious but variants including A475V, L452R, V483A and F490L became resistant to some neutralizing antibodies. Moreover, the majority of glycosylation deletions were less infectious whilst deletion of both N331 and N343 glycosylation drastically reduced infectivity, revealing the importance of glycosylation for viral infectivity. Interestingly, N234Q was markedly resistant to neutralizing antibodies, whereas N165Q became more sensitive. These findings could be of value in the development of vaccine and therapeutic antibodies.

DOI: 10.1016/j.cell.2020.07.012

Source: https://www.cell.com/cell/fulltext/S0092-8674(20)30877-1