2020年7月17日，中国食品药品检定研究院王佑春及黄维金作为共同通讯作者在国际顶尖杂志Cell 在线发表题为“The impact of mutations in SARS-CoV-2 spike on viral infectivity and antigenicity”的研究论文，该研究观察了80个突变和26个糖基化位点的修饰，对康复期患者的中和抗体和血清的感染性和反应性。
HighlightsOver 100 mutations were selected for analyses on their infectivity and antigenicity The dominant D614G itself and combined with other mutations are more infectious Ablation of both N331 and N343 glycosylation at RBD drastically reduced infectivity Ten mutations such as N234Q, L452R, A475V, V483A was markedly resistant to some mAbs Summary 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. |
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