Qianqian Li, Jiajing Wu, J. 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
Cell, 2020
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.
Cited by 490 publications.
Field of study: Biology