The viruses used in this article from BrainVTA are in the table below
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VSV-S |
PV-SARS-CoV-2-S-VSV-ΔG-GFP |
Pengcheng Han, Chao Su, Yanfang Zhang, Chongzhi Bai, Anqi Zheng, Chengpeng Qiao, Qing Wang, Sheng Niu, Qian Chen, Yuqin Zhang, Weiwei Li, Hanyi Liao, Jing Li, Zengyuan Zhang, Heecheol Cho, Mengsu Yang, Xiaoyu Rong, Yu Hu, Niu Huang, Jinghua Yan, Qihui Wang, Xin Zhao, George Fu Gao, Jianxun Qi
Pub Date: 2021-10-20,
DOI: 10.1038/s41467-021-26401-w,
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Multiple SARS-CoV-2 variants of concern (VOCs) have been emerging and some have been linked to an increase in case numbers globally. However, there is yet a lack of understanding of the molecular basis for the interactions between the human ACE2 (hACE2) receptor and these VOCs. Here we examined several VOCs including Alpha, Beta, and Gamma, and demonstrate that five variants receptor-binding domain (RBD) increased binding affinity for hACE2, and four variants pseudoviruses increased entry into susceptible cells. Crystal structures of hACE2-RBD complexes help identify the key residues facilitating changes in hACE2 binding affinity. Additionally, soluble hACE2 protein efficiently prevent most of the variants pseudoviruses. Our findings provide important molecular information and may help the development of novel therapeutic and prophylactic agents targeting these emerging mutants.
Figure 1. Entry of SARS-CoV-2 variant pseudoviruses into Huh7 cells.
In this study, the authors examined six different SARS-CoV-2 RBD variants, including Alpha, Beta, Gamma, Mink-Y453F, Mink-F486L, and Mink-N501T. These data will provide a useful information to develop antiviral drugs against SARS-CoV-2
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