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Molecular insights into receptor binding of recent emerging SARS-CoV-2 variants

Medicine and Health

Molecular insights into receptor binding of recent emerging SARS-CoV-2 variants

P. Han, C. Su, et al.

Exciting new research led by Pengcheng Han and colleagues reveals that multiple SARS-CoV-2 variants enhance their ability to bind to human cells, potentially increasing infection rates. This study not only identifies crucial molecular interactions but also presents soluble hACE2 proteins as a promising barrier against these variants, opening avenues for innovative therapeutic strategies.

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Playback language: English
Abstract
Multiple SARS-CoV-2 variants of concern (VOCs) have been emerging and some have been linked to an increase in case numbers globally. This study examined several VOCs (Alpha, Beta, Gamma, Mink-Y453F, Mink-F486L, and Mink-N501T) and found 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 identified key residues facilitating changes in hACE2 binding affinity. Soluble hACE2 protein efficiently prevented most variants' pseudoviruses. These findings provide important molecular information for developing novel therapeutic and prophylactic agents.
Publisher
NATURE COMMUNICATIONS
Published On
Oct 26, 2021
Authors
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
Tags
SARS-CoV-2
variants
hACE2
binding affinity
therapeutics
molecular interactions
pseudoviruses

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