Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2

被引：354

作者：

Han, Pengcheng ^{[1
,2
]}

Li, Linjie ^{[1
,3
]}

Liu, Sheng ^{[4
]}

Wang, Qisheng ^{[5
]}

Zhang, Di ^{[1
,6
]}

Xu, Zepeng ^{[1
,6
]}

Han, Pu ^{[1
]}

Li, Xiaomei ^{[7
]}

Peng, Qi ^{[1
]}

Su, Chao ^{[8
]}

Huang, Baihan ^{[1
]}

Li, Dedong ^{[1
]}

Zhang, Rong ^{[1
]}

Tian, Mingxiong ^{[9
]}

Fu, Lutang ^{[4
]}

Gao, Yuanzhu ^{[4
]}

Zhao, Xin ^{[1
]}

Liu, Kefang ^{[1
]}

Qi, Jianxun ^{[1
,3
]}

Gao, George F. ^{[1
,3
]}

Wang, Peiyi ^{[4
]}

机构：

[1] Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China

[2] Southeast Univ, Zhongda Hosp, Sch Med, Nanjing 210009, Peoples R China

[3] Univ Chinese Acad Sci, Beijing 100049, Peoples R China

[4] Southern Univ Sci & Technol, Cryo EM Ctr, Dept Biol, Shenzhen 518055, Peoples R China

[5] Chinese Acad Sci, Shanghai Adv Res Inst, Shanghai Synchrotron Radiat Facil, Shanghai 201204, Peoples R China

[6] Univ Macau, Fac Hlth Sci, Macau 999078, Peoples R China

[7] Shanxi Acad Adv Res & Innovat, Cryo EM Ctr, Taiyuan 030032, Peoples R China

[8] City Univ Hong Kong, Dept Biomed Sci, Hong Kong 999077, Peoples R China

[9] Shanxi Univ, Coll Life Sci, Taiyuan 03006, Peoples R China

来源：

CELL | 2022年 / 185卷 / 04期

基金：

国家重点研发计划;

关键词：

VARIANT B.1.1.7; ESCAPE; NEUTRALIZATION; EPIDEMIOLOGY; MOLPROBITY; FEATURES;

D O I：

10.1016/j.cell.2022.01.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The coronavirus disease 2019 (COVID-19) pandemic continues worldwide with many variants arising, some of which are variants of concern (VOCs). A recent VOC, omicron (B.1.1.529), which obtains a large number of mutations in the receptor-binding domain (RBD) of the spike protein, has risen to intense scientific and public attention. Here, we studied the binding properties between the human receptor ACE2 (hACE2) and the VOC RBDs and resolved the crystal and cryoelectron microscopy structures of the omicron RBD-hACE2 complex as well as the crystal structure of the delta RBD-hACE2 complex. We found that, unlike alpha, beta, and gamma, omicron RBD binds to hACE2 at a similar affinity to that of the prototype RBD, which might be due to compensation of multiple mutations for both immune escape and transmissibility. The complex structures of omicron RBD-hACE2 and delta RBD-hACE2 reveal the structural basis of how RBD-specific mutations bind to hACE2.

引用

页码：630 / +

页数：22

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