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Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2
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...
Autores principales: | , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8733278/ https://www.ncbi.nlm.nih.gov/pubmed/35093192 http://dx.doi.org/10.1016/j.cell.2022.01.001 |
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author | Han, Pengcheng Li, Linjie Liu, Sheng Wang, Qisheng Zhang, Di Xu, Zepeng Han, Pu Li, Xiaomei Peng, Qi Su, Chao Huang, Baihan Li, Dedong Zhang, Rong Tian, Mingxiong Fu, Lutang Gao, Yuanzhu Zhao, Xin Liu, Kefang Qi, Jianxun Gao, George F. Wang, Peiyi |
author_facet | Han, Pengcheng Li, Linjie Liu, Sheng Wang, Qisheng Zhang, Di Xu, Zepeng Han, Pu Li, Xiaomei Peng, Qi Su, Chao Huang, Baihan Li, Dedong Zhang, Rong Tian, Mingxiong Fu, Lutang Gao, Yuanzhu Zhao, Xin Liu, Kefang Qi, Jianxun Gao, George F. Wang, Peiyi |
author_sort | Han, Pengcheng |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-8733278 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-87332782022-01-06 Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 Han, Pengcheng Li, Linjie Liu, Sheng Wang, Qisheng Zhang, Di Xu, Zepeng Han, Pu Li, Xiaomei Peng, Qi Su, Chao Huang, Baihan Li, Dedong Zhang, Rong Tian, Mingxiong Fu, Lutang Gao, Yuanzhu Zhao, Xin Liu, Kefang Qi, Jianxun Gao, George F. Wang, Peiyi Cell Article 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. Elsevier Inc. 2022-02-17 2022-01-06 /pmc/articles/PMC8733278/ /pubmed/35093192 http://dx.doi.org/10.1016/j.cell.2022.01.001 Text en © 2022 Elsevier Inc. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Han, Pengcheng Li, Linjie Liu, Sheng Wang, Qisheng Zhang, Di Xu, Zepeng Han, Pu Li, Xiaomei Peng, Qi Su, Chao Huang, Baihan Li, Dedong Zhang, Rong Tian, Mingxiong Fu, Lutang Gao, Yuanzhu Zhao, Xin Liu, Kefang Qi, Jianxun Gao, George F. Wang, Peiyi Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 |
title | Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 |
title_full | Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 |
title_fullStr | Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 |
title_full_unstemmed | Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 |
title_short | Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 |
title_sort | receptor binding and complex structures of human ace2 to spike rbd from omicron and delta sars-cov-2 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8733278/ https://www.ncbi.nlm.nih.gov/pubmed/35093192 http://dx.doi.org/10.1016/j.cell.2022.01.001 |
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