Publication

Broad host range of SARS-CoV-2 and the molecular basis for SARS-CoV-2 binding to cat ACE2

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Last modified
  • 07/08/2025
Type of Material
Authors
    Lili Wu, Chinese Academy of SciencesQian Chen, Chinese Academy of SciencesKefang Liu, Chinese Academy of SciencesJia Wang, Tsinghua UniversityPengcheng Han, Emory UniversityYanfang Zhang, Chinese Academy of SciencesYu Hu, Chinese Academy of SciencesYumin Meng, Chinese Academy of SciencesXiaoqian Pan, Univ Chinese Acad SciChengpeng Qiao, Chinese Academy of SciencesSiyu Tian, Chinese Academy of SciencesPei Du, Chinese Academy of SciencesHao Song, Chinese Academy of SciencesWeifeng Shi, Shandong First Medical University & Shandong Academy of Medical SciencesJianxun Qi, Chinese Academy of SciencesHong-Wei Wang, Tsinghua UniversityJinghua Yan, Chinese Academy of SciencesGeorge F Gao, Chinese Academy of SciencesQihui Wang, Chinese Academy of Sciences
Language
  • English
Date
  • 2020-09-29
Publisher
  • SPRINGERNATURE
Publication Version
Copyright Statement
  • © The Author(s) 2020
License
Final Published Version (URL)
Title of Journal or Parent Work
Volume
  • 6
Issue
  • 1
Start Page
  • 68
End Page
  • 68
Grant/Funding Information
  • This work was supported by the Ministry of Science and Technology of the People’s Republic of China (2020YFC0840801 and 2020YFC0845900), the Chinese Academy of Sciences (XDB29010202) and the National Natural Science Foundation of China (81922044 and 81973228). Q.W. is supported by the Youth Innovation Promotion Association CAS (2018119). G.F.G is supported by the foundation of the NSFC Innovative Research Group (81621091).
Supplemental Material (URL)
Abstract
  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of the recent pandemic COVID-19, is reported to have originated from bats, with its intermediate host unknown to date. Here, we screened 26 animal counterparts of the human ACE2 (hACE2), the receptor for SARS-CoV-2 and SARS-CoV, and found that the ACE2s from various species, including pets, domestic animals and multiple wild animals, could bind to SARS-CoV-2 receptor binding domain (RBD) and facilitate the transduction of SARS-CoV-2 pseudovirus. Comparing to SARS-CoV-2, SARS-CoV seems to have a slightly wider range in choosing its receptor. We further resolved the cryo-electron microscopy (cryo-EM) structure of the cat ACE2 (cACE2) in complex with the SARS-CoV-2 RBD at a resolution of 3 Å, revealing similar binding mode as hACE2 to the SARS-CoV-2 RBD. These results shed light on pursuing the intermediate host of SARS-CoV-2 and highlight the necessity of monitoring susceptible hosts to prevent further outbreaks.
Author Notes
Keywords
Research Categories
  • Engineering, Biomedical

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