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-Structure paper
Title | Broad host range of SARS-CoV-2 and the molecular basis for SARS-CoV-2 binding to cat ACE2. |
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Journal, issue, pages | Cell Discov, Vol. 6, Page 68, Year 2020 |
Publish date | Sep 29, 2020 |
Authors | Lili Wu / Qian Chen / Kefang Liu / Jia Wang / Pengcheng Han / Yanfang Zhang / Yu Hu / Yumin Meng / Xiaoqian Pan / Chengpeng Qiao / Siyu Tian / Pei Du / Hao Song / Weifeng Shi / Jianxun Qi / Hong-Wei Wang / Jinghua Yan / George Fu Gao / Qihui Wang / |
PubMed 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. ...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. |
External links | Cell Discov / PubMed:33020722 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.0 Å |
Structure data | EMDB-30305, PDB-7c8d: |
Chemicals | ChemComp-ZN: |
Source |
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Keywords | HYDROLASE/VIRAL PROTEIN / ACE2 / SARS-CoV-2 / Cryo-EM / complex / PROTEIN BINDING / HYDROLASE-VIRAL PROTEIN complex |