tetano
Editor, Senior Moderator
Cell Discov
. 2020 Sep 29;6:68.
doi: 10.1038/s41421-020-00210-9. eCollection 2020.
Broad host range of SARS-CoV-2 and the molecular basis for SARS-CoV-2 binding to cat ACE2
Lili Wu[SUP] #[/SUP][SUP] 1 2 [/SUP], Qian Chen[SUP] #[/SUP][SUP] 1 3 [/SUP], Kefang Liu[SUP] #[/SUP][SUP] 2 4 5 [/SUP], Jia Wang[SUP] #[/SUP][SUP] 6 [/SUP], Pengcheng Han[SUP] 7 [/SUP], Yanfang Zhang[SUP] 4 8 [/SUP], Yu Hu[SUP] 4 9 [/SUP], Yumin Meng[SUP] 4 [/SUP], Xiaoqian Pan[SUP] 2 4 [/SUP], Chengpeng Qiao[SUP] 1 [/SUP], Siyu Tian[SUP] 1 2 [/SUP], Pei Du[SUP] 1 [/SUP], Hao Song[SUP] 10 [/SUP], Weifeng Shi[SUP] 11 [/SUP], Jianxun Qi[SUP] 4 12 [/SUP], Hong-Wei Wang[SUP] 6 [/SUP], Jinghua Yan[SUP] 1 12 [/SUP], George Fu Gao[SUP] 4 [/SUP], Qihui Wang[SUP] 1 3 12 [/SUP]
Affiliations
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 ?, 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.
Keywords: Cryoelectron microscopy; Molecular biology.
. 2020 Sep 29;6:68.
doi: 10.1038/s41421-020-00210-9. eCollection 2020.
Broad host range of SARS-CoV-2 and the molecular basis for SARS-CoV-2 binding to cat ACE2
Lili Wu[SUP] #[/SUP][SUP] 1 2 [/SUP], Qian Chen[SUP] #[/SUP][SUP] 1 3 [/SUP], Kefang Liu[SUP] #[/SUP][SUP] 2 4 5 [/SUP], Jia Wang[SUP] #[/SUP][SUP] 6 [/SUP], Pengcheng Han[SUP] 7 [/SUP], Yanfang Zhang[SUP] 4 8 [/SUP], Yu Hu[SUP] 4 9 [/SUP], Yumin Meng[SUP] 4 [/SUP], Xiaoqian Pan[SUP] 2 4 [/SUP], Chengpeng Qiao[SUP] 1 [/SUP], Siyu Tian[SUP] 1 2 [/SUP], Pei Du[SUP] 1 [/SUP], Hao Song[SUP] 10 [/SUP], Weifeng Shi[SUP] 11 [/SUP], Jianxun Qi[SUP] 4 12 [/SUP], Hong-Wei Wang[SUP] 6 [/SUP], Jinghua Yan[SUP] 1 12 [/SUP], George Fu Gao[SUP] 4 [/SUP], Qihui Wang[SUP] 1 3 12 [/SUP]
Affiliations
- PMID: 33020722
- PMCID: PMC7526519
- DOI: 10.1038/s41421-020-00210-9
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 ?, 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.
Keywords: Cryoelectron microscopy; Molecular biology.