OmniVira

Literature detail

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

Lili Wu1,2 Qian Chen1,3 Kefang Liu2,4,5 Jia Wang6 Pengcheng Han7 Yanfang Zhang4,8 Yu Hu4,9 Yumin Meng4 Xiaoqian Pan2,4 Chengpeng Qiao1 Siyu Tian1,2 Pei Du1 Hao Song10 Weifeng Shi11 Jianxun Qi4,12 Hong-Wei Wang6 Jinghua Yan1,12 George Fu Gao4 Qihui Wang1,3,12
Affiliations 12 institutions
  1. CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101 China.
  2. University of Chinese Academy of Sciences, Beijing, 100049 China.
  3. Institute of Physical Science and Information, Anhui University, Hefei, Anhui 230039 China.
  4. CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101 China.
  5. Faculty of Health Sciences, University of Macau, Macau, SAR China.
  6. Ministry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center of Biological Structures, School of Life Sciences, Tsinghua University, Beijing, 100084 China.
  7. Department of biomedical engineering, Emory University, Atlanta, GA 10033 USA.
  8. Laboratory of Protein Engineering and Vaccines,Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, 300308 China.
  9. School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026 China.
  10. Research Network of Immunity and Health (RNIH), Beijing Institute of Life Science, Chinese Academy of Sciences, Beijing, 100101 China.
  11. Key Laboratory of Etiology and Epidemiology of Emerging Infectious Diseases in Universities of Shandong, Shandong First Medical University & Shandong Academy of Medical Sciences, Taian, Shandong 27100 China.
  12. Savaid Medical School, University of Chinese Academy of Sciences, Beijing, 100049 China.
PMID 33020722 2020 Cell Discov eng epublish
PubMed DOI Browse context

Article

Publication summary

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.

Cryoelectron microscopy Molecular biology

Structured evidence records

Evidence records

4 total
Host Range Experiment 2 records
Host Range Experiment Extraction confidence 0.90
Key finding

ACE2 proteins from multiple animal species, including pets, domestic and wild animals, were able to mediate SARS-CoV-2 pseudovirus entry, indicating broad host susceptibility.

Virus
SARS-CoV-2
Host
Metazoa
Location
Not specified
Supporting text

We screened 26 animal counterparts of the human ACE2 (hACE2)... 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.

Method
ACE2 binding assay; pseudovirus transduction
Experimental system
pseudovirus assay
Host Range Experiment Extraction confidence 0.90
Key finding

Structural analysis showed that cat ACE2 binds to SARS-CoV-2 receptor binding domain similarly to human ACE2, supporting potential susceptibility in cats.

Virus
SARS-CoV-2
Location
Not specified
Supporting text

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.

Method
cryo-electron microscopy; receptor binding analysis
Experimental system
cryo-EM structural assay
Receptor Usage 2 records
Receptor Usage Extraction confidence 0.95
Key finding

SARS-CoV-2 receptor binding domain binds cat ACE2 in a similar mode as human ACE2 as shown by cryo-EM structure.

Virus
SARS-CoV-2
Location
Not specified
Supporting text

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.

Method
cryo-electron microscopy; structural analysis
Receptors
cat ACE2
Receptor Usage Extraction confidence 0.95
Key finding

ACE2 proteins from multiple animal species can bind SARS-CoV-2 receptor binding domain and enable pseudovirus entry, supporting cross-species receptor usage.

Virus
SARS-CoV-2
Host
Not specified
Location
Not specified
Supporting text

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.

Method
binding assay; pseudovirus assay
Receptors
ACE2