OmniVira

Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species.

Kefang Liu1 Xiaoqian Pan2,3 Linjie Li2,3 Feng Yu4 Anqi Zheng1 Pei Du1 Pengcheng Han2,5 Yumin Meng1 Yanfang Zhang2,6 Lili Wu1 Qian Chen2,7 Chunli Song7 Yunfei Jia2,8 Sheng Niu2,8 Dan Lu1 Chengpeng Qiao1 Zhihai Chen9 Dongli Ma10 Xiaopeng Ma10 Shuguang Tan1 Xin Zhao1 Jianxun Qi2,11 George F Gao2,12 Qihui Wang2,13
Affiliations 13 institutions
  1. CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  2. CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China
  3. University of the Chinese Academy of Sciences, Beijing 100049, China.
  4. Shanghai Synchrotron Radiation Facility, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201204, China.
  5. Department of Biomedical Engineering, Emory University, Atlanta, GA 10033, USA.
  6. Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
  7. Institute of Physical Science and Information, Anhui University, Hefei 230039, China.
  8. College of Veterinary Medicine, Shanxi Agricultural University, Jinzhong 030801, China.
  9. Center of Infectious Disease, Beijing Ditan Hospital, Capital Medical University, 100015 Beijing, China.
  10. Shenzhen Children's Hospital, Shenzhen 518036, China.
  11. University of the Chinese Academy of Sciences, Beijing 100049, China. Electronic address: [email protected].
  12. University of the Chinese Academy of Sciences, Beijing 100049, China. Electronic address: [email protected].
  13. University of the Chinese Academy of Sciences, Beijing 100049, China. Electronic address: [email protected].
PMID34139177 DOI10.1016/j.cell.2021.05.031 Year2021 Journal Cell Languageeng Statusppublish

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been spreading worldwide, causing a global pandemic. Bat-origin RaTG13 is currently the most phylogenetically related virus. Here we obtained the complex structure of the RaTG13 receptor binding domain (RBD) with human ACE2 (hACE2) and evaluated binding of RaTG13 RBD to 24 additional ACE2 orthologs. By substituting residues in the RaTG13 RBD with their counterparts in the SARS-CoV-2 RBD, we found that residue 501, the major position found in variants of concern (VOCs) 501Y.V1/V2/V3, plays a key role in determining the potential host range of RaTG13. We also found that SARS-CoV-2 could induce strong cross-reactive antibodies to RaTG13 and identified a SARS-CoV-2 monoclonal antibody (mAb), CB6, that could cross-neutralize RaTG13 pseudovirus. These results elucidate the receptor binding and host adaption mechanisms of RaTG13 and emphasize the importance of continuous surveillance of coronaviruses (CoVs) carried by animal reservoirs to prevent another spillover of CoVs.

ACE2 54 COVID-19 467 intermediate horseshoe bat 0 RaTG13 3 RBD 13 SARS-CoV-2 550 Amino Acid Sequence 128 Angiotensin-Converting Enzyme 2 177 Animals 1948 Antibodies, Monoclonal 26 Binding Sites 89 Chiroptera 371 COVID-19 425 Host Specificity 132 Humans 1440 Phylogeny 805 Protein Binding 193 Receptors, Virus 204 SARS-CoV-2 453 Sequence Alignment 51 ACE2 protein, human 87

Evidence records

0 total

No structured evidence records are linked to this article.