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Structural basis of SARS-CoV-2 and its variants binding to intermediate horseshoe bat ACE2.
Tang, Lingfeng; Zhang, Di; Han, Pu; Kang, Xinrui; Zheng, Anqi; Xu, Zepeng; Zhao, Xin; Wang, Vivien Ya-Fan; Qi, Jianxun; Wang, Qihui; Liu, Kefang; Gao, George F.
  • Tang L; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Zhang D; Faculty of Health Sciences, University of Macau, Macau SAR 999078, China.
  • Han P; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Kang X; Faculty of Health Sciences, University of Macau, Macau SAR 999078, China.
  • Zheng A; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Xu Z; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Zhao X; University of Chinese Academy of Sciences, Beijing 100049, China.
  • Wang VY; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Qi J; University of Chinese Academy of Sciences, Beijing 100049, China.
  • Wang Q; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Liu K; Faculty of Health Sciences, University of Macau, Macau SAR 999078, China.
  • Gao GF; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Int J Biol Sci ; 18(12): 4658-4668, 2022.
Article in English | MEDLINE | ID: covidwho-2025287
ABSTRACT
Coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has caused a global pandemic. Intermediate horseshoe bats (Rhinolophus affinis) are hosts of RaTG13, the second most phylogenetically related viruses to SARS-CoV-2. We report the binding between intermediate horseshoe bat ACE2 (bACE2-Ra) and SARS-CoV-2 receptor-binding domain (RBD), supporting the pseudotyped SARS-CoV-2 viral infection. A 3.3 Å resolution crystal structure of the bACE2-Ra/SARS-CoV-2 RBD complex was determined. The interaction networks of Patch 1 showed differences in R34 and E35 of bACE2-Ra compared to hACE2 and big-eared horseshoe bat ACE2 (bACE2-Rm). The E35K substitution, existing in other species, significantly enhanced the binding affinity owing to its electrostatic attraction with E484 of SARS-CoV-2 RBD. Furthermore, bACE2-Ra showed extensive support for the SARS-CoV-2 variants. These results broaden our knowledge of the ACE2/RBD interaction mechanism and emphasize the importance of continued surveillance of intermediate horseshoe bats to prevent spillover risk.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Chiroptera / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 Type of study: Prognostic study Topics: Variants Limits: Animals Language: English Journal: Int J Biol Sci Journal subject: Biology Year: 2022 Document Type: Article Affiliation country: Ijbs.73640

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Chiroptera / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 Type of study: Prognostic study Topics: Variants Limits: Animals Language: English Journal: Int J Biol Sci Journal subject: Biology Year: 2022 Document Type: Article Affiliation country: Ijbs.73640