Cross-species recognition of SARS-CoV-2 to bat ACE2.

Proceedings of the National Academy of Sciences of the United States of America
Kefang LiuGeorge Fu Gao

Abstract

The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has emerged as a major threat to global health. Although varied SARS-CoV-2-related coronaviruses have been isolated from bats and SARS-CoV-2 may infect bat, the structural basis for SARS-CoV-2 to utilize the human receptor counterpart bat angiotensin-converting enzyme 2 (bACE2) for virus infection remains less understood. Here, we report that the SARS-CoV-2 spike protein receptor binding domain (RBD) could bind to bACE2 from Rhinolophus macrotis (bACE2-Rm) with substantially lower affinity compared with that to the human ACE2 (hACE2), and its infectivity to host cells expressing bACE2-Rm was confirmed with pseudotyped SARS-CoV-2 virus and SARS-CoV-2 wild virus. The structure of the SARS-CoV-2 RBD with the bACE2-Rm complex was determined, revealing a binding mode similar to that of hACE2. The analysis of binding details between SARS-CoV-2 RBD and bACE2-Rm revealed that the interacting network involving Y41 and E42 of bACE2-Rm showed substantial differences with that to hACE2. Bats have extensive species diversity and the residues for RBD binding in bACE2 receptor varied substantially among different bat species...Continue Reading

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Apr 4, 2021·Animals : an Open Access Journal From MDPI·John T HancockAlexander Greenhough
Jun 17, 2021·Physical Chemistry Chemical Physics : PCCP·Yongjian ZangShengli Zhang

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Datasets Mentioned

BETA
ADN93471.1

Methods Mentioned

BETA
glycosylation
surface
flow cytometry
chips
chip
Assay

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