Structural basis of SARS-CoV-2 and its variants binding to intermediate horseshoe bat ACE2.
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.
Keywords
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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