7XA7

Crystal structure of SARS-CoV-2 receptor-binding domain in complex with intermediate horseshoe bat ACE2

Summary for 7XA7

• Entry DOI: 10.2210/pdb7xa7/pdb
• Descriptor: Angiotensin-converting enzyme, Spike protein S1, ZINC ION, ... (5 entities in total)
• Functional Keywords: complex, viral protein
• Biological source: Rhinolophus affinis (Intermediate horseshoe bat); More
• Total number of polymer chains: 8
• Total formula weight: 380493.53

Authors

Tang, L.F.,Zhang, D.,Han, P.,Qi, J.X. (deposition date: 2022-03-17, release date: 2022-12-21, Last modification date: 2024-11-06)

Primary citation

Tang, L.,Zhang, D.,Han, P.,Kang, X.,Zheng, A.,Xu, Z.,Zhao, X.,Wang, V.Y.,Qi, J.,Wang, Q.,Liu, K.,Gao, G.F.
Structural basis of SARS-CoV-2 and its variants binding to intermediate horseshoe bat ACE2.
Int J Biol Sci, 18:4658-4668, 2022

PubMed 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 () 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.

PubMed: 35874946
DOI: 10.7150/ijbs.73640

Experimental method

X-RAY DIFFRACTION (3.31 Å)