8YFT

Cryo-EM structure of SARS-CoV-2 alpha variant spike protein in complex with raccoon dog ACE2 (local refinement)

Summary for 8YFT

• Entry DOI: 10.2210/pdb8yft/pdb
• EMDB information: 39229
• Descriptor: Angiotensin-converting enzyme, Spike protein S1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: sars-cov-2, alpha, rbd, raccoon dog, ace2, viral protein-hydrolase complex, viral protein/hydrolase
• Biological source: Nyctereutes procyonoides (raccoon dog); More
• Total number of polymer chains: 2
• Total formula weight: 97755.71

Authors

Li, L.J.,Luo, C.L.,Qi, J.X.,Gao, G.F. (deposition date: 2024-02-25, release date: 2024-10-23, Last modification date: 2025-04-30)

Primary citation

Luo, C.,Li, L.,Gu, Y.,Zhang, H.,Xu, Z.,Sun, J.,Shi, K.,Ma, S.,Tian, W.X.,Liu, K.,Gao, G.F.
Receptor binding and structural basis of raccoon dog ACE2 binding to SARS-CoV-2 prototype and its variants.
Plos Pathog., 20:e1012713-e1012713, 2024

PubMed Abstract: Raccoon dog was proposed as a potential host of SARS-CoV-2, but no evidence support such a notion. In our study, we investigated the binding affinities of raccoon dog ACE2 (rdACE2) to the spike (S) protein receptor binding domain (RBD) of SARS-CoV-2 prototype (PT) and its variants. It revealed that the binding affinities of RBD from SARS-CoV-2 variants were generally lower than that of the PT RBD. Through structural and functional analyses, we found amino acids H34 and M82 play pivotal roles in maintaining the binding affinity of ACE2 to different SARS-CoV-2 sub-variants. These results suggest that raccoon dogs exhibit lower susceptibility to SARS-CoV-2 compared to those animal species with a high prevalence of SARS-CoV-2 transmission.

PubMed: 39637248
DOI: 10.1371/journal.ppat.1012713

Experimental method

ELECTRON MICROSCOPY (3.16 Å)