8WLO
Cryo-EM structure of SARS-CoV-2 prototype spike protein in complex with hippopotamus ACE2
This is a non-PDB format compatible entry.
Summary for 8WLO
Entry DOI | 10.2210/pdb8wlo/pdb |
EMDB information | 37626 |
Descriptor | Spike glycoprotein, Angiotensin-converting enzyme, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | complex, viral protein/hydrolase, viral protein-hydrolase complex |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) More |
Total number of polymer chains | 4 |
Total formula weight | 485380.89 |
Authors | Han, P.,Yang, R.R.,Li, S.H. (deposition date: 2023-09-30, release date: 2024-03-27, Last modification date: 2024-10-30) |
Primary citation | Yang, R.,Han, P.,Han, P.,Li, D.,Zhao, R.,Niu, S.,Liu, K.,Li, S.,Tian, W.X.,Gao, G.F. Molecular basis of hippopotamus ACE2 binding to SARS-CoV-2. J.Virol., 98:e0045124-e0045124, 2024 Cited by PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a wide range of hosts, including hippopotami, which are semi-aquatic mammals and phylogenetically closely related to Cetacea. In this study, we characterized the binding properties of hippopotamus angiotensin-converting enzyme 2 (hiACE2) to the spike (S) protein receptor binding domains (RBDs) of the SARS-CoV-2 prototype (PT) and variants of concern (VOCs). Furthermore, the cryo-electron microscopy (cryo-EM) structure of the SARS-CoV-2 PT S protein complexed with hiACE2 was resolved. Structural and mutational analyses revealed that L30 and F83, which are specific to hiACE2, played a crucial role in the hiACE2/SARS-CoV-2 RBD interaction. In addition, comparative and structural analysis of ACE2 orthologs suggested that the cetaceans may have the potential to be infected by SARS-CoV-2. These results provide crucial molecular insights into the susceptibility of hippopotami to SARS-CoV-2 and suggest the potential risk of SARS-CoV-2 VOCs spillover and the necessity for surveillance. PubMed: 38591877DOI: 10.1128/jvi.00451-24 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.62 Å) |
Structure validation
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