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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 DOI10.2210/pdb8wlo/pdb
EMDB information37626
DescriptorSpike 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 Keywordscomplex, viral protein/hydrolase, viral protein-hydrolase complex
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
More
Total number of polymer chains4
Total formula weight485380.89
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 citationYang, 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: 38591877
DOI: 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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