Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2.

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Tytuł:: Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2.
Autorzy:: Wrobel AG; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK. .
Benton DJ; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK. .
Xu P; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK.; Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, Guangdong, China.
Calder LJ; Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, NW1 1AT, London, UK.
Borg A; Structural Biology Science Technology Platform, Francis Crick Institute, NW1 1AT, London, UK.
Roustan C; Structural Biology Science Technology Platform, Francis Crick Institute, NW1 1AT, London, UK.
Martin SR; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK.
Rosenthal PB; Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, NW1 1AT, London, UK.
Skehel JJ; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK.
Gamblin SJ; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK. .
Źródło:: Nature communications [Nat Commun] 2021 Feb 05; Vol. 12 (1), pp. 837. Date of Electronic Publication: 2021 Feb 05.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: [London] : Nature Pub. Group
MeSH Terms:: Evolution, Molecular*
COVID-19/*prevention & control
SARS-CoV-2/*genetics
Spike Glycoprotein, Coronavirus/*genetics
Angiotensin-Converting Enzyme 2/metabolism ; Animals ; Binding, Competitive ; COVID-19/epidemiology ; COVID-19/virology ; Cryoelectron Microscopy ; Humans ; Models, Molecular ; Pandemics ; Pangolins/virology ; Protein Binding ; Protein Domains ; SARS-CoV-2/metabolism ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/metabolism
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Grant Information:: FC001143 United Kingdom CRUK_ Cancer Research UK; FC001078 United Kingdom WT_ Wellcome Trust; FC001143 United Kingdom MRC_ Medical Research Council; FC001078 United Kingdom CRUK_ Cancer Research UK; United Kingdom WT_ Wellcome Trust; FC001143 United Kingdom WT_ Wellcome Trust; FC001078 United Kingdom MRC_ Medical Research Council
Substance Nomenclature:: 0 (Spike Glycoprotein, Coronavirus)
0 (spike protein, SARS-CoV-2)
EC 3.4.17.23 (ACE2 protein, human)
EC 3.4.17.23 (Angiotensin-Converting Enzyme 2)
Entry Date(s):: Date Created: 20210206 Date Completed: 20210222 Latest Revision: 20210222
Update Code:: 20240104
PubMed Central ID:: PMC7864994
DOI:: 10.1038/s41467-021-21006-9
PMID:: 33547281
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Coronaviruses of bats and pangolins have been implicated in the origin and evolution of the pandemic SARS-CoV-2. We show that spikes from Guangdong Pangolin-CoVs, closely related to SARS-CoV-2, bind strongly to human and pangolin ACE2 receptors. We also report the cryo-EM structure of a Pangolin-CoV spike protein and show it adopts a fully-closed conformation and that, aside from the Receptor-Binding Domain, it resembles the spike of a bat coronavirus RaTG13 more than that of SARS-CoV-2.

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