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SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects.
Wrobel, Antoni G; Benton, Donald J; Xu, Pengqi; Roustan, Chloë; Martin, Stephen R; Rosenthal, Peter B; Skehel, John J; Gamblin, Steven J.
  • Wrobel AG; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK. antoni.wrobel@crick.ac.uk.
  • Benton DJ; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK. donald.benton@crick.ac.uk.
  • Xu P; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK.
  • Roustan C; Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, Guangdong, China.
  • Martin SR; Structural Biology Science Technology Platform, Francis Crick Institute, London, UK.
  • Rosenthal PB; Structural Biology Science Technology Platform, Francis Crick Institute, London, UK.
  • Skehel JJ; Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, London, UK.
  • Gamblin SJ; Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK.
Nat Struct Mol Biol ; 27(8): 763-767, 2020 08.
Article in English | MEDLINE | ID: covidwho-640223
ABSTRACT
SARS-CoV-2 is thought to have emerged from bats, possibly via a secondary host. Here, we investigate the relationship of spike (S) glycoprotein from SARS-CoV-2 with the S protein of a closely related bat virus, RaTG13. We determined cryo-EM structures for RaTG13 S and for both furin-cleaved and uncleaved SARS-CoV-2 S; we compared these with recently reported structures for uncleaved SARS-CoV-2 S. We also biochemically characterized their relative stabilities and affinities for the SARS-CoV-2 receptor ACE2. Although the overall structures of human and bat virus S proteins are similar, there are key differences in their properties, including a more stable precleavage form of human S and about 1,000-fold tighter binding of SARS-CoV-2 to human receptor. These observations suggest that cleavage at the furin-cleavage site decreases the overall stability of SARS-CoV-2 S and facilitates the adoption of the open conformation that is required for S to bind to the ACE2 receptor.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Receptors, Virus / Peptidyl-Dipeptidase A / Host-Pathogen Interactions / Spike Glycoprotein, Coronavirus / Betacoronavirus Type of study: Experimental Studies / Observational study / Prognostic study Topics: Variants Language: English Journal: Nat Struct Mol Biol Journal subject: Molecular Biology Year: 2020 Document Type: Article Affiliation country: S41594-020-0468-7

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Receptors, Virus / Peptidyl-Dipeptidase A / Host-Pathogen Interactions / Spike Glycoprotein, Coronavirus / Betacoronavirus Type of study: Experimental Studies / Observational study / Prognostic study Topics: Variants Language: English Journal: Nat Struct Mol Biol Journal subject: Molecular Biology Year: 2020 Document Type: Article Affiliation country: S41594-020-0468-7