SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects
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 uncl...
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| Vydané v: | Nature structural & molecular biology Ročník 27; číslo 8; s. 763 - 767 |
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| Hlavní autori: | , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
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United States
Nature Publishing Group
01.08.2020
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| ISSN: | 1545-9993, 1545-9985, 1545-9985 |
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| 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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| AbstractList | 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. 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.Cryo-EM and functional analyses of furin-cleaved spike from SARS-CoV-2 and the closely related spike from bat virus RaTG13 reveal differences in protein stability and binding to human receptor ACE2. 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.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. |
| Author | Xu, Pengqi Roustan, Chloë Wrobel, Antoni G Rosenthal, Peter B Skehel, John J Gamblin, Steven J Benton, Donald J Martin, Stephen R |
| Author_xml | – sequence: 1 givenname: Antoni G orcidid: 0000-0002-6680-5587 surname: Wrobel fullname: Wrobel, Antoni G email: antoni.wrobel@crick.ac.uk organization: Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK. antoni.wrobel@crick.ac.uk – sequence: 2 givenname: Donald J orcidid: 0000-0001-6748-9339 surname: Benton fullname: Benton, Donald J email: donald.benton@crick.ac.uk organization: Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK. donald.benton@crick.ac.uk – sequence: 3 givenname: Pengqi surname: Xu fullname: Xu, Pengqi organization: Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, Guangdong, China – sequence: 4 givenname: Chloë surname: Roustan fullname: Roustan, Chloë organization: Structural Biology Science Technology Platform, Francis Crick Institute, London, UK – sequence: 5 givenname: Stephen R surname: Martin fullname: Martin, Stephen R organization: Structural Biology Science Technology Platform, Francis Crick Institute, London, UK – sequence: 6 givenname: Peter B orcidid: 0000-0002-0387-2862 surname: Rosenthal fullname: Rosenthal, Peter B organization: Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, London, UK – sequence: 7 givenname: John J surname: Skehel fullname: Skehel, John J organization: Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK – sequence: 8 givenname: Steven J orcidid: 0000-0001-5331-639X surname: Gamblin fullname: Gamblin, Steven J email: steven.gamblin@crick.ac.uk organization: Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK. steven.gamblin@crick.ac.uk |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32647346$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | The Author(s), under exclusive licence to Springer Nature America, Inc. 2020. |
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| References | 32848232 - Nat Struct Mol Biol. 2020 Oct;27(10):1001. doi: 10.1038/s41594-020-0509-2. |
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| Snippet | 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... |
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| SubjectTerms | ACE2 Angiotensin-Converting Enzyme 2 Animals Betacoronavirus - genetics Betacoronavirus - metabolism Betacoronavirus - ultrastructure Binding Binding Sites Chiroptera - virology Cleavage Coronavirus Infections - virology COVID-19 Cryoelectron Microscopy Evolution, Molecular Furin Furin - chemistry Gene Expression Glycoproteins HEK293 Cells Host-Pathogen Interactions - genetics Humans Models, Molecular Pandemics Peptidyl-Dipeptidase A - chemistry Peptidyl-Dipeptidase A - genetics Peptidyl-Dipeptidase A - metabolism Pneumonia, Viral - virology Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Interaction Domains and Motifs Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - metabolism Protein Stability Proteins Proteolysis Receptors Receptors, Virus - chemistry Receptors, Virus - genetics Receptors, Virus - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 Spike glycoprotein Spike Glycoprotein, Coronavirus - chemistry Spike Glycoprotein, Coronavirus - genetics Spike Glycoprotein, Coronavirus - metabolism Stability Structural Homology, Protein Viruses |
| Title | SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects |
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