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-Structure paper
タイトル | SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 27, Issue 8, Page 763-767, Year 2020 |
掲載日 | 2020年7月9日 |
著者 | Antoni G Wrobel / Donald J Benton / Pengqi Xu / Chloë Roustan / Stephen R Martin / Peter B Rosenthal / John J Skehel / Steven J Gamblin / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Struct Mol Biol / PubMed:32647346 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.6 - 6.8 Å |
構造データ | EMDB-11203, PDB-6zge: EMDB-11204, PDB-6zgf: EMDB-11205, PDB-6zgg: EMDB-11206, PDB-6zgh: EMDB-11207, PDB-6zgi: |
化合物 | ChemComp-NAG: ChemComp-HOH: |
由来 |
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キーワード | VIRAL PROTEIN / SARS-CoV-2 / Spike / Virus Glycoprotein / Coronavirus |