|Title||Controlling the SARS-CoV-2 spike glycoprotein conformation.|
|Journal, issue, pages||Nat Struct Mol Biol, Vol. 27, Issue 10, Page 925-933, Year 2020|
|Publish date||Jul 22, 2020|
|Authors||Rory Henderson / Robert J Edwards / Katayoun Mansouri / Katarzyna Janowska / Victoria Stalls / Sophie M C Gobeil / Megan Kopp / Dapeng Li / Rob Parks / Allen L Hsu / Mario J Borgnia / Barton F Haynes / Priyamvada Acharya /|
|PubMed Abstract||The coronavirus (CoV) spike (S) protein, involved in viral-host cell fusion, is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The ...The coronavirus (CoV) spike (S) protein, involved in viral-host cell fusion, is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The highly flexible S-protein, with its mobile domains, presents a moving target to the immune system. Here, to better understand S-protein mobility, we implemented a structure-based vector analysis of available β-CoV S-protein structures. Despite an overall similarity in domain organization, we found that S-proteins from different β-CoVs display distinct configurations. Based on this analysis, we developed two soluble ectodomain constructs for the SARS-CoV-2 S-protein, in which the highly immunogenic and mobile receptor binding domain (RBD) is either locked in the all-RBDs 'down' position or adopts 'up' state conformations more readily than the wild-type S-protein. These results demonstrate that the conformation of the S-protein can be controlled via rational design and can provide a framework for the development of engineered CoV S-proteins for vaccine applications.|
|External links||Nat Struct Mol Biol / PubMed:32699321|
|Methods||EM (single particle)|
|Resolution||2.7 - 12.06 Å|
|Keywords||Binding Sites / Cryoelectron Microscopy / Microscopy, Electron / Models, Molecular / Mutation / Protein Conformation / Protein Domains / Protein Subunits / Spike Glycoprotein, Coronavirus / spike protein, SARS-CoV-2 / VIRAL PROTEIN / Trimer|
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