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Controlling the SARS-CoV-2 spike glycoprotein conformation

Nature structural & molecular biology, 2020-10, Vol.27 (10), p.925-933 [Peer Reviewed Journal]

ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-0479-4 ;PMID: 32699321

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Title:
Controlling the SARS-CoV-2 spike glycoprotein conformation
Author: Henderson, Rory ; Edwards, Robert J ; Mansouri, Katayoun ; Janowska, Katarzyna ; Stalls, Victoria ; Gobeil, Sophie M C ; Kopp, Megan ; Li, Dapeng ; Parks, Rob ; Hsu, Allen L ; Borgnia, Mario J ; Haynes, Barton F ; Acharya, Priyamvada
Subjects: Binding Sites ; Cryoelectron Microscopy ; Microscopy, Electron - methods ; Models, Molecular ; Mutation ; Protein Conformation ; Protein Domains ; Protein Subunits - chemistry ; Spike Glycoprotein, Coronavirus - chemistry ; Spike Glycoprotein, Coronavirus - genetics ; Spike Glycoprotein, Coronavirus - metabolism
Is Part Of: Nature structural & molecular biology, 2020-10, Vol.27 (10), p.925-933
Description: 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.
Publisher: United States
Language: English
Identifier: ISSN: 1545-9993
EISSN: 1545-9985
DOI: 10.1038/s41594-020-0479-4
PMID: 32699321
Source: MEDLINE
ProQuest Central

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Controlling the SARS-CoV-2 spike glycoprotein conformation

ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-0479-4 ;PMID: 32699321

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