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Cited by 435

The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.

Controlling the SARS-CoV-2 spike glycoprotein conformation

Open access
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·2020·Nature Structural & Molecular Biology

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 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. The SARS-CoV-2 spike glycoprotein is flexible, and its receptor-binding domain (RBD) fluctuates between up or down conformations. Mutations engineered into the spike ectodomain either lock the RBD in the down state or make it adopt the up conformation more readily.

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Metadata

Authors
Henderson, R., Edwards, R. J., Mansouri, K., Janowska, K., Stalls, V., Gobeil, S. M. C., Kopp, M., Li, D., Parks, R., Hsu, A. L., Borgnia, M. J., Haynes, B. F., & Acharya, P.
Venue
Nature Structural & Molecular Biology
Published
2020-07-22
Volume
27
Issue
10
Pages
925-933
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W3045149055
Cited by
435
References
52
FWCI
10.11
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Controlling the SARS-CoV-2 spike glycoprotein conformation. https://app.cochat.ai/papers/10.1038/s41594-020-0479-4
The paper
Henderson, R., Edwards, R. J., Mansouri, K., Janowska, K., Stalls, V., Gobeil, S. M. C., Kopp, M., Li, D., Parks, R., Hsu, A. L., Borgnia, M. J., Haynes, B. F., & Acharya, P. (2020). Controlling the SARS-CoV-2 spike glycoprotein conformation. Nature Structural & Molecular Biology. https://doi.org/10.1038/s41594-020-0479-4

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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